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'description' => '<p><span>As an alternative we offer the purified <a href="../p/h3k79me3-polyclonal-antibody-classic-50-ug-42-ul">H3K79me3 polyclonal antibody</a> (C15410068).<br /></span></p>
<p><span>Polyclonal antibody raised in rabbit against histone H3 containing the trimethylated lysine 79 (H3K79me3), using a KLH-conjugated synthetic peptide.</span></p>',
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<p><small><strong> Figure 1. Determination of the antibody titer </strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of Diagenode antibody directed against H3K79me3 (Cat. No. CS-068-100) in antigen coated wells. The antigen used was a peptide containing the histone modification of interest. By plotting the absorbance against the antibody dilution (Figure 1), the titer of the antibody was estimated to be 1:70,000. </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15310068_fig2.png" alt="Dot Blot" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong> Figure 2. Cross reactivity test of the Diagenode antibody directed against H3K79me3 </strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H3K79me3 (Cat. No. CS-068-100) with peptides containing other modifications of histone H3. These include mono- and dimethylation of the same lysine and mono-, di- and trimethylation of lysine 9, 27 and 36. One hundred to 0.2 pmol of the peptides were spotted on a membrane. The antibody was used at a dilution of 1:50,000. Figure 2 shows a high specificity of the antibody for the modification of interest. </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15310068_fig3.png" alt="Western Blot" