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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP.jpg" alt="H2A.Zac Antibody ChIP Grade" /></p>
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<p><small><strong> Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 1 million HeLaS3 cells using the “Auto Histone ChIP-seq” kit (Cat. No. AB-Auto02-A100) on the SX-8G IP-Star automated system. A titration of the antibody consisting of 1, 2, 5 and 10 μg per ChIP experiment was analysed. IgG (2 μg/ IP) was used as negative IP control. QPCR was performed using primers specific for the promoters of the ACTB and EIF4A2 genes, used as positive control targets and for the coding region of the MYT1 gene, used as a negative control target. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA). These results confirm the observation that acetylation of H2A.Z is present at active promoters. </small></p>
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<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-A.jpg" alt="H2A.Zac Antibody for ChIP" /></p>
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<p><small><strong> Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP was performed with 1 μg of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) on sheared chromatin from 1 million HeLaS3 cells using the “iDeal ChIP-seq” kit (Cat. No. AB-001-0024). IgG (2 μg/IP) was used as a negative IP control. The IP’d DNA was analysed by QPCR as described above (figure 1A). The IP’d DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 1 shows the peak distribution along the complete sequence and a 600 kb region of the X-chromosome (figure 1B and C) and in 100 kb regions surrounding the EIF4A2, ACTB and GAPDH genes (figure 1D, E and F). These results clearly show an enrichment of the H2A.Z acetylation at the promoters of active genes. </small></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" alt="H2A.Zac Antibody for ChIP-seq" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-C.jpg" alt="H2A.Zac Antibody for ChIP-seq assay" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-D.jpg" alt="H2A.Zac Antibody validated in ChIP-seq" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-E.jpg" alt="H2A.Zac Antibody ChIP-seq Grade " /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-F.jpg" alt="H2A.Zac Antibody for ChIP-seq" /></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_ELISA.jpg" alt="H2A.Zac Antibody ELISA validation" /></p>
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<p><small><strong> Figure 3. Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (Cat. No. pAb-173-050), crude serum and flow through in antigen coated wells. The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:8,800. </small></p>
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<div class="row">
<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_DB.jpg" alt="H2A.Zac Antibody validated in Dot Blot" /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br /> A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173- 050) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest. </small></p>
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<div class="row">
<div class="small-5 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_IF.jpg" alt="H2A.Zac Antibody validated in Immunofluorescence " /></p>
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<div class="small-7 columns">
<p><small><strong> Figure 5. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br /> HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. pAb-173-050) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right. </small></p>
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<td>0.5 μg/ChIP</td>
<td>Fig 1, 2</td>
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<td>1:5,000</td>
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<td>Fig 6</td>
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<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP.jpg" alt="H2A.Zac Antibody ChIP Grade" /></p>
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<p><small><strong> Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 1 million HeLaS3 cells using the “Auto Histone ChIP-seq” kit (Cat. No. AB-Auto02-A100) on the SX-8G IP-Star automated system. A titration of the antibody consisting of 1, 2, 5 and 10 μg per ChIP experiment was analysed. IgG (2 μg/ IP) was used as negative IP control. QPCR was performed using primers specific for the promoters of the ACTB and EIF4A2 genes, used as positive control targets and for the coding region of the MYT1 gene, used as a negative control target. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA). These results confirm the observation that acetylation of H2A.Z is present at active promoters. </small></p>
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<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-A.jpg" alt="H2A.Zac Antibody for ChIP" /></p>
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<p><small><strong> Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP was performed with 1 μg of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) on sheared chromatin from 1 million HeLaS3 cells using the “iDeal ChIP-seq” kit (Cat. No. AB-001-0024). IgG (2 μg/IP) was used as a negative IP control. The IP’d DNA was analysed by QPCR as described above (figure 1A). The IP’d DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 1 shows the peak distribution along the complete sequence and a 600 kb region of the X-chromosome (figure 1B and C) and in 100 kb regions surrounding the EIF4A2, ACTB and GAPDH genes (figure 1D, E and F). These results clearly show an enrichment of the H2A.Z acetylation at the promoters of active genes. </small></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" alt="H2A.Zac Antibody for ChIP-seq" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-C.jpg" alt="H2A.Zac Antibody for ChIP-seq assay" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-D.jpg" alt="H2A.Zac Antibody validated in ChIP-seq" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-E.jpg" alt="H2A.Zac Antibody ChIP-seq Grade " /></p>
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<p><small><strong> Figure 3. Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (Cat. No. pAb-173-050), crude serum and flow through in antigen coated wells. The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:8,800. </small></p>
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<div class="row">
<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_DB.jpg" alt="H2A.Zac Antibody validated in Dot Blot" /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br /> A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173- 050) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest. </small></p>
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<div class="row">
<div class="small-5 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_IF.jpg" alt="H2A.Zac Antibody validated in Immunofluorescence " /></p>
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<div class="small-7 columns">
<p><small><strong> Figure 5. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br /> HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. pAb-173-050) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right. </small></p>
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<td>ChIP/ChIP-seq <sup>*</sup></td>
<td>0.5 μg/ChIP</td>
<td>Fig 1, 2</td>
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<tr>
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<td>1:5,000</td>
<td>Fig 3</td>
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<td>1:20,000</td>
<td>Fig 4</td>
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<td>1:1,000</td>
<td>Fig 5</td>
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<td>Fig 6</td>
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<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<p><strong>Figure 3. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (cat. No. C15410173). The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:265,000.</p>
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<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
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<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<p><strong>Figure 3. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (cat. No. C15410173). The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:265,000.</p>
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<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
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<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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<p><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
<p><sup>HeLa cells transfected with a Cas9 expression vector (left) or untransfected cells (right) were fixed in methanol at -20°C, permeabilized with acetone at -20°C and blocked with PBS containing 2% BSA. The cells were stained with the Cas9 C-terminal antibody (Cat. No. C15200229) diluted 1:400, followed by incubation with an anti-mouse secondary antibody coupled to AF488. The bottom images show counter-staining of the nuclei with Hoechst 33342.</sup></p>
<h5><sup>Check our selection of antibodies validated in IF.</sup></h5>',
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'description' => '<p>Histones are the main protein components of chromatin involved in the compaction of DNA into nucleosomes, the basic units of chromatin. A <strong>nucleosome</strong> consists of one pair of each of the core histones (<strong>H2A</strong>, <strong>H2B</strong>, <strong>H3</strong> and <strong>H4</strong>) forming an octameric structure wrapped by 146 base pairs of DNA. The different nucleosomes are linked by the linker histone<strong> H1, </strong>allowing for further condensation of chromatin.</p>
<p>The core histones have a globular structure with large unstructured N-terminal tails protruding from the nucleosome. They can undergo to multiple post-translational modifications (PTM), mainly at the N-terminal tails. These <strong>post-translational modifications </strong>include methylation, acetylation, phosphorylation, ubiquitinylation, citrullination, sumoylation, deamination and crotonylation. The most well characterized PTMs are <strong>methylation,</strong> <strong>acetylation and phosphorylation</strong>. Histone methylation occurs mainly on lysine (K) residues, which can be mono-, di- or tri-methylated, and on arginines (R), which can be mono-methylated and symmetrically or asymmetrically di-methylated. Histone acetylation occurs on lysines and histone phosphorylation mainly on serines (S), threonines (T) and tyrosines (Y).</p>
<p>The PTMs of the different residues are involved in numerous processes such as DNA repair, DNA replication and chromosome condensation. They influence the chromatin organization and can be positively or negatively associated with gene expression. Trimethylation of H3K4, H3K36 and H3K79, and lysine acetylation generally result in an open chromatin configuration (figure below) and are therefore associated with <strong>euchromatin</strong> and gene activation. Trimethylation of H3K9, K3K27 and H4K20, on the other hand, is enriched in <strong>heterochromatin </strong>and associated with gene silencing. The combination of different histone modifications is called the "<strong>histone code</strong>”, analogous to the genetic code.</p>
<p><img src="https://www.diagenode.com/img/categories/antibodies/histone-marks-illustration.png" /></p>
<p>Diagenode is proud to offer a large range of antibodies against histones and histone modifications. Our antibodies are highly specific and have been validated in many applications, including <strong>ChIP</strong> and <strong>ChIP-seq</strong>.</p>
<p>Diagenode’s collection includes antibodies recognizing:</p>
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<li><strong>Histone H1 variants</strong></li>
<li><strong>Histone H2A, H2A variants and histone H2A</strong> <strong>modifications</strong> (serine phosphorylation, lysine acetylation, lysine ubiquitinylation)</li>
<li><strong>Histone H2B and H2B</strong> <strong>modifications </strong>(serine phosphorylation, lysine acetylation)</li>
<li><strong>Histone H3 and H3 modifications </strong>(lysine methylation (mono-, di- and tri-methylated), lysine acetylation, serine phosphorylation, threonine phosphorylation, arginine methylation (mono-methylated, symmetrically and asymmetrically di-methylated))</li>
<li><strong>Histone H4 and H4 modifications (</strong>lysine methylation (mono-, di- and tri-methylated), lysine acetylation, arginine methylation (mono-methylated and symmetrically di-methylated), serine phosphorylation )</li>
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<p><span style="font-weight: 400;"><strong>HDAC's HAT's, HMT's and other</strong> <strong>enzymes</strong> which modify histones can be found in the category <a href="../categories/chromatin-modifying-proteins-histone-transferase">Histone modifying enzymes</a><br /></span></p>
<p><span style="font-weight: 400;"> Diagenode’s highly validated antibodies:</span></p>
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<li><span style="font-weight: 400;"> Highly sensitive and specific</span></li>
<li><span style="font-weight: 400;"> Cost-effective (requires less antibody per reaction)</span></li>
<li><span style="font-weight: 400;"> Batch-specific data is available on the website</span></li>
<li><span style="font-weight: 400;"> Expert technical support</span></li>
<li><span style="font-weight: 400;"> Sample sizes available</span></li>
<li><span style="font-weight: 400;"> 100% satisfaction guarantee</span></li>
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<p><span style="font-weight: 400;">Diagenode provides leading solutions for epigenetic research. Because ChIP-seq is a widely-used technique, we validate our antibodies in ChIP and ChIP-seq experiments (in addition to conventional methods like Western blot, Dot blot, ELISA, and immunofluorescence) to provide the highest quality antibody. We standardize our validation and production to guarantee high product quality without technical bias. Diagenode guarantees ChIP-seq grade antibody performance under our suggested conditions.</span></p>
<div class="row">
<div class="small-12 medium-9 large-9 columns">
<p><strong>ChIP-seq profile</strong> of active (H3K4me3 and H3K36me3) and inactive (H3K27me3) marks using Diagenode antibodies.</p>
<img src="https://www.diagenode.com/img/categories/antibodies/chip-seq-grade-antibodies.png" /></div>
<div class="small-12 medium-3 large-3 columns">
<p><small> ChIP was performed on sheared chromatin from 100,000 K562 cells using iDeal ChIP-seq kit for Histones (cat. No. C01010051) with 1 µg of the Diagenode antibodies against H3K27me3 (cat. No. C15410195) and H3K4me3 (cat. No. C15410003), and 0.5 µg of the antibody against H3K36me3 (cat. No. C15410192). The IP'd DNA was subsequently analysed on an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. The figure shows the signal distribution along the complete sequence of human chromosome 3, a zoomin to a 10 Mb region and a further zoomin to a 1.5 Mb region. </small></p>
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<p>Diagenode’s highly validated antibodies:</p>
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<p>Diagenode has partnered with leading epigenetics experts and numerous epigenetics consortiums to bring to you a validated and comprehensive collection of epigenetic antibodies. As an expert in epigenetics, we are committed to offering highly-specific antibodies validated for ChIP/ChIP-seq and many other applications. All batch-specific validation data is available on our website.<br /><a href="../categories/antibodies">Read about our expertise in antibody production</a>.</p>
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<li><strong>Focused</strong> - Diagenode's selection of antibodies is exclusively dedicated for epigenetic research. <a title="See the full collection." href="../categories/all-antibodies">See the full collection.</a></li>
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<li><strong>Classified</strong> based on level of validation for flexibility of application</li>
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<p>Existing sample sizes are listed below. We will soon expand our collection. Are you looking for a sample size of another antibody? Just <a href="mailto:agnieszka.zelisko@diagenode.com?Subject=Sample%20Size%20Request" target="_top">Contact us</a>.</p>',
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'description' => '<p><span style="font-weight: 400;">All Diagenode’s antibodies are listed below. Please, use our Quick search field to find the antibody of interest by target name, application, purity.</span></p>
<p><span style="font-weight: 400;">Diagenode’s highly validated antibodies:</span></p>
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<li>Cost-effective (requires less antibody per reaction)</li>
<li>Batch-specific data is available on the website</li>
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<p><br />Chromatin immunoprecipitation (<b>ChIP</b>) is a technique to study the associations of proteins with the specific genomic regions in intact cells. One of the most important steps of this protocol is the immunoprecipitation of targeted protein using the antibody specifically recognizing it. The quality of antibodies used in ChIP is essential for the success of the experiment. Diagenode offers extensively validated ChIP-grade antibodies, confirmed for their specificity, and high level of performance in ChIP. Each batch is validated, and batch-specific data are available on the website.</p>
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<p><strong>ChIP results</strong> obtained with the antibody directed against H3K4me3 (Cat. No. <a href="../p/h3k4me3-polyclonal-antibody-premium-50-ug-50-ul">C15410003</a>). </p>
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<div class="small-12 medium-6 large-6 columns"><img src="https://www.diagenode.com/img/product/antibodies/C15410003-fig1-ChIP.jpg" alt="" width="400" height="315" /> </div>
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<p>Our aim at Diagenode is to offer the largest collection of highly specific <strong>ChIP-grade antibodies</strong>. We add new antibodies monthly. Find your ChIP-grade antibody in the list below and check more information about tested applications, extensive validation data, and product information.</p>',
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'authors' => 'Bieluszewski T. et al.',
'description' => '<p>Nucleosomal acetyltransferase of H4 (NuA4) is an essential transcriptional coactivator in eukaryotes, but remains poorly characterized in plants. Here, we describe Arabidopsis homologs of the NuA4 scaffold proteins Enhancer of Polycomb-Like 1 (AtEPL1) and Esa1-Associated Factor 1 (AtEAF1). Loss of AtEAF1 results in inhibition of growth and chloroplast development. These effects are stronger in the Atepl1 mutant and are further enhanced by loss of Golden2-Like (GLK) transcription factors, suggesting that NuA4 activates nuclear plastid genes alongside GLK. We demonstrate that AtEPL1 is necessary for nucleosomal acetylation of histones H4 and H2A.Z by NuA4 in vitro. These chromatin marks are diminished genome-wide in Atepl1, while another active chromatin mark, H3K9 acetylation (H3K9ac), is locally enhanced. Expression of many chloroplast-related genes depends on NuA4, as they are downregulated with loss of H4ac and H2A.Zac. Finally, we demonstrate that NuA4 promotes H2A.Z deposition and by doing so prevents spurious activation of stress response genes.</p>',
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'name' => 'Neonatal exposure to hyperoxia leads to persistent disturbances in pulmonary histone signatures associated with NOS3 and STAT3 in a mouse model.',
'authors' => 'Chao CM, van den Bruck R, Lork S, Merkle J, Krampen L, Weil PP, Aydin M, Bellusci S, Jenke AC, Postberg J',
'description' => '<p>Background: Early pulmonary oxygen exposure is one of the most important factors implicated in the development of bronchopulmonary dysplasia (BPD). Methods: Here, we analyzed short- and long-term effects of neonatal hyperoxia on NOS3 and STAT3 expression and corresponding epigenetic signatures using a hyperoxia-based mouse model of BPD. Results: Early hyperoxia exposure led to a significant increase in NOS3 (median fold change × 2.37, IQR 1.54-3.68) and STAT3 (median fold change × 2.83, IQR 2.21-3.88) mRNA levels in pulmonary endothelial cells with corresponding changes in histone modification patterns such as H2aZac and H3K9ac hyperacetylation at the respective gene loci. No complete restoration in histone signatures at these loci was observed, and responsivity to later hyperoxia was altered in mouse lungs. In vitro, histone signatures in human aortic endothelial cells (HAEC) remained altered for several weeks after an initial long-term exposure to trichostatin A. This was associated with a substantial increase in baseline eNOS (median 27.2, IQR 22.3-35.6) and STAT3α (median 5.8, IQR 4.8-7.3) mRNA levels with a subsequent significant reduction in eNOS expression upon exposure to hypoxia. Conclusions: Early hyperoxia induced permanent changes in histones signatures at the NOS3 and STAT3 gene locus might partly explain the altered vascular response patterns in children with BPD.</p>',
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'pmid' => 'http://www.pubmed.gov/29581793',
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'authors' => 'Postberg J, Kanders M, Forcob S, Willems R, Orth V, Hensel KO, Weil PP, Wirth S, Jenke AC',
'description' => 'BACKGROUND: An adverse intrauterine environment leads to permanent physiological changes including vascular tone regulation, potentially influencing the risk for adult vascular diseases. We therefore aimed to monitor responsive NOS3 expression in human umbilical artery endothelial cells (HUAEC) and to study the underlying epigenetic signatures involved in its regulation. RESULTS: NOS3 and STAT3 mRNA levels were elevated in HUAEC of patients who suffered from placental insufficiency. 5-hydroxymethylcytosine, H3K9ac and Histone 2A (H2A).Zac at the NOS3 transcription start site directly correlated with NOS3 mRNA levels. Concomitantly, we observed entangled histone acetylation patterns and NOS3 response upon hypoxic conditions in vitro. Knock-down of either NOS3 or STAT3 by RNAi provided evidence for a functional NOS3/STAT3 relationship. Moreover, we recognized massive turnover of Stat3 at a discrete binding site in the NOS3 promoter. Interestingly, induced hyperacetylation resulted in short-termed increase of NOS3 mRNA followed by deferred decrease indicating that NOS3 expression could become self-attenuated by co-expressed intronic 27 nt-ncRNA. Reporter assay results and phylogenetic analyses enabled us to propose a novel model for STAT3-3'-UTR targeting by this 27-nt-ncRNA. CONCLUSIONS: An adverse intrauterine environment leads to adaptive changes of NOS3 expression. Apparently, a rapid NOS3 self-limiting response upon ectopic triggers co-exists with longer termed expression changes in response to placental insufficiency involving differential epigenetic signatures. Their persistence might contribute to impaired vascular endothelial response and consequently increase the risk of cardiovascular disease later in life.',
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'name' => 'H2A.Zac Antibody',
'description' => '<p><span>Polyclonal antibody raised in rabbit against histone <strong>H2A.Z acetylated at lysines 4, 7 and 11,</strong> using a KLH-conjugated synthetic peptide.</span></p>',
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'info1' => '<div class="row">
<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP.jpg" /></center></div>
<div class="small-6 columns">
<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<div class="extra-spaced"></div>
<div class="row">
<div class="small-12 columns"><center>A.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-A.jpg" width="700" /></center><center>B.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" width="700" /></center><center>C.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-C.jpg" width="700" /></center>
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<center>D.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-D.jpg" width="700" /></center></div>
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<div class="row">
<div class="small-12 columns">
<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<div class="small-6 columns">
<p><strong>Figure 3. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (cat. No. C15410173). The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:265,000.</p>
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<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
<p></p>
<p></p>
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<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_WB.jpg" /></center></div>
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<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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<p><small><strong> Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 1 million HeLaS3 cells using the “Auto Histone ChIP-seq” kit (Cat. No. AB-Auto02-A100) on the SX-8G IP-Star automated system. A titration of the antibody consisting of 1, 2, 5 and 10 μg per ChIP experiment was analysed. IgG (2 μg/ IP) was used as negative IP control. QPCR was performed using primers specific for the promoters of the ACTB and EIF4A2 genes, used as positive control targets and for the coding region of the MYT1 gene, used as a negative control target. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA). These results confirm the observation that acetylation of H2A.Z is present at active promoters. </small></p>
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<p><small><strong> Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP was performed with 1 μg of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) on sheared chromatin from 1 million HeLaS3 cells using the “iDeal ChIP-seq” kit (Cat. No. AB-001-0024). IgG (2 μg/IP) was used as a negative IP control. The IP’d DNA was analysed by QPCR as described above (figure 1A). The IP’d DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 1 shows the peak distribution along the complete sequence and a 600 kb region of the X-chromosome (figure 1B and C) and in 100 kb regions surrounding the EIF4A2, ACTB and GAPDH genes (figure 1D, E and F). These results clearly show an enrichment of the H2A.Z acetylation at the promoters of active genes. </small></p>
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<p><small><strong> Figure 3. Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (Cat. No. pAb-173-050), crude serum and flow through in antigen coated wells. The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:8,800. </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_DB.jpg" alt="H2A.Zac Antibody validated in Dot Blot" /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br /> A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173- 050) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest. </small></p>
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<div class="small-5 columns">
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<p><small><strong> Figure 5. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br /> HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. pAb-173-050) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right. </small></p>
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<span class="success label" style="">C15410173</span>
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<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<p><strong>Figure 3. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (cat. No. C15410173). The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:265,000.</p>
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<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
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<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<div class="small-12 columns"><center>A.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-A.jpg" width="700" /></center><center>B.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" width="700" /></center><center>C.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-C.jpg" width="700" /></center>
<div class="extra-spaced"></div>
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<div class="extra-spaced"></div>
<center>D.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-D.jpg" width="700" /></center></div>
</div>
<div class="row">
<div class="small-12 columns">
<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<div class="row">
<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_ELISA.jpg" /></center></div>
<div class="small-6 columns">
<p><strong>Figure 3. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (cat. No. C15410173). The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:265,000.</p>
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<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_DB.jpg" width="220" /></center></div>
<div class="small-8 columns">
<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
<p></p>
<p></p>
<p></p>
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<div class="row">
<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_WB.jpg" /></center></div>
<div class="small-8 columns">
<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<div class="extra-spaced"></div>
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<div class="small-12 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_IF.jpg" width="700" /></center></div>
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<div class="small-12 columns">
<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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'name' => 'CpG signalling, H2A.Z/H3 acetylation and microRNA-mediated deferred self-attenuation orchestrate foetal NOS3 expression.',
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'description' => 'BACKGROUND: An adverse intrauterine environment leads to permanent physiological changes including vascular tone regulation, potentially influencing the risk for adult vascular diseases. We therefore aimed to monitor responsive NOS3 expression in human umbilical artery endothelial cells (HUAEC) and to study the underlying epigenetic signatures involved in its regulation. RESULTS: NOS3 and STAT3 mRNA levels were elevated in HUAEC of patients who suffered from placental insufficiency. 5-hydroxymethylcytosine, H3K9ac and Histone 2A (H2A).Zac at the NOS3 transcription start site directly correlated with NOS3 mRNA levels. Concomitantly, we observed entangled histone acetylation patterns and NOS3 response upon hypoxic conditions in vitro. Knock-down of either NOS3 or STAT3 by RNAi provided evidence for a functional NOS3/STAT3 relationship. Moreover, we recognized massive turnover of Stat3 at a discrete binding site in the NOS3 promoter. Interestingly, induced hyperacetylation resulted in short-termed increase of NOS3 mRNA followed by deferred decrease indicating that NOS3 expression could become self-attenuated by co-expressed intronic 27 nt-ncRNA. Reporter assay results and phylogenetic analyses enabled us to propose a novel model for STAT3-3'-UTR targeting by this 27-nt-ncRNA. CONCLUSIONS: An adverse intrauterine environment leads to adaptive changes of NOS3 expression. Apparently, a rapid NOS3 self-limiting response upon ectopic triggers co-exists with longer termed expression changes in response to placental insufficiency involving differential epigenetic signatures. Their persistence might contribute to impaired vascular endothelial response and consequently increase the risk of cardiovascular disease later in life.',
'date' => '2015-01-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/25699114',
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP.jpg" alt="H2A.Zac Antibody ChIP Grade" /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 1 million HeLaS3 cells using the “Auto Histone ChIP-seq” kit (Cat. No. AB-Auto02-A100) on the SX-8G IP-Star automated system. A titration of the antibody consisting of 1, 2, 5 and 10 μg per ChIP experiment was analysed. IgG (2 μg/ IP) was used as negative IP control. QPCR was performed using primers specific for the promoters of the ACTB and EIF4A2 genes, used as positive control targets and for the coding region of the MYT1 gene, used as a negative control target. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA). These results confirm the observation that acetylation of H2A.Z is present at active promoters. </small></p>
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<p><small><strong> Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP was performed with 1 μg of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) on sheared chromatin from 1 million HeLaS3 cells using the “iDeal ChIP-seq” kit (Cat. No. AB-001-0024). IgG (2 μg/IP) was used as a negative IP control. The IP’d DNA was analysed by QPCR as described above (figure 1A). The IP’d DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 1 shows the peak distribution along the complete sequence and a 600 kb region of the X-chromosome (figure 1B and C) and in 100 kb regions surrounding the EIF4A2, ACTB and GAPDH genes (figure 1D, E and F). These results clearly show an enrichment of the H2A.Z acetylation at the promoters of active genes. </small></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" alt="H2A.Zac Antibody for ChIP-seq" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-C.jpg" alt="H2A.Zac Antibody for ChIP-seq assay" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-D.jpg" alt="H2A.Zac Antibody validated in ChIP-seq" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-E.jpg" alt="H2A.Zac Antibody ChIP-seq Grade " /></p>
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<p><small><strong> Figure 3. Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (Cat. No. pAb-173-050), crude serum and flow through in antigen coated wells. The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:8,800. </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_DB.jpg" alt="H2A.Zac Antibody validated in Dot Blot" /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br /> A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173- 050) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest. </small></p>
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<div class="small-5 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_IF.jpg" alt="H2A.Zac Antibody validated in Immunofluorescence " /></p>
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<p><small><strong> Figure 5. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br /> HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. pAb-173-050) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right. </small></p>
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'description' => 'Histones are the main constituents of the protein part of chromosomes of eukaryotic cells. They are rich in the amino acids arginine and lysine and have been greatly conserved during evolution. Histones pack the DNA into tight masses of chromatin. Two core histones of each class H2A, H2B, H3 and H4 assemble and are wrapped by 146 base pairs of DNA to form one octameric nucleosome. Histone tails undergo numerous post-translational modifications, which either directly or indirectly alter chromatin structure to facilitate transcriptional activation or repression or other nuclear processes. In addition to the genetic code, combinations of the different histone modifications reveal the so-called “histone code”. Histone methylation and demethylation is dynamically regulated by respectively histone methyl transferases and histone demethylases. Acetylation of the histone H2A variant H2A.Z is associated with the promoters of active genes.',
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<p><small><sup>*</sup> Please note that the optimal antibody amount per IP should be determined by the end-user. We recommend testing 0.5-5 μg per IP.</small></p>',
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<p><small><strong> Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 1 million HeLaS3 cells using the “Auto Histone ChIP-seq” kit (Cat. No. AB-Auto02-A100) on the SX-8G IP-Star automated system. A titration of the antibody consisting of 1, 2, 5 and 10 μg per ChIP experiment was analysed. IgG (2 μg/ IP) was used as negative IP control. QPCR was performed using primers specific for the promoters of the ACTB and EIF4A2 genes, used as positive control targets and for the coding region of the MYT1 gene, used as a negative control target. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA). These results confirm the observation that acetylation of H2A.Z is present at active promoters. </small></p>
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<p><small><strong> Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP was performed with 1 μg of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) on sheared chromatin from 1 million HeLaS3 cells using the “iDeal ChIP-seq” kit (Cat. No. AB-001-0024). IgG (2 μg/IP) was used as a negative IP control. The IP’d DNA was analysed by QPCR as described above (figure 1A). The IP’d DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 1 shows the peak distribution along the complete sequence and a 600 kb region of the X-chromosome (figure 1B and C) and in 100 kb regions surrounding the EIF4A2, ACTB and GAPDH genes (figure 1D, E and F). These results clearly show an enrichment of the H2A.Z acetylation at the promoters of active genes. </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-E.jpg" alt="H2A.Zac Antibody ChIP-seq Grade " /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-F.jpg" alt="H2A.Zac Antibody for ChIP-seq" /></p>
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<p><small><strong> Figure 3. Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (Cat. No. pAb-173-050), crude serum and flow through in antigen coated wells. The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:8,800. </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_DB.jpg" alt="H2A.Zac Antibody validated in Dot Blot" /></p>
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<p><small><strong> Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br /> A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173- 050) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest. </small></p>
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<p><small><strong> Figure 5. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br /> HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. pAb-173-050) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right. </small></p>
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'description' => 'Histones are the main constituents of the protein part of chromosomes of eukaryotic cells. They are rich in the amino acids arginine and lysine and have been greatly conserved during evolution. Histones pack the DNA into tight masses of chromatin. Two core histones of each class H2A, H2B, H3 and H4 assemble and are wrapped by 146 base pairs of DNA to form one octameric nucleosome. Histone tails undergo numerous post-translational modifications, which either directly or indirectly alter chromatin structure to facilitate transcriptional activation or repression or other nuclear processes. In addition to the genetic code, combinations of the different histone modifications reveal the so-called “histone code”. Histone methylation and demethylation is dynamically regulated by respectively histone methyl transferases and histone demethylases. Acetylation of the histone H2A variant H2A.Z is associated with the promoters of active genes.',
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<th>References</th>
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<td>ChIP/ChIP-seq <sup>*</sup></td>
<td>0.5 μg/ChIP</td>
<td>Fig 1, 2</td>
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<tr>
<td>ELISA</td>
<td>1:5,000</td>
<td>Fig 3</td>
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<tr>
<td>Dot Blotting</td>
<td>1:20,000</td>
<td>Fig 4</td>
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<tr>
<td>Western Blotting</td>
<td>1:1,000</td>
<td>Fig 5</td>
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<tr>
<td>Immunofluorescence</td>
<td>1:500</td>
<td>Fig 6</td>
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<p><small><sup>*</sup> Please note that the optimal antibody amount per IP should be determined by the end-user. We recommend testing 0.5-5 μg per IP.</small></p>',
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'description' => '<p><span>Polyclonal antibody raised in rabbit against histone <strong>H2A.Z acetylated at lysines 4, 7 and 11,</strong> using a KLH-conjugated synthetic peptide.</span></p>',
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<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP.jpg" /></center></div>
<div class="small-6 columns">
<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<div class="extra-spaced"></div>
<div class="row">
<div class="small-12 columns"><center>A.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-A.jpg" width="700" /></center><center>B.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" width="700" /></center><center>C.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-C.jpg" width="700" /></center>
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</div>
<div class="row">
<div class="small-12 columns">
<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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</div>
<div class="extra-spaced"></div>
<div class="row">
<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_ELISA.jpg" /></center></div>
<div class="small-6 columns">
<p><strong>Figure 3. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (cat. No. C15410173). The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:265,000.</p>
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<div class="small-8 columns">
<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
<p></p>
<p></p>
<p></p>
</div>
</div>
<div class="row">
<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_WB.jpg" /></center></div>
<div class="small-8 columns">
<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP.jpg" /></center></div>
<div class="small-6 columns">
<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<div class="small-12 columns"><center>A.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-A.jpg" width="700" /></center><center>B.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" width="700" /></center><center>C.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-C.jpg" width="700" /></center>
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<div class="small-12 columns">
<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<div class="small-6 columns">
<p><strong>Figure 3. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (cat. No. C15410173). The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:265,000.</p>
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<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
<p></p>
<p></p>
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<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_WB.jpg" /></center></div>
<div class="small-8 columns">
<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<div class="extra-spaced"></div>
<div class="row">
<div class="small-12 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_IF.jpg" width="700" /></center></div>
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<div class="row">
<div class="small-12 columns">
<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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<p>Diagenode offers huge selection of highly sensitive antibodies validated in IF.</p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15200229-IF.jpg" alt="" height="245" width="256" /></p>
<p><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
<p><sup>HeLa cells transfected with a Cas9 expression vector (left) or untransfected cells (right) were fixed in methanol at -20°C, permeabilized with acetone at -20°C and blocked with PBS containing 2% BSA. The cells were stained with the Cas9 C-terminal antibody (Cat. No. C15200229) diluted 1:400, followed by incubation with an anti-mouse secondary antibody coupled to AF488. The bottom images show counter-staining of the nuclei with Hoechst 33342.</sup></p>
<h5><sup>Check our selection of antibodies validated in IF.</sup></h5>',
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'description' => '<p>Histones are the main protein components of chromatin involved in the compaction of DNA into nucleosomes, the basic units of chromatin. A <strong>nucleosome</strong> consists of one pair of each of the core histones (<strong>H2A</strong>, <strong>H2B</strong>, <strong>H3</strong> and <strong>H4</strong>) forming an octameric structure wrapped by 146 base pairs of DNA. The different nucleosomes are linked by the linker histone<strong> H1, </strong>allowing for further condensation of chromatin.</p>
<p>The core histones have a globular structure with large unstructured N-terminal tails protruding from the nucleosome. They can undergo to multiple post-translational modifications (PTM), mainly at the N-terminal tails. These <strong>post-translational modifications </strong>include methylation, acetylation, phosphorylation, ubiquitinylation, citrullination, sumoylation, deamination and crotonylation. The most well characterized PTMs are <strong>methylation,</strong> <strong>acetylation and phosphorylation</strong>. Histone methylation occurs mainly on lysine (K) residues, which can be mono-, di- or tri-methylated, and on arginines (R), which can be mono-methylated and symmetrically or asymmetrically di-methylated. Histone acetylation occurs on lysines and histone phosphorylation mainly on serines (S), threonines (T) and tyrosines (Y).</p>
<p>The PTMs of the different residues are involved in numerous processes such as DNA repair, DNA replication and chromosome condensation. They influence the chromatin organization and can be positively or negatively associated with gene expression. Trimethylation of H3K4, H3K36 and H3K79, and lysine acetylation generally result in an open chromatin configuration (figure below) and are therefore associated with <strong>euchromatin</strong> and gene activation. Trimethylation of H3K9, K3K27 and H4K20, on the other hand, is enriched in <strong>heterochromatin </strong>and associated with gene silencing. The combination of different histone modifications is called the "<strong>histone code</strong>”, analogous to the genetic code.</p>
<p><img src="https://www.diagenode.com/img/categories/antibodies/histone-marks-illustration.png" /></p>
<p>Diagenode is proud to offer a large range of antibodies against histones and histone modifications. Our antibodies are highly specific and have been validated in many applications, including <strong>ChIP</strong> and <strong>ChIP-seq</strong>.</p>
<p>Diagenode’s collection includes antibodies recognizing:</p>
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<li><strong>Histone H1 variants</strong></li>
<li><strong>Histone H2A, H2A variants and histone H2A</strong> <strong>modifications</strong> (serine phosphorylation, lysine acetylation, lysine ubiquitinylation)</li>
<li><strong>Histone H2B and H2B</strong> <strong>modifications </strong>(serine phosphorylation, lysine acetylation)</li>
<li><strong>Histone H3 and H3 modifications </strong>(lysine methylation (mono-, di- and tri-methylated), lysine acetylation, serine phosphorylation, threonine phosphorylation, arginine methylation (mono-methylated, symmetrically and asymmetrically di-methylated))</li>
<li><strong>Histone H4 and H4 modifications (</strong>lysine methylation (mono-, di- and tri-methylated), lysine acetylation, arginine methylation (mono-methylated and symmetrically di-methylated), serine phosphorylation )</li>
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<p><span style="font-weight: 400;"><strong>HDAC's HAT's, HMT's and other</strong> <strong>enzymes</strong> which modify histones can be found in the category <a href="../categories/chromatin-modifying-proteins-histone-transferase">Histone modifying enzymes</a><br /></span></p>
<p><span style="font-weight: 400;"> Diagenode’s highly validated antibodies:</span></p>
<ul>
<li><span style="font-weight: 400;"> Highly sensitive and specific</span></li>
<li><span style="font-weight: 400;"> Cost-effective (requires less antibody per reaction)</span></li>
<li><span style="font-weight: 400;"> Batch-specific data is available on the website</span></li>
<li><span style="font-weight: 400;"> Expert technical support</span></li>
<li><span style="font-weight: 400;"> Sample sizes available</span></li>
<li><span style="font-weight: 400;"> 100% satisfaction guarantee</span></li>
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<p><span style="font-weight: 400;">Diagenode provides leading solutions for epigenetic research. Because ChIP-seq is a widely-used technique, we validate our antibodies in ChIP and ChIP-seq experiments (in addition to conventional methods like Western blot, Dot blot, ELISA, and immunofluorescence) to provide the highest quality antibody. We standardize our validation and production to guarantee high product quality without technical bias. Diagenode guarantees ChIP-seq grade antibody performance under our suggested conditions.</span></p>
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<p><strong>ChIP-seq profile</strong> of active (H3K4me3 and H3K36me3) and inactive (H3K27me3) marks using Diagenode antibodies.</p>
<img src="https://www.diagenode.com/img/categories/antibodies/chip-seq-grade-antibodies.png" /></div>
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<p><small> ChIP was performed on sheared chromatin from 100,000 K562 cells using iDeal ChIP-seq kit for Histones (cat. No. C01010051) with 1 µg of the Diagenode antibodies against H3K27me3 (cat. No. C15410195) and H3K4me3 (cat. No. C15410003), and 0.5 µg of the antibody against H3K36me3 (cat. No. C15410192). The IP'd DNA was subsequently analysed on an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. The figure shows the signal distribution along the complete sequence of human chromosome 3, a zoomin to a 10 Mb region and a further zoomin to a 1.5 Mb region. </small></p>
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<p>Diagenode’s highly validated antibodies:</p>
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<li>Highly sensitive and specific</li>
<li>Cost-effective (requires less antibody per reaction)</li>
<li>Batch-specific data is available on the website</li>
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<p>Diagenode has partnered with leading epigenetics experts and numerous epigenetics consortiums to bring to you a validated and comprehensive collection of epigenetic antibodies. As an expert in epigenetics, we are committed to offering highly-specific antibodies validated for ChIP/ChIP-seq and many other applications. All batch-specific validation data is available on our website.<br /><a href="../categories/antibodies">Read about our expertise in antibody production</a>.</p>
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<p><span style="font-weight: 400;">Diagenode’s highly validated antibodies:</span></p>
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<p><br />Chromatin immunoprecipitation (<b>ChIP</b>) is a technique to study the associations of proteins with the specific genomic regions in intact cells. One of the most important steps of this protocol is the immunoprecipitation of targeted protein using the antibody specifically recognizing it. The quality of antibodies used in ChIP is essential for the success of the experiment. Diagenode offers extensively validated ChIP-grade antibodies, confirmed for their specificity, and high level of performance in ChIP. Each batch is validated, and batch-specific data are available on the website.</p>
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<p><strong>ChIP results</strong> obtained with the antibody directed against H3K4me3 (Cat. No. <a href="../p/h3k4me3-polyclonal-antibody-premium-50-ug-50-ul">C15410003</a>). </p>
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<div class="small-12 medium-6 large-6 columns"><img src="https://www.diagenode.com/img/product/antibodies/C15410003-fig1-ChIP.jpg" alt="" width="400" height="315" /> </div>
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<p>Our aim at Diagenode is to offer the largest collection of highly specific <strong>ChIP-grade antibodies</strong>. We add new antibodies monthly. Find your ChIP-grade antibody in the list below and check more information about tested applications, extensive validation data, and product information.</p>',
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'authors' => 'Bieluszewski T. et al.',
'description' => '<p>Nucleosomal acetyltransferase of H4 (NuA4) is an essential transcriptional coactivator in eukaryotes, but remains poorly characterized in plants. Here, we describe Arabidopsis homologs of the NuA4 scaffold proteins Enhancer of Polycomb-Like 1 (AtEPL1) and Esa1-Associated Factor 1 (AtEAF1). Loss of AtEAF1 results in inhibition of growth and chloroplast development. These effects are stronger in the Atepl1 mutant and are further enhanced by loss of Golden2-Like (GLK) transcription factors, suggesting that NuA4 activates nuclear plastid genes alongside GLK. We demonstrate that AtEPL1 is necessary for nucleosomal acetylation of histones H4 and H2A.Z by NuA4 in vitro. These chromatin marks are diminished genome-wide in Atepl1, while another active chromatin mark, H3K9 acetylation (H3K9ac), is locally enhanced. Expression of many chloroplast-related genes depends on NuA4, as they are downregulated with loss of H4ac and H2A.Zac. Finally, we demonstrate that NuA4 promotes H2A.Z deposition and by doing so prevents spurious activation of stress response genes.</p>',
'date' => '2022-01-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/35022409',
'doi' => '10.1038/s41467-021-27882-5',
'modified' => '2022-05-19 17:02:00',
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(int) 1 => array(
'id' => '3473',
'name' => 'Neonatal exposure to hyperoxia leads to persistent disturbances in pulmonary histone signatures associated with NOS3 and STAT3 in a mouse model.',
'authors' => 'Chao CM, van den Bruck R, Lork S, Merkle J, Krampen L, Weil PP, Aydin M, Bellusci S, Jenke AC, Postberg J',
'description' => '<p>Background: Early pulmonary oxygen exposure is one of the most important factors implicated in the development of bronchopulmonary dysplasia (BPD). Methods: Here, we analyzed short- and long-term effects of neonatal hyperoxia on NOS3 and STAT3 expression and corresponding epigenetic signatures using a hyperoxia-based mouse model of BPD. Results: Early hyperoxia exposure led to a significant increase in NOS3 (median fold change × 2.37, IQR 1.54-3.68) and STAT3 (median fold change × 2.83, IQR 2.21-3.88) mRNA levels in pulmonary endothelial cells with corresponding changes in histone modification patterns such as H2aZac and H3K9ac hyperacetylation at the respective gene loci. No complete restoration in histone signatures at these loci was observed, and responsivity to later hyperoxia was altered in mouse lungs. In vitro, histone signatures in human aortic endothelial cells (HAEC) remained altered for several weeks after an initial long-term exposure to trichostatin A. This was associated with a substantial increase in baseline eNOS (median 27.2, IQR 22.3-35.6) and STAT3α (median 5.8, IQR 4.8-7.3) mRNA levels with a subsequent significant reduction in eNOS expression upon exposure to hypoxia. Conclusions: Early hyperoxia induced permanent changes in histones signatures at the NOS3 and STAT3 gene locus might partly explain the altered vascular response patterns in children with BPD.</p>',
'date' => '2018-01-01',
'pmid' => 'http://www.pubmed.gov/29581793',
'doi' => '10.1186/s13148-018-0469-0',
'modified' => '2019-02-15 21:45:12',
'created' => '2019-02-14 15:01:22',
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(int) 2 => array(
'id' => '2613',
'name' => 'CpG signalling, H2A.Z/H3 acetylation and microRNA-mediated deferred self-attenuation orchestrate foetal NOS3 expression.',
'authors' => 'Postberg J, Kanders M, Forcob S, Willems R, Orth V, Hensel KO, Weil PP, Wirth S, Jenke AC',
'description' => 'BACKGROUND: An adverse intrauterine environment leads to permanent physiological changes including vascular tone regulation, potentially influencing the risk for adult vascular diseases. We therefore aimed to monitor responsive NOS3 expression in human umbilical artery endothelial cells (HUAEC) and to study the underlying epigenetic signatures involved in its regulation. RESULTS: NOS3 and STAT3 mRNA levels were elevated in HUAEC of patients who suffered from placental insufficiency. 5-hydroxymethylcytosine, H3K9ac and Histone 2A (H2A).Zac at the NOS3 transcription start site directly correlated with NOS3 mRNA levels. Concomitantly, we observed entangled histone acetylation patterns and NOS3 response upon hypoxic conditions in vitro. Knock-down of either NOS3 or STAT3 by RNAi provided evidence for a functional NOS3/STAT3 relationship. Moreover, we recognized massive turnover of Stat3 at a discrete binding site in the NOS3 promoter. Interestingly, induced hyperacetylation resulted in short-termed increase of NOS3 mRNA followed by deferred decrease indicating that NOS3 expression could become self-attenuated by co-expressed intronic 27 nt-ncRNA. Reporter assay results and phylogenetic analyses enabled us to propose a novel model for STAT3-3'-UTR targeting by this 27-nt-ncRNA. CONCLUSIONS: An adverse intrauterine environment leads to adaptive changes of NOS3 expression. Apparently, a rapid NOS3 self-limiting response upon ectopic triggers co-exists with longer termed expression changes in response to placental insufficiency involving differential epigenetic signatures. Their persistence might contribute to impaired vascular endothelial response and consequently increase the risk of cardiovascular disease later in life.',
'date' => '2015-01-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/25699114',
'doi' => '',
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'name' => 'H2A.Zac Antibody',
'description' => '<p><span>Polyclonal antibody raised in rabbit against histone <strong>H2A.Z acetylated at lysines 4, 7 and 11,</strong> using a KLH-conjugated synthetic peptide.</span></p>',
'label1' => 'Validation Data',
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<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP.jpg" /></center></div>
<div class="small-6 columns">
<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<div class="small-12 columns"><center>A.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-A.jpg" width="700" /></center><center>B.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" width="700" /></center><center>C.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-C.jpg" width="700" /></center>
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<center>D.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-D.jpg" width="700" /></center></div>
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<div class="row">
<div class="small-12 columns">
<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<div class="row">
<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_ELISA.jpg" /></center></div>
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<p><strong>Figure 3. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (cat. No. C15410173). The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:265,000.</p>
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<div class="row">
<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_DB.jpg" width="220" /></center></div>
<div class="small-8 columns">
<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
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<p></p>
<p></p>
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<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_WB.jpg" /></center></div>
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<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<div class="row">
<div class="small-12 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_IF.jpg" width="700" /></center></div>
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<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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</div>',
'label2' => 'Target Description',
'info2' => '<p>Histones are the main constituents of the protein part of chromosomes of eukaryotic cells. They are rich in the amino acids arginine and lysine and have been greatly conserved during evolution. Histones pack the DNA into tight masses of chromatin. Two core histones of each class H2A, H2B, H3 and H4 assemble and are wrapped by 146 base pairs of DNA to form one octameric nucleosome. Histone tails undergo numerous post-translational modifications, which either directly or indirectly alter chromatin structure to facilitate transcriptional activation or repression or other nuclear processes. In addition to the genetic code, combinations of the different histone modifications reveal the so-called "histone code". Histone methylation and demethylation is dynamically regulated by respectively histone methyl transferases and histone demethylases. Acetylation of the histone H2A variant H2A.Z is associated with the promoters of active genes.</p>',
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'format' => '50 μg',
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'slug' => 'h2a-zac-polyclonal-antibody-classic-50-mg-72-ml',
'meta_title' => 'H2A.Zac Antibody - ChIP-seq Grade (C15410173) | Diagenode',
'meta_keywords' => '',
'meta_description' => 'H2A.Zac (Histone H2A.Z acetylated at lysines 4, 7 and 11) Polyclonal Antibody validated in ChIP-seq, ChIP-qPCR, DB, IF and ELISA. Batch-specific data available on the website. Sample size available.',
'modified' => '2024-01-17 16:35:59',
'created' => '2015-06-29 14:08:20'
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<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP.jpg" alt="H2A.Zac Antibody ChIP Grade" /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 1 million HeLaS3 cells using the “Auto Histone ChIP-seq” kit (Cat. No. AB-Auto02-A100) on the SX-8G IP-Star automated system. A titration of the antibody consisting of 1, 2, 5 and 10 μg per ChIP experiment was analysed. IgG (2 μg/ IP) was used as negative IP control. QPCR was performed using primers specific for the promoters of the ACTB and EIF4A2 genes, used as positive control targets and for the coding region of the MYT1 gene, used as a negative control target. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA). These results confirm the observation that acetylation of H2A.Z is present at active promoters. </small></p>
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<div class="row">
<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-A.jpg" alt="H2A.Zac Antibody for ChIP" /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP was performed with 1 μg of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) on sheared chromatin from 1 million HeLaS3 cells using the “iDeal ChIP-seq” kit (Cat. No. AB-001-0024). IgG (2 μg/IP) was used as a negative IP control. The IP’d DNA was analysed by QPCR as described above (figure 1A). The IP’d DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 1 shows the peak distribution along the complete sequence and a 600 kb region of the X-chromosome (figure 1B and C) and in 100 kb regions surrounding the EIF4A2, ACTB and GAPDH genes (figure 1D, E and F). These results clearly show an enrichment of the H2A.Z acetylation at the promoters of active genes. </small></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" alt="H2A.Zac Antibody for ChIP-seq" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-C.jpg" alt="H2A.Zac Antibody for ChIP-seq assay" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-D.jpg" alt="H2A.Zac Antibody validated in ChIP-seq" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-E.jpg" alt="H2A.Zac Antibody ChIP-seq Grade " /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-F.jpg" alt="H2A.Zac Antibody for ChIP-seq" /></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_ELISA.jpg" alt="H2A.Zac Antibody ELISA validation" /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 3. Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (Cat. No. pAb-173-050), crude serum and flow through in antigen coated wells. The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:8,800. </small></p>
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<div class="row">
<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_DB.jpg" alt="H2A.Zac Antibody validated in Dot Blot" /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br /> A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173- 050) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest. </small></p>
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</div>
<div class="row">
<div class="small-5 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_IF.jpg" alt="H2A.Zac Antibody validated in Immunofluorescence " /></p>
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<div class="small-7 columns">
<p><small><strong> Figure 5. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br /> HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. pAb-173-050) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right. </small></p>
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<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<p><strong>Figure 3. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (cat. No. C15410173). The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:265,000.</p>
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<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
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<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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'description' => 'BACKGROUND: An adverse intrauterine environment leads to permanent physiological changes including vascular tone regulation, potentially influencing the risk for adult vascular diseases. We therefore aimed to monitor responsive NOS3 expression in human umbilical artery endothelial cells (HUAEC) and to study the underlying epigenetic signatures involved in its regulation. RESULTS: NOS3 and STAT3 mRNA levels were elevated in HUAEC of patients who suffered from placental insufficiency. 5-hydroxymethylcytosine, H3K9ac and Histone 2A (H2A).Zac at the NOS3 transcription start site directly correlated with NOS3 mRNA levels. Concomitantly, we observed entangled histone acetylation patterns and NOS3 response upon hypoxic conditions in vitro. Knock-down of either NOS3 or STAT3 by RNAi provided evidence for a functional NOS3/STAT3 relationship. Moreover, we recognized massive turnover of Stat3 at a discrete binding site in the NOS3 promoter. Interestingly, induced hyperacetylation resulted in short-termed increase of NOS3 mRNA followed by deferred decrease indicating that NOS3 expression could become self-attenuated by co-expressed intronic 27 nt-ncRNA. Reporter assay results and phylogenetic analyses enabled us to propose a novel model for STAT3-3'-UTR targeting by this 27-nt-ncRNA. CONCLUSIONS: An adverse intrauterine environment leads to adaptive changes of NOS3 expression. Apparently, a rapid NOS3 self-limiting response upon ectopic triggers co-exists with longer termed expression changes in response to placental insufficiency involving differential epigenetic signatures. Their persistence might contribute to impaired vascular endothelial response and consequently increase the risk of cardiovascular disease later in life.',
'date' => '2015-01-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/25699114',
'doi' => '',
'modified' => '2015-07-24 15:39:05',
'created' => '2015-07-24 15:39:05',
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'publication_id' => '2613'
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<p><small><strong> Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 1 million HeLaS3 cells using the “Auto Histone ChIP-seq” kit (Cat. No. AB-Auto02-A100) on the SX-8G IP-Star automated system. A titration of the antibody consisting of 1, 2, 5 and 10 μg per ChIP experiment was analysed. IgG (2 μg/ IP) was used as negative IP control. QPCR was performed using primers specific for the promoters of the ACTB and EIF4A2 genes, used as positive control targets and for the coding region of the MYT1 gene, used as a negative control target. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA). These results confirm the observation that acetylation of H2A.Z is present at active promoters. </small></p>
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<p><small><strong> Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP was performed with 1 μg of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) on sheared chromatin from 1 million HeLaS3 cells using the “iDeal ChIP-seq” kit (Cat. No. AB-001-0024). IgG (2 μg/IP) was used as a negative IP control. The IP’d DNA was analysed by QPCR as described above (figure 1A). The IP’d DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 1 shows the peak distribution along the complete sequence and a 600 kb region of the X-chromosome (figure 1B and C) and in 100 kb regions surrounding the EIF4A2, ACTB and GAPDH genes (figure 1D, E and F). These results clearly show an enrichment of the H2A.Z acetylation at the promoters of active genes. </small></p>
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<p><small><strong> Figure 3. Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (Cat. No. pAb-173-050), crude serum and flow through in antigen coated wells. The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:8,800. </small></p>
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<p><small><strong> Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br /> A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173- 050) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest. </small></p>
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<p><small><strong> Figure 5. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br /> HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. pAb-173-050) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right. </small></p>
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<td>ChIP/ChIP-seq <sup>*</sup></td>
<td>0.5 μg/ChIP</td>
<td>Fig 1, 2</td>
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<td>1:5,000</td>
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<td>1:1,000</td>
<td>Fig 5</td>
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<td>Immunofluorescence</td>
<td>1:500</td>
<td>Fig 6</td>
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<p><small><sup>*</sup> Please note that the optimal antibody amount per IP should be determined by the end-user. We recommend testing 0.5-5 μg per IP.</small></p>',
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'description' => '<p><span>Polyclonal antibody raised in rabbit against histone <strong>H2A.Z acetylated at lysines 4, 7 and 11,</strong> using a KLH-conjugated synthetic peptide.</span></p>',
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<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP.jpg" alt="H2A.Zac Antibody ChIP Grade" /></p>
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<p><small><strong> Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 1 million HeLaS3 cells using the “Auto Histone ChIP-seq” kit (Cat. No. AB-Auto02-A100) on the SX-8G IP-Star automated system. A titration of the antibody consisting of 1, 2, 5 and 10 μg per ChIP experiment was analysed. IgG (2 μg/ IP) was used as negative IP control. QPCR was performed using primers specific for the promoters of the ACTB and EIF4A2 genes, used as positive control targets and for the coding region of the MYT1 gene, used as a negative control target. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA). These results confirm the observation that acetylation of H2A.Z is present at active promoters. </small></p>
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<div class="row">
<div class="small-4 columns">
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<p><small><strong> Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP was performed with 1 μg of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) on sheared chromatin from 1 million HeLaS3 cells using the “iDeal ChIP-seq” kit (Cat. No. AB-001-0024). IgG (2 μg/IP) was used as a negative IP control. The IP’d DNA was analysed by QPCR as described above (figure 1A). The IP’d DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 1 shows the peak distribution along the complete sequence and a 600 kb region of the X-chromosome (figure 1B and C) and in 100 kb regions surrounding the EIF4A2, ACTB and GAPDH genes (figure 1D, E and F). These results clearly show an enrichment of the H2A.Z acetylation at the promoters of active genes. </small></p>
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<div class="row">
<div class="small-4 columns">
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<div class="small-8 columns">
<p><small><strong> Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br /> A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173- 050) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest. </small></p>
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<div class="row">
<div class="small-5 columns">
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<p><small><strong> Figure 5. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br /> HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. pAb-173-050) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right. </small></p>
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<p><small><sup>*</sup> Please note that the optimal antibody amount per IP should be determined by the end-user. We recommend testing 0.5-5 μg per IP.</small></p>',
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'name' => 'H2A.Zac Antibody',
'description' => '<p><span>Polyclonal antibody raised in rabbit against histone <strong>H2A.Z acetylated at lysines 4, 7 and 11,</strong> using a KLH-conjugated synthetic peptide.</span></p>',
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<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP.jpg" /></center></div>
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<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<div class="row">
<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_ELISA.jpg" /></center></div>
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<p><strong>Figure 3. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (cat. No. C15410173). The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:265,000.</p>
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<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
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<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_WB.jpg" /></center></div>
<div class="small-8 columns">
<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<div class="small-12 columns"><center>A.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-A.jpg" width="700" /></center><center>B.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" width="700" /></center><center>C.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-C.jpg" width="700" /></center>
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<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
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<div class="row">
<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_WB.jpg" /></center></div>
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<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15200229-IF.jpg" alt="" height="245" width="256" /></p>
<p><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
<p><sup>HeLa cells transfected with a Cas9 expression vector (left) or untransfected cells (right) were fixed in methanol at -20°C, permeabilized with acetone at -20°C and blocked with PBS containing 2% BSA. The cells were stained with the Cas9 C-terminal antibody (Cat. No. C15200229) diluted 1:400, followed by incubation with an anti-mouse secondary antibody coupled to AF488. The bottom images show counter-staining of the nuclei with Hoechst 33342.</sup></p>
<h5><sup>Check our selection of antibodies validated in IF.</sup></h5>',
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'description' => '<p>Histones are the main protein components of chromatin involved in the compaction of DNA into nucleosomes, the basic units of chromatin. A <strong>nucleosome</strong> consists of one pair of each of the core histones (<strong>H2A</strong>, <strong>H2B</strong>, <strong>H3</strong> and <strong>H4</strong>) forming an octameric structure wrapped by 146 base pairs of DNA. The different nucleosomes are linked by the linker histone<strong> H1, </strong>allowing for further condensation of chromatin.</p>
<p>The core histones have a globular structure with large unstructured N-terminal tails protruding from the nucleosome. They can undergo to multiple post-translational modifications (PTM), mainly at the N-terminal tails. These <strong>post-translational modifications </strong>include methylation, acetylation, phosphorylation, ubiquitinylation, citrullination, sumoylation, deamination and crotonylation. The most well characterized PTMs are <strong>methylation,</strong> <strong>acetylation and phosphorylation</strong>. Histone methylation occurs mainly on lysine (K) residues, which can be mono-, di- or tri-methylated, and on arginines (R), which can be mono-methylated and symmetrically or asymmetrically di-methylated. Histone acetylation occurs on lysines and histone phosphorylation mainly on serines (S), threonines (T) and tyrosines (Y).</p>
<p>The PTMs of the different residues are involved in numerous processes such as DNA repair, DNA replication and chromosome condensation. They influence the chromatin organization and can be positively or negatively associated with gene expression. Trimethylation of H3K4, H3K36 and H3K79, and lysine acetylation generally result in an open chromatin configuration (figure below) and are therefore associated with <strong>euchromatin</strong> and gene activation. Trimethylation of H3K9, K3K27 and H4K20, on the other hand, is enriched in <strong>heterochromatin </strong>and associated with gene silencing. The combination of different histone modifications is called the "<strong>histone code</strong>”, analogous to the genetic code.</p>
<p><img src="https://www.diagenode.com/img/categories/antibodies/histone-marks-illustration.png" /></p>
<p>Diagenode is proud to offer a large range of antibodies against histones and histone modifications. Our antibodies are highly specific and have been validated in many applications, including <strong>ChIP</strong> and <strong>ChIP-seq</strong>.</p>
<p>Diagenode’s collection includes antibodies recognizing:</p>
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<li><strong>Histone H1 variants</strong></li>
<li><strong>Histone H2A, H2A variants and histone H2A</strong> <strong>modifications</strong> (serine phosphorylation, lysine acetylation, lysine ubiquitinylation)</li>
<li><strong>Histone H2B and H2B</strong> <strong>modifications </strong>(serine phosphorylation, lysine acetylation)</li>
<li><strong>Histone H3 and H3 modifications </strong>(lysine methylation (mono-, di- and tri-methylated), lysine acetylation, serine phosphorylation, threonine phosphorylation, arginine methylation (mono-methylated, symmetrically and asymmetrically di-methylated))</li>
<li><strong>Histone H4 and H4 modifications (</strong>lysine methylation (mono-, di- and tri-methylated), lysine acetylation, arginine methylation (mono-methylated and symmetrically di-methylated), serine phosphorylation )</li>
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<p><span style="font-weight: 400;"><strong>HDAC's HAT's, HMT's and other</strong> <strong>enzymes</strong> which modify histones can be found in the category <a href="../categories/chromatin-modifying-proteins-histone-transferase">Histone modifying enzymes</a><br /></span></p>
<p><span style="font-weight: 400;"> Diagenode’s highly validated antibodies:</span></p>
<ul>
<li><span style="font-weight: 400;"> Highly sensitive and specific</span></li>
<li><span style="font-weight: 400;"> Cost-effective (requires less antibody per reaction)</span></li>
<li><span style="font-weight: 400;"> Batch-specific data is available on the website</span></li>
<li><span style="font-weight: 400;"> Expert technical support</span></li>
<li><span style="font-weight: 400;"> Sample sizes available</span></li>
<li><span style="font-weight: 400;"> 100% satisfaction guarantee</span></li>
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<p><span style="font-weight: 400;">Diagenode provides leading solutions for epigenetic research. Because ChIP-seq is a widely-used technique, we validate our antibodies in ChIP and ChIP-seq experiments (in addition to conventional methods like Western blot, Dot blot, ELISA, and immunofluorescence) to provide the highest quality antibody. We standardize our validation and production to guarantee high product quality without technical bias. Diagenode guarantees ChIP-seq grade antibody performance under our suggested conditions.</span></p>
<div class="row">
<div class="small-12 medium-9 large-9 columns">
<p><strong>ChIP-seq profile</strong> of active (H3K4me3 and H3K36me3) and inactive (H3K27me3) marks using Diagenode antibodies.</p>
<img src="https://www.diagenode.com/img/categories/antibodies/chip-seq-grade-antibodies.png" /></div>
<div class="small-12 medium-3 large-3 columns">
<p><small> ChIP was performed on sheared chromatin from 100,000 K562 cells using iDeal ChIP-seq kit for Histones (cat. No. C01010051) with 1 µg of the Diagenode antibodies against H3K27me3 (cat. No. C15410195) and H3K4me3 (cat. No. C15410003), and 0.5 µg of the antibody against H3K36me3 (cat. No. C15410192). The IP'd DNA was subsequently analysed on an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. The figure shows the signal distribution along the complete sequence of human chromosome 3, a zoomin to a 10 Mb region and a further zoomin to a 1.5 Mb region. </small></p>
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<p>Diagenode’s highly validated antibodies:</p>
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<li>Highly sensitive and specific</li>
<li>Cost-effective (requires less antibody per reaction)</li>
<li>Batch-specific data is available on the website</li>
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<p>Diagenode has partnered with leading epigenetics experts and numerous epigenetics consortiums to bring to you a validated and comprehensive collection of epigenetic antibodies. As an expert in epigenetics, we are committed to offering highly-specific antibodies validated for ChIP/ChIP-seq and many other applications. All batch-specific validation data is available on our website.<br /><a href="../categories/antibodies">Read about our expertise in antibody production</a>.</p>
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<li><strong>Focused</strong> - Diagenode's selection of antibodies is exclusively dedicated for epigenetic research. <a title="See the full collection." href="../categories/all-antibodies">See the full collection.</a></li>
<li><strong>Strict quality standards</strong> with rigorous QC and validation</li>
<li><strong>Classified</strong> based on level of validation for flexibility of application</li>
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<p>Existing sample sizes are listed below. We will soon expand our collection. Are you looking for a sample size of another antibody? Just <a href="mailto:agnieszka.zelisko@diagenode.com?Subject=Sample%20Size%20Request" target="_top">Contact us</a>.</p>',
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<p><span style="font-weight: 400;">Diagenode’s highly validated antibodies:</span></p>
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<li>Highly sensitive and specific</li>
<li>Cost-effective (requires less antibody per reaction)</li>
<li>Batch-specific data is available on the website</li>
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<div class="small-12 columns"><center></center>
<p><br />Chromatin immunoprecipitation (<b>ChIP</b>) is a technique to study the associations of proteins with the specific genomic regions in intact cells. One of the most important steps of this protocol is the immunoprecipitation of targeted protein using the antibody specifically recognizing it. The quality of antibodies used in ChIP is essential for the success of the experiment. Diagenode offers extensively validated ChIP-grade antibodies, confirmed for their specificity, and high level of performance in ChIP. Each batch is validated, and batch-specific data are available on the website.</p>
<p></p>
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<p><strong>ChIP results</strong> obtained with the antibody directed against H3K4me3 (Cat. No. <a href="../p/h3k4me3-polyclonal-antibody-premium-50-ug-50-ul">C15410003</a>). </p>
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<div class="small-12 medium-6 large-6 columns"><img src="https://www.diagenode.com/img/product/antibodies/C15410003-fig1-ChIP.jpg" alt="" width="400" height="315" /> </div>
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<p></p>
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<p></p>
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<p>Our aim at Diagenode is to offer the largest collection of highly specific <strong>ChIP-grade antibodies</strong>. We add new antibodies monthly. Find your ChIP-grade antibody in the list below and check more information about tested applications, extensive validation data, and product information.</p>',
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'authors' => 'Bieluszewski T. et al.',
'description' => '<p>Nucleosomal acetyltransferase of H4 (NuA4) is an essential transcriptional coactivator in eukaryotes, but remains poorly characterized in plants. Here, we describe Arabidopsis homologs of the NuA4 scaffold proteins Enhancer of Polycomb-Like 1 (AtEPL1) and Esa1-Associated Factor 1 (AtEAF1). Loss of AtEAF1 results in inhibition of growth and chloroplast development. These effects are stronger in the Atepl1 mutant and are further enhanced by loss of Golden2-Like (GLK) transcription factors, suggesting that NuA4 activates nuclear plastid genes alongside GLK. We demonstrate that AtEPL1 is necessary for nucleosomal acetylation of histones H4 and H2A.Z by NuA4 in vitro. These chromatin marks are diminished genome-wide in Atepl1, while another active chromatin mark, H3K9 acetylation (H3K9ac), is locally enhanced. Expression of many chloroplast-related genes depends on NuA4, as they are downregulated with loss of H4ac and H2A.Zac. Finally, we demonstrate that NuA4 promotes H2A.Z deposition and by doing so prevents spurious activation of stress response genes.</p>',
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'authors' => 'Chao CM, van den Bruck R, Lork S, Merkle J, Krampen L, Weil PP, Aydin M, Bellusci S, Jenke AC, Postberg J',
'description' => '<p>Background: Early pulmonary oxygen exposure is one of the most important factors implicated in the development of bronchopulmonary dysplasia (BPD). Methods: Here, we analyzed short- and long-term effects of neonatal hyperoxia on NOS3 and STAT3 expression and corresponding epigenetic signatures using a hyperoxia-based mouse model of BPD. Results: Early hyperoxia exposure led to a significant increase in NOS3 (median fold change × 2.37, IQR 1.54-3.68) and STAT3 (median fold change × 2.83, IQR 2.21-3.88) mRNA levels in pulmonary endothelial cells with corresponding changes in histone modification patterns such as H2aZac and H3K9ac hyperacetylation at the respective gene loci. No complete restoration in histone signatures at these loci was observed, and responsivity to later hyperoxia was altered in mouse lungs. In vitro, histone signatures in human aortic endothelial cells (HAEC) remained altered for several weeks after an initial long-term exposure to trichostatin A. This was associated with a substantial increase in baseline eNOS (median 27.2, IQR 22.3-35.6) and STAT3α (median 5.8, IQR 4.8-7.3) mRNA levels with a subsequent significant reduction in eNOS expression upon exposure to hypoxia. Conclusions: Early hyperoxia induced permanent changes in histones signatures at the NOS3 and STAT3 gene locus might partly explain the altered vascular response patterns in children with BPD.</p>',
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'description' => 'BACKGROUND: An adverse intrauterine environment leads to permanent physiological changes including vascular tone regulation, potentially influencing the risk for adult vascular diseases. We therefore aimed to monitor responsive NOS3 expression in human umbilical artery endothelial cells (HUAEC) and to study the underlying epigenetic signatures involved in its regulation. RESULTS: NOS3 and STAT3 mRNA levels were elevated in HUAEC of patients who suffered from placental insufficiency. 5-hydroxymethylcytosine, H3K9ac and Histone 2A (H2A).Zac at the NOS3 transcription start site directly correlated with NOS3 mRNA levels. Concomitantly, we observed entangled histone acetylation patterns and NOS3 response upon hypoxic conditions in vitro. Knock-down of either NOS3 or STAT3 by RNAi provided evidence for a functional NOS3/STAT3 relationship. Moreover, we recognized massive turnover of Stat3 at a discrete binding site in the NOS3 promoter. Interestingly, induced hyperacetylation resulted in short-termed increase of NOS3 mRNA followed by deferred decrease indicating that NOS3 expression could become self-attenuated by co-expressed intronic 27 nt-ncRNA. Reporter assay results and phylogenetic analyses enabled us to propose a novel model for STAT3-3'-UTR targeting by this 27-nt-ncRNA. CONCLUSIONS: An adverse intrauterine environment leads to adaptive changes of NOS3 expression. Apparently, a rapid NOS3 self-limiting response upon ectopic triggers co-exists with longer termed expression changes in response to placental insufficiency involving differential epigenetic signatures. Their persistence might contribute to impaired vascular endothelial response and consequently increase the risk of cardiovascular disease later in life.',
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<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP.jpg" /></center></div>
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<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<div class="small-12 columns"><center>A.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-A.jpg" width="700" /></center><center>B.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" width="700" /></center><center>C.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-C.jpg" width="700" /></center>
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<div class="row">
<div class="small-12 columns">
<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<div class="extra-spaced"></div>
<div class="row">
<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_ELISA.jpg" /></center></div>
<div class="small-6 columns">
<p><strong>Figure 3. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (cat. No. C15410173). The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:265,000.</p>
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<div class="extra-spaced"></div>
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<div class="row">
<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_DB.jpg" width="220" /></center></div>
<div class="small-8 columns">
<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
<p></p>
<p></p>
<p></p>
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<div class="row">
<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_WB.jpg" /></center></div>
<div class="small-8 columns">
<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<div class="extra-spaced"></div>
<div class="extra-spaced"></div>
<div class="row">
<div class="small-12 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_IF.jpg" width="700" /></center></div>
</div>
<div class="row">
<div class="small-12 columns">
<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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<p><small><strong> Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 1 million HeLaS3 cells using the “Auto Histone ChIP-seq” kit (Cat. No. AB-Auto02-A100) on the SX-8G IP-Star automated system. A titration of the antibody consisting of 1, 2, 5 and 10 μg per ChIP experiment was analysed. IgG (2 μg/ IP) was used as negative IP control. QPCR was performed using primers specific for the promoters of the ACTB and EIF4A2 genes, used as positive control targets and for the coding region of the MYT1 gene, used as a negative control target. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA). These results confirm the observation that acetylation of H2A.Z is present at active promoters. </small></p>
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<p><small><strong> Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP was performed with 1 μg of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) on sheared chromatin from 1 million HeLaS3 cells using the “iDeal ChIP-seq” kit (Cat. No. AB-001-0024). IgG (2 μg/IP) was used as a negative IP control. The IP’d DNA was analysed by QPCR as described above (figure 1A). The IP’d DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 1 shows the peak distribution along the complete sequence and a 600 kb region of the X-chromosome (figure 1B and C) and in 100 kb regions surrounding the EIF4A2, ACTB and GAPDH genes (figure 1D, E and F). These results clearly show an enrichment of the H2A.Z acetylation at the promoters of active genes. </small></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" alt="H2A.Zac Antibody for ChIP-seq" /></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-E.jpg" alt="H2A.Zac Antibody ChIP-seq Grade " /></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_ELISA.jpg" alt="H2A.Zac Antibody ELISA validation" /></p>
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<p><small><strong> Figure 3. Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (Cat. No. pAb-173-050), crude serum and flow through in antigen coated wells. The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:8,800. </small></p>
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<div class="row">
<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_DB.jpg" alt="H2A.Zac Antibody validated in Dot Blot" /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br /> A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173- 050) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest. </small></p>
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<div class="row">
<div class="small-5 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_IF.jpg" alt="H2A.Zac Antibody validated in Immunofluorescence " /></p>
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<div class="small-7 columns">
<p><small><strong> Figure 5. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br /> HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. pAb-173-050) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right. </small></p>
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<a href="/jp/p/h2a-zac-polyclonal-antibody-classic-50-mg-72-ml"><img src="/img/product/antibodies/chipseq-grade-ab-icon.png" alt="ChIP-seq Grade" class="th"/></a> </div>
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<span class="success label" style="">C15410173</span>
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<h6 style="height:60px">H2A.Zac polyclonal antibody </h6>
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<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP.jpg" /></center></div>
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<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<p><strong>Figure 3. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (cat. No. C15410173). The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:265,000.</p>
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<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
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<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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'description' => '<p><span>Polyclonal antibody raised in rabbit against histone <strong>H2A.Z acetylated at lysines 4, 7 and 11,</strong> using a KLH-conjugated synthetic peptide.</span></p>',
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<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP.jpg" /></center></div>
<div class="small-6 columns">
<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<div class="small-12 columns"><center>A.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-A.jpg" width="700" /></center><center>B.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" width="700" /></center><center>C.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-C.jpg" width="700" /></center>
<div class="extra-spaced"></div>
<div class="extra-spaced"></div>
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<div class="row">
<div class="small-12 columns">
<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<div class="row">
<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_ELISA.jpg" /></center></div>
<div class="small-6 columns">
<p><strong>Figure 3. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (cat. No. C15410173). The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:265,000.</p>
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<div class="row">
<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_DB.jpg" width="220" /></center></div>
<div class="small-8 columns">
<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
<p></p>
<p></p>
<p></p>
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</div>
<div class="row">
<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_WB.jpg" /></center></div>
<div class="small-8 columns">
<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<div class="extra-spaced"></div>
<div class="extra-spaced"></div>
<div class="row">
<div class="small-12 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_IF.jpg" width="700" /></center></div>
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<div class="row">
<div class="small-12 columns">
<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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'name' => 'CpG signalling, H2A.Z/H3 acetylation and microRNA-mediated deferred self-attenuation orchestrate foetal NOS3 expression.',
'authors' => 'Postberg J, Kanders M, Forcob S, Willems R, Orth V, Hensel KO, Weil PP, Wirth S, Jenke AC',
'description' => 'BACKGROUND: An adverse intrauterine environment leads to permanent physiological changes including vascular tone regulation, potentially influencing the risk for adult vascular diseases. We therefore aimed to monitor responsive NOS3 expression in human umbilical artery endothelial cells (HUAEC) and to study the underlying epigenetic signatures involved in its regulation. RESULTS: NOS3 and STAT3 mRNA levels were elevated in HUAEC of patients who suffered from placental insufficiency. 5-hydroxymethylcytosine, H3K9ac and Histone 2A (H2A).Zac at the NOS3 transcription start site directly correlated with NOS3 mRNA levels. Concomitantly, we observed entangled histone acetylation patterns and NOS3 response upon hypoxic conditions in vitro. Knock-down of either NOS3 or STAT3 by RNAi provided evidence for a functional NOS3/STAT3 relationship. Moreover, we recognized massive turnover of Stat3 at a discrete binding site in the NOS3 promoter. Interestingly, induced hyperacetylation resulted in short-termed increase of NOS3 mRNA followed by deferred decrease indicating that NOS3 expression could become self-attenuated by co-expressed intronic 27 nt-ncRNA. Reporter assay results and phylogenetic analyses enabled us to propose a novel model for STAT3-3'-UTR targeting by this 27-nt-ncRNA. CONCLUSIONS: An adverse intrauterine environment leads to adaptive changes of NOS3 expression. Apparently, a rapid NOS3 self-limiting response upon ectopic triggers co-exists with longer termed expression changes in response to placental insufficiency involving differential epigenetic signatures. Their persistence might contribute to impaired vascular endothelial response and consequently increase the risk of cardiovascular disease later in life.',
'date' => '2015-01-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/25699114',
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'modified' => '2015-07-24 15:39:05',
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<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP.jpg" alt="H2A.Zac Antibody ChIP Grade" /></p>
</div>
<div class="small-8 columns">
<p><small><strong> Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 1 million HeLaS3 cells using the “Auto Histone ChIP-seq” kit (Cat. No. AB-Auto02-A100) on the SX-8G IP-Star automated system. A titration of the antibody consisting of 1, 2, 5 and 10 μg per ChIP experiment was analysed. IgG (2 μg/ IP) was used as negative IP control. QPCR was performed using primers specific for the promoters of the ACTB and EIF4A2 genes, used as positive control targets and for the coding region of the MYT1 gene, used as a negative control target. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA). These results confirm the observation that acetylation of H2A.Z is present at active promoters. </small></p>
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<div class="row">
<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-A.jpg" alt="H2A.Zac Antibody for ChIP" /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP was performed with 1 μg of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) on sheared chromatin from 1 million HeLaS3 cells using the “iDeal ChIP-seq” kit (Cat. No. AB-001-0024). IgG (2 μg/IP) was used as a negative IP control. The IP’d DNA was analysed by QPCR as described above (figure 1A). The IP’d DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 1 shows the peak distribution along the complete sequence and a 600 kb region of the X-chromosome (figure 1B and C) and in 100 kb regions surrounding the EIF4A2, ACTB and GAPDH genes (figure 1D, E and F). These results clearly show an enrichment of the H2A.Z acetylation at the promoters of active genes. </small></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" alt="H2A.Zac Antibody for ChIP-seq" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-C.jpg" alt="H2A.Zac Antibody for ChIP-seq assay" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-D.jpg" alt="H2A.Zac Antibody validated in ChIP-seq" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-E.jpg" alt="H2A.Zac Antibody ChIP-seq Grade " /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-F.jpg" alt="H2A.Zac Antibody for ChIP-seq" /></p>
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<div class="row">
<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_ELISA.jpg" alt="H2A.Zac Antibody ELISA validation" /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 3. Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (Cat. No. pAb-173-050), crude serum and flow through in antigen coated wells. The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:8,800. </small></p>
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<div class="row">
<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_DB.jpg" alt="H2A.Zac Antibody validated in Dot Blot" /></p>
</div>
<div class="small-8 columns">
<p><small><strong> Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br /> A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173- 050) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest. </small></p>
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</div>
<div class="row">
<div class="small-5 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_IF.jpg" alt="H2A.Zac Antibody validated in Immunofluorescence " /></p>
</div>
<div class="small-7 columns">
<p><small><strong> Figure 5. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br /> HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. pAb-173-050) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right. </small></p>
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'description' => 'Histones are the main constituents of the protein part of chromosomes of eukaryotic cells. They are rich in the amino acids arginine and lysine and have been greatly conserved during evolution. Histones pack the DNA into tight masses of chromatin. Two core histones of each class H2A, H2B, H3 and H4 assemble and are wrapped by 146 base pairs of DNA to form one octameric nucleosome. Histone tails undergo numerous post-translational modifications, which either directly or indirectly alter chromatin structure to facilitate transcriptional activation or repression or other nuclear processes. In addition to the genetic code, combinations of the different histone modifications reveal the so-called “histone code”. Histone methylation and demethylation is dynamically regulated by respectively histone methyl transferases and histone demethylases. Acetylation of the histone H2A variant H2A.Z is associated with the promoters of active genes.',
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'reactivity' => 'Human: positive. Other species: not tested.',
'type' => 'Polyclonal, <strong>ChIP grade, ChIP-seq grade</strong>',
'purity' => 'Affinity purified',
'classification' => 'Classic',
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<thead>
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<th>Suggested dilution</th>
<th>References</th>
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<td>ChIP/ChIP-seq <sup>*</sup></td>
<td>0.5 μg/ChIP</td>
<td>Fig 1, 2</td>
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<tr>
<td>ELISA</td>
<td>1:5,000</td>
<td>Fig 3</td>
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<tr>
<td>Dot Blotting</td>
<td>1:20,000</td>
<td>Fig 4</td>
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<tr>
<td>Western Blotting</td>
<td>1:1,000</td>
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<td>1:500</td>
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<p><small><strong> Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 1 million HeLaS3 cells using the “Auto Histone ChIP-seq” kit (Cat. No. AB-Auto02-A100) on the SX-8G IP-Star automated system. A titration of the antibody consisting of 1, 2, 5 and 10 μg per ChIP experiment was analysed. IgG (2 μg/ IP) was used as negative IP control. QPCR was performed using primers specific for the promoters of the ACTB and EIF4A2 genes, used as positive control targets and for the coding region of the MYT1 gene, used as a negative control target. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA). These results confirm the observation that acetylation of H2A.Z is present at active promoters. </small></p>
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<p><small><strong> Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP was performed with 1 μg of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) on sheared chromatin from 1 million HeLaS3 cells using the “iDeal ChIP-seq” kit (Cat. No. AB-001-0024). IgG (2 μg/IP) was used as a negative IP control. The IP’d DNA was analysed by QPCR as described above (figure 1A). The IP’d DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 1 shows the peak distribution along the complete sequence and a 600 kb region of the X-chromosome (figure 1B and C) and in 100 kb regions surrounding the EIF4A2, ACTB and GAPDH genes (figure 1D, E and F). These results clearly show an enrichment of the H2A.Z acetylation at the promoters of active genes. </small></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" alt="H2A.Zac Antibody for ChIP-seq" /></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-D.jpg" alt="H2A.Zac Antibody validated in ChIP-seq" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-E.jpg" alt="H2A.Zac Antibody ChIP-seq Grade " /></p>
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<p><small><strong> Figure 3. Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (Cat. No. pAb-173-050), crude serum and flow through in antigen coated wells. The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:8,800. </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_DB.jpg" alt="H2A.Zac Antibody validated in Dot Blot" /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br /> A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173- 050) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest. </small></p>
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<div class="row">
<div class="small-5 columns">
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<p><small><strong> Figure 5. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br /> HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. pAb-173-050) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right. </small></p>
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'description' => 'Histones are the main constituents of the protein part of chromosomes of eukaryotic cells. They are rich in the amino acids arginine and lysine and have been greatly conserved during evolution. Histones pack the DNA into tight masses of chromatin. Two core histones of each class H2A, H2B, H3 and H4 assemble and are wrapped by 146 base pairs of DNA to form one octameric nucleosome. Histone tails undergo numerous post-translational modifications, which either directly or indirectly alter chromatin structure to facilitate transcriptional activation or repression or other nuclear processes. In addition to the genetic code, combinations of the different histone modifications reveal the so-called “histone code”. Histone methylation and demethylation is dynamically regulated by respectively histone methyl transferases and histone demethylases. Acetylation of the histone H2A variant H2A.Z is associated with the promoters of active genes.',
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<th>References</th>
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<td>ChIP/ChIP-seq <sup>*</sup></td>
<td>0.5 μg/ChIP</td>
<td>Fig 1, 2</td>
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<tr>
<td>ELISA</td>
<td>1:5,000</td>
<td>Fig 3</td>
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<tr>
<td>Dot Blotting</td>
<td>1:20,000</td>
<td>Fig 4</td>
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<tr>
<td>Western Blotting</td>
<td>1:1,000</td>
<td>Fig 5</td>
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<td>Immunofluorescence</td>
<td>1:500</td>
<td>Fig 6</td>
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<p><small><sup>*</sup> Please note that the optimal antibody amount per IP should be determined by the end-user. We recommend testing 0.5-5 μg per IP.</small></p>',
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'name' => 'H2A.Zac Antibody',
'description' => '<p><span>Polyclonal antibody raised in rabbit against histone <strong>H2A.Z acetylated at lysines 4, 7 and 11,</strong> using a KLH-conjugated synthetic peptide.</span></p>',
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<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP.jpg" /></center></div>
<div class="small-6 columns">
<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<div class="extra-spaced"></div>
<div class="row">
<div class="small-12 columns"><center>A.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-A.jpg" width="700" /></center><center>B.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" width="700" /></center><center>C.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-C.jpg" width="700" /></center>
<div class="extra-spaced"></div>
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<center>D.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-D.jpg" width="700" /></center></div>
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<div class="row">
<div class="small-12 columns">
<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<div class="extra-spaced"></div>
<div class="row">
<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_ELISA.jpg" /></center></div>
<div class="small-6 columns">
<p><strong>Figure 3. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (cat. No. C15410173). The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:265,000.</p>
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<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_DB.jpg" width="220" /></center></div>
<div class="small-8 columns">
<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
<p></p>
<p></p>
<p></p>
</div>
</div>
<div class="row">
<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_WB.jpg" /></center></div>
<div class="small-8 columns">
<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<div class="row">
<div class="small-12 columns">
<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_ELISA.jpg" /></center></div>
<div class="small-6 columns">
<p><strong>Figure 3. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (cat. No. C15410173). The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:265,000.</p>
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<div class="small-8 columns">
<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
<p></p>
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<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_WB.jpg" /></center></div>
<div class="small-8 columns">
<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<div class="small-12 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_IF.jpg" width="700" /></center></div>
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<div class="small-12 columns">
<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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<p>Diagenode offers huge selection of highly sensitive antibodies validated in IF.</p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15200229-IF.jpg" alt="" height="245" width="256" /></p>
<p><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
<p><sup>HeLa cells transfected with a Cas9 expression vector (left) or untransfected cells (right) were fixed in methanol at -20°C, permeabilized with acetone at -20°C and blocked with PBS containing 2% BSA. The cells were stained with the Cas9 C-terminal antibody (Cat. No. C15200229) diluted 1:400, followed by incubation with an anti-mouse secondary antibody coupled to AF488. The bottom images show counter-staining of the nuclei with Hoechst 33342.</sup></p>
<h5><sup>Check our selection of antibodies validated in IF.</sup></h5>',
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'description' => '<p>Histones are the main protein components of chromatin involved in the compaction of DNA into nucleosomes, the basic units of chromatin. A <strong>nucleosome</strong> consists of one pair of each of the core histones (<strong>H2A</strong>, <strong>H2B</strong>, <strong>H3</strong> and <strong>H4</strong>) forming an octameric structure wrapped by 146 base pairs of DNA. The different nucleosomes are linked by the linker histone<strong> H1, </strong>allowing for further condensation of chromatin.</p>
<p>The core histones have a globular structure with large unstructured N-terminal tails protruding from the nucleosome. They can undergo to multiple post-translational modifications (PTM), mainly at the N-terminal tails. These <strong>post-translational modifications </strong>include methylation, acetylation, phosphorylation, ubiquitinylation, citrullination, sumoylation, deamination and crotonylation. The most well characterized PTMs are <strong>methylation,</strong> <strong>acetylation and phosphorylation</strong>. Histone methylation occurs mainly on lysine (K) residues, which can be mono-, di- or tri-methylated, and on arginines (R), which can be mono-methylated and symmetrically or asymmetrically di-methylated. Histone acetylation occurs on lysines and histone phosphorylation mainly on serines (S), threonines (T) and tyrosines (Y).</p>
<p>The PTMs of the different residues are involved in numerous processes such as DNA repair, DNA replication and chromosome condensation. They influence the chromatin organization and can be positively or negatively associated with gene expression. Trimethylation of H3K4, H3K36 and H3K79, and lysine acetylation generally result in an open chromatin configuration (figure below) and are therefore associated with <strong>euchromatin</strong> and gene activation. Trimethylation of H3K9, K3K27 and H4K20, on the other hand, is enriched in <strong>heterochromatin </strong>and associated with gene silencing. The combination of different histone modifications is called the "<strong>histone code</strong>”, analogous to the genetic code.</p>
<p><img src="https://www.diagenode.com/img/categories/antibodies/histone-marks-illustration.png" /></p>
<p>Diagenode is proud to offer a large range of antibodies against histones and histone modifications. Our antibodies are highly specific and have been validated in many applications, including <strong>ChIP</strong> and <strong>ChIP-seq</strong>.</p>
<p>Diagenode’s collection includes antibodies recognizing:</p>
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<li><strong>Histone H1 variants</strong></li>
<li><strong>Histone H2A, H2A variants and histone H2A</strong> <strong>modifications</strong> (serine phosphorylation, lysine acetylation, lysine ubiquitinylation)</li>
<li><strong>Histone H2B and H2B</strong> <strong>modifications </strong>(serine phosphorylation, lysine acetylation)</li>
<li><strong>Histone H3 and H3 modifications </strong>(lysine methylation (mono-, di- and tri-methylated), lysine acetylation, serine phosphorylation, threonine phosphorylation, arginine methylation (mono-methylated, symmetrically and asymmetrically di-methylated))</li>
<li><strong>Histone H4 and H4 modifications (</strong>lysine methylation (mono-, di- and tri-methylated), lysine acetylation, arginine methylation (mono-methylated and symmetrically di-methylated), serine phosphorylation )</li>
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<p><span style="font-weight: 400;"><strong>HDAC's HAT's, HMT's and other</strong> <strong>enzymes</strong> which modify histones can be found in the category <a href="../categories/chromatin-modifying-proteins-histone-transferase">Histone modifying enzymes</a><br /></span></p>
<p><span style="font-weight: 400;"> Diagenode’s highly validated antibodies:</span></p>
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<li><span style="font-weight: 400;"> Highly sensitive and specific</span></li>
<li><span style="font-weight: 400;"> Cost-effective (requires less antibody per reaction)</span></li>
<li><span style="font-weight: 400;"> Batch-specific data is available on the website</span></li>
<li><span style="font-weight: 400;"> Expert technical support</span></li>
<li><span style="font-weight: 400;"> Sample sizes available</span></li>
<li><span style="font-weight: 400;"> 100% satisfaction guarantee</span></li>
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<p><strong>ChIP-seq profile</strong> of active (H3K4me3 and H3K36me3) and inactive (H3K27me3) marks using Diagenode antibodies.</p>
<img src="https://www.diagenode.com/img/categories/antibodies/chip-seq-grade-antibodies.png" /></div>
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<p><small> ChIP was performed on sheared chromatin from 100,000 K562 cells using iDeal ChIP-seq kit for Histones (cat. No. C01010051) with 1 µg of the Diagenode antibodies against H3K27me3 (cat. No. C15410195) and H3K4me3 (cat. No. C15410003), and 0.5 µg of the antibody against H3K36me3 (cat. No. C15410192). The IP'd DNA was subsequently analysed on an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. The figure shows the signal distribution along the complete sequence of human chromosome 3, a zoomin to a 10 Mb region and a further zoomin to a 1.5 Mb region. </small></p>
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<p>Diagenode’s highly validated antibodies:</p>
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<li>Highly sensitive and specific</li>
<li>Cost-effective (requires less antibody per reaction)</li>
<li>Batch-specific data is available on the website</li>
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<p>Diagenode has partnered with leading epigenetics experts and numerous epigenetics consortiums to bring to you a validated and comprehensive collection of epigenetic antibodies. As an expert in epigenetics, we are committed to offering highly-specific antibodies validated for ChIP/ChIP-seq and many other applications. All batch-specific validation data is available on our website.<br /><a href="../categories/antibodies">Read about our expertise in antibody production</a>.</p>
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<p><span style="font-weight: 400;">Diagenode’s highly validated antibodies:</span></p>
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<p><br />Chromatin immunoprecipitation (<b>ChIP</b>) is a technique to study the associations of proteins with the specific genomic regions in intact cells. One of the most important steps of this protocol is the immunoprecipitation of targeted protein using the antibody specifically recognizing it. The quality of antibodies used in ChIP is essential for the success of the experiment. Diagenode offers extensively validated ChIP-grade antibodies, confirmed for their specificity, and high level of performance in ChIP. Each batch is validated, and batch-specific data are available on the website.</p>
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<p><strong>ChIP results</strong> obtained with the antibody directed against H3K4me3 (Cat. No. <a href="../p/h3k4me3-polyclonal-antibody-premium-50-ug-50-ul">C15410003</a>). </p>
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<p>Our aim at Diagenode is to offer the largest collection of highly specific <strong>ChIP-grade antibodies</strong>. We add new antibodies monthly. Find your ChIP-grade antibody in the list below and check more information about tested applications, extensive validation data, and product information.</p>',
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'description' => '<p style="text-align: justify;"><span>Epigenetic research tools have evolved over time from endpoint PCR to qPCR to the analyses of large sets of genome-wide sequencing data. ChIP sequencing (ChIP-seq) has now become the gold standard method for chromatin studies, given the accuracy and coverage scale of the approach over other methods. Successful ChIP-seq, however, requires a higher level of experimental accuracy and consistency in all steps of ChIP than ever before. Particularly crucial is the quality of ChIP antibodies. </span></p>',
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'name' => 'NuA4 and H2A.Z control environmental responses and autotrophicgrowth in Arabidopsis',
'authors' => 'Bieluszewski T. et al.',
'description' => '<p>Nucleosomal acetyltransferase of H4 (NuA4) is an essential transcriptional coactivator in eukaryotes, but remains poorly characterized in plants. Here, we describe Arabidopsis homologs of the NuA4 scaffold proteins Enhancer of Polycomb-Like 1 (AtEPL1) and Esa1-Associated Factor 1 (AtEAF1). Loss of AtEAF1 results in inhibition of growth and chloroplast development. These effects are stronger in the Atepl1 mutant and are further enhanced by loss of Golden2-Like (GLK) transcription factors, suggesting that NuA4 activates nuclear plastid genes alongside GLK. We demonstrate that AtEPL1 is necessary for nucleosomal acetylation of histones H4 and H2A.Z by NuA4 in vitro. These chromatin marks are diminished genome-wide in Atepl1, while another active chromatin mark, H3K9 acetylation (H3K9ac), is locally enhanced. Expression of many chloroplast-related genes depends on NuA4, as they are downregulated with loss of H4ac and H2A.Zac. Finally, we demonstrate that NuA4 promotes H2A.Z deposition and by doing so prevents spurious activation of stress response genes.</p>',
'date' => '2022-01-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/35022409',
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'name' => 'Neonatal exposure to hyperoxia leads to persistent disturbances in pulmonary histone signatures associated with NOS3 and STAT3 in a mouse model.',
'authors' => 'Chao CM, van den Bruck R, Lork S, Merkle J, Krampen L, Weil PP, Aydin M, Bellusci S, Jenke AC, Postberg J',
'description' => '<p>Background: Early pulmonary oxygen exposure is one of the most important factors implicated in the development of bronchopulmonary dysplasia (BPD). Methods: Here, we analyzed short- and long-term effects of neonatal hyperoxia on NOS3 and STAT3 expression and corresponding epigenetic signatures using a hyperoxia-based mouse model of BPD. Results: Early hyperoxia exposure led to a significant increase in NOS3 (median fold change × 2.37, IQR 1.54-3.68) and STAT3 (median fold change × 2.83, IQR 2.21-3.88) mRNA levels in pulmonary endothelial cells with corresponding changes in histone modification patterns such as H2aZac and H3K9ac hyperacetylation at the respective gene loci. No complete restoration in histone signatures at these loci was observed, and responsivity to later hyperoxia was altered in mouse lungs. In vitro, histone signatures in human aortic endothelial cells (HAEC) remained altered for several weeks after an initial long-term exposure to trichostatin A. This was associated with a substantial increase in baseline eNOS (median 27.2, IQR 22.3-35.6) and STAT3α (median 5.8, IQR 4.8-7.3) mRNA levels with a subsequent significant reduction in eNOS expression upon exposure to hypoxia. Conclusions: Early hyperoxia induced permanent changes in histones signatures at the NOS3 and STAT3 gene locus might partly explain the altered vascular response patterns in children with BPD.</p>',
'date' => '2018-01-01',
'pmid' => 'http://www.pubmed.gov/29581793',
'doi' => '10.1186/s13148-018-0469-0',
'modified' => '2019-02-15 21:45:12',
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'name' => 'CpG signalling, H2A.Z/H3 acetylation and microRNA-mediated deferred self-attenuation orchestrate foetal NOS3 expression.',
'authors' => 'Postberg J, Kanders M, Forcob S, Willems R, Orth V, Hensel KO, Weil PP, Wirth S, Jenke AC',
'description' => 'BACKGROUND: An adverse intrauterine environment leads to permanent physiological changes including vascular tone regulation, potentially influencing the risk for adult vascular diseases. We therefore aimed to monitor responsive NOS3 expression in human umbilical artery endothelial cells (HUAEC) and to study the underlying epigenetic signatures involved in its regulation. RESULTS: NOS3 and STAT3 mRNA levels were elevated in HUAEC of patients who suffered from placental insufficiency. 5-hydroxymethylcytosine, H3K9ac and Histone 2A (H2A).Zac at the NOS3 transcription start site directly correlated with NOS3 mRNA levels. Concomitantly, we observed entangled histone acetylation patterns and NOS3 response upon hypoxic conditions in vitro. Knock-down of either NOS3 or STAT3 by RNAi provided evidence for a functional NOS3/STAT3 relationship. Moreover, we recognized massive turnover of Stat3 at a discrete binding site in the NOS3 promoter. Interestingly, induced hyperacetylation resulted in short-termed increase of NOS3 mRNA followed by deferred decrease indicating that NOS3 expression could become self-attenuated by co-expressed intronic 27 nt-ncRNA. Reporter assay results and phylogenetic analyses enabled us to propose a novel model for STAT3-3'-UTR targeting by this 27-nt-ncRNA. CONCLUSIONS: An adverse intrauterine environment leads to adaptive changes of NOS3 expression. Apparently, a rapid NOS3 self-limiting response upon ectopic triggers co-exists with longer termed expression changes in response to placental insufficiency involving differential epigenetic signatures. Their persistence might contribute to impaired vascular endothelial response and consequently increase the risk of cardiovascular disease later in life.',
'date' => '2015-01-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/25699114',
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'id' => '2259',
'antibody_id' => '105',
'name' => 'H2A.Zac Antibody',
'description' => '<p><span>Polyclonal antibody raised in rabbit against histone <strong>H2A.Z acetylated at lysines 4, 7 and 11,</strong> using a KLH-conjugated synthetic peptide.</span></p>',
'label1' => 'Validation Data',
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<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP.jpg" /></center></div>
<div class="small-6 columns">
<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<div class="small-12 columns"><center>A.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-A.jpg" width="700" /></center><center>B.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" width="700" /></center><center>C.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-C.jpg" width="700" /></center>
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<center>D.<img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-D.jpg" width="700" /></center></div>
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<div class="row">
<div class="small-12 columns">
<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<div class="row">
<div class="small-6 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_ELISA.jpg" /></center></div>
<div class="small-6 columns">
<p><strong>Figure 3. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (cat. No. C15410173). The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:265,000.</p>
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<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_DB.jpg" width="220" /></center></div>
<div class="small-8 columns">
<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
<p></p>
<p></p>
<p></p>
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<div class="small-4 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_WB.jpg" /></center></div>
<div class="small-8 columns">
<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<div class="row">
<div class="small-12 columns"><center><img src="https://www.diagenode.com/img/product/antibodies/C15410173_IF.jpg" width="700" /></center></div>
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<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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'info2' => '<p>Histones are the main constituents of the protein part of chromosomes of eukaryotic cells. They are rich in the amino acids arginine and lysine and have been greatly conserved during evolution. Histones pack the DNA into tight masses of chromatin. Two core histones of each class H2A, H2B, H3 and H4 assemble and are wrapped by 146 base pairs of DNA to form one octameric nucleosome. Histone tails undergo numerous post-translational modifications, which either directly or indirectly alter chromatin structure to facilitate transcriptional activation or repression or other nuclear processes. In addition to the genetic code, combinations of the different histone modifications reveal the so-called "histone code". Histone methylation and demethylation is dynamically regulated by respectively histone methyl transferases and histone demethylases. Acetylation of the histone H2A variant H2A.Z is associated with the promoters of active genes.</p>',
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'format' => '50 μg',
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'slug' => 'h2a-zac-polyclonal-antibody-classic-50-mg-72-ml',
'meta_title' => 'H2A.Zac Antibody - ChIP-seq Grade (C15410173) | Diagenode',
'meta_keywords' => '',
'meta_description' => 'H2A.Zac (Histone H2A.Z acetylated at lysines 4, 7 and 11) Polyclonal Antibody validated in ChIP-seq, ChIP-qPCR, DB, IF and ELISA. Batch-specific data available on the website. Sample size available.',
'modified' => '2024-01-17 16:35:59',
'created' => '2015-06-29 14:08:20'
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<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP.jpg" alt="H2A.Zac Antibody ChIP Grade" /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 1 million HeLaS3 cells using the “Auto Histone ChIP-seq” kit (Cat. No. AB-Auto02-A100) on the SX-8G IP-Star automated system. A titration of the antibody consisting of 1, 2, 5 and 10 μg per ChIP experiment was analysed. IgG (2 μg/ IP) was used as negative IP control. QPCR was performed using primers specific for the promoters of the ACTB and EIF4A2 genes, used as positive control targets and for the coding region of the MYT1 gene, used as a negative control target. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA). These results confirm the observation that acetylation of H2A.Z is present at active promoters. </small></p>
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<div class="row">
<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-A.jpg" alt="H2A.Zac Antibody for ChIP" /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br /> ChIP was performed with 1 μg of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173-050) on sheared chromatin from 1 million HeLaS3 cells using the “iDeal ChIP-seq” kit (Cat. No. AB-001-0024). IgG (2 μg/IP) was used as a negative IP control. The IP’d DNA was analysed by QPCR as described above (figure 1A). The IP’d DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 1 shows the peak distribution along the complete sequence and a 600 kb region of the X-chromosome (figure 1B and C) and in 100 kb regions surrounding the EIF4A2, ACTB and GAPDH genes (figure 1D, E and F). These results clearly show an enrichment of the H2A.Z acetylation at the promoters of active genes. </small></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-B.jpg" alt="H2A.Zac Antibody for ChIP-seq" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-C.jpg" alt="H2A.Zac Antibody for ChIP-seq assay" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-D.jpg" alt="H2A.Zac Antibody validated in ChIP-seq" /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-E.jpg" alt="H2A.Zac Antibody ChIP-seq Grade " /></p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_CHIP-SEQ-F.jpg" alt="H2A.Zac Antibody for ChIP-seq" /></p>
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<div class="row">
<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_ELISA.jpg" alt="H2A.Zac Antibody ELISA validation" /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 3. Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (Cat. No. pAb-173-050), crude serum and flow through in antigen coated wells. The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:8,800. </small></p>
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<div class="row">
<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410173_DB.jpg" alt="H2A.Zac Antibody validated in Dot Blot" /></p>
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<p><small><strong> Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br /> A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (Cat. No. pAb-173- 050) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest. </small></p>
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<p><small><strong> Figure 5. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br /> HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. pAb-173-050) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right. </small></p>
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<p><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP assays were performed using HeLa cells, the Diagenode antibody against H2A.Zac (cat. No. C15410173) and optimized primer pairs for qPCR. ChIP was performed on sheared chromatin from 100,000 K562 cells using the iDeal ChIP-seq kit. A titration of the antibody consisting of 0.2, 0.5, 1 and 2 µg per ChIP experiment was analysed. IgG (1 µg/IP) was used as negative IP control. QPCR was performed using primers specific for the promoter of the EIF4A2 gene, used as positive control target and for the coding region of the MYT1 gene, and the Sat2 satellite repeat, used as negative control targets. Figure 1 shows the recovery (the relative amount of immunoprecipitated DNA compared to input DNA).</p>
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<p><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against H2A.Zac</strong><br />ChIP was performed with 0.5 µg of the Diagenode antibody against H2A.Zac (cat. No. C15410173) as described above. The IP'd DNA was subsequently analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer's instructions. The 36 bp tags were aligned to the human genome using the ELAND algorithm. Figure 2 shows the peak distribution along the complete sequence and a 1 Mb region of human chromosome 1 (figure 2A and B) and in two regions surrounding the GAPDH and the EIF4A2 positive control gene (figure 2C and D, respectively).</p>
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<p><strong>Figure 3. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against H2A.Zac (cat. No. C15410173). The antigen used was a peptide containing the histone modifications of interest. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the purified antibody was estimated to be 1:265,000.</p>
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<p><strong>Figure 4. Cross reactivity test using the Diagenode antibody directed against H2A.Zac</strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H2A.Zac (cat. No. C15410173) with peptides containing other histone acetylations and the unmodified H2A.Z sequence. One hundred to 0.2 pmol of the respective peptides were spotted on a membrane. The antibody was used at a dilution of 1:20,000. Figure 4 shows a high specificity of the antibody for the modification of interest.</p>
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<p><strong>Figure 5. Western blot analysis using the Diagenode antibody directed against H2A.Zac</strong><br />Western blot was performed on whole cell extracts (25 µg, lane 1) from HeLa cells, and on 1 µg of recombinant histone H2A, H2B, H3 and H4 (lane 2, 3, 4 and 5, respectively) using the Diagenode antibody against H2A.Zac (cat. No. C15410173). The antibody was diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right, the marker (in kDa) is shown on the left.</p>
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<p><strong>Figure 6. Immunofluorescence using the Diagenode antibody directed against H2A.Zac</strong><br />HeLa cells were stained with the Diagenode antibody against H2A.Zac (cat. No. C15410173) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labelled with the H2A.Zac antibody (left) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The middle panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</p>
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'meta_title' => 'ChIP Quantitative PCR Antibodies (ChIP-qPCR) | Diagenode',
'modified' => '2016-01-20 11:30:24',
'created' => '2015-10-20 11:45:36',
'locale' => 'jpn'
)
$description = ''
$name = 'ChIP-qPCR (ab)'
$document = array(
'id' => '38',
'name' => 'Epigenetic Antibodies Brochure',
'description' => '<p>More than in any other immuoprecipitation assays, quality antibodies are critical tools in many epigenetics experiments. Since 10 years, Diagenode has developed the most stringent quality production available on the market for antibodies exclusively focused on epigenetic uses. All our antibodies have been qualified to work in epigenetic applications.</p>',
'image_id' => null,
'type' => 'Brochure',
'url' => 'files/brochures/Epigenetic_Antibodies_Brochure.pdf',
'slug' => 'epigenetic-antibodies-brochure',
'meta_keywords' => '',
'meta_description' => '',
'modified' => '2016-06-15 11:24:06',
'created' => '2015-07-03 16:05:27',
'ProductsDocument' => array(
'id' => '1307',
'product_id' => '2667',
'document_id' => '38'
)
)
$sds = array(
'id' => '3605',
'name' => 'SDS C15410173 H2A Zac Antibody BE nl',
'language' => 'nl',
'url' => 'files/SDS/H2A_Zac/SDS-C15410173-H2A_Zac_Antibody-BE-nl-GHS_2_0.pdf',
'countries' => 'BE',
'modified' => '2024-01-17 16:34:02',
'created' => '2024-01-17 16:34:02',
'ProductsSafetySheet' => array(
'id' => '5881',
'product_id' => '2667',
'safety_sheet_id' => '3605'
)
)
$publication = array(
'id' => '2613',
'name' => 'CpG signalling, H2A.Z/H3 acetylation and microRNA-mediated deferred self-attenuation orchestrate foetal NOS3 expression.',
'authors' => 'Postberg J, Kanders M, Forcob S, Willems R, Orth V, Hensel KO, Weil PP, Wirth S, Jenke AC',
'description' => 'BACKGROUND: An adverse intrauterine environment leads to permanent physiological changes including vascular tone regulation, potentially influencing the risk for adult vascular diseases. We therefore aimed to monitor responsive NOS3 expression in human umbilical artery endothelial cells (HUAEC) and to study the underlying epigenetic signatures involved in its regulation. RESULTS: NOS3 and STAT3 mRNA levels were elevated in HUAEC of patients who suffered from placental insufficiency. 5-hydroxymethylcytosine, H3K9ac and Histone 2A (H2A).Zac at the NOS3 transcription start site directly correlated with NOS3 mRNA levels. Concomitantly, we observed entangled histone acetylation patterns and NOS3 response upon hypoxic conditions in vitro. Knock-down of either NOS3 or STAT3 by RNAi provided evidence for a functional NOS3/STAT3 relationship. Moreover, we recognized massive turnover of Stat3 at a discrete binding site in the NOS3 promoter. Interestingly, induced hyperacetylation resulted in short-termed increase of NOS3 mRNA followed by deferred decrease indicating that NOS3 expression could become self-attenuated by co-expressed intronic 27 nt-ncRNA. Reporter assay results and phylogenetic analyses enabled us to propose a novel model for STAT3-3'-UTR targeting by this 27-nt-ncRNA. CONCLUSIONS: An adverse intrauterine environment leads to adaptive changes of NOS3 expression. Apparently, a rapid NOS3 self-limiting response upon ectopic triggers co-exists with longer termed expression changes in response to placental insufficiency involving differential epigenetic signatures. Their persistence might contribute to impaired vascular endothelial response and consequently increase the risk of cardiovascular disease later in life.',
'date' => '2015-01-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/25699114',
'doi' => '',
'modified' => '2015-07-24 15:39:05',
'created' => '2015-07-24 15:39:05',
'ProductsPublication' => array(
'id' => '249',
'product_id' => '2667',
'publication_id' => '2613'
)
)
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View::_evaluate() - CORE/Cake/View/View.php, line 971
View::_render() - CORE/Cake/View/View.php, line 933
View::render() - CORE/Cake/View/View.php, line 473
Controller::render() - CORE/Cake/Controller/Controller.php, line 963
ProductsController::slug() - APP/Controller/ProductsController.php, line 1052
ReflectionMethod::invokeArgs() - [internal], line ??
Controller::invokeAction() - CORE/Cake/Controller/Controller.php, line 491
Dispatcher::_invoke() - CORE/Cake/Routing/Dispatcher.php, line 193
Dispatcher::dispatch() - CORE/Cake/Routing/Dispatcher.php, line 167
[main] - APP/webroot/index.php, line 118
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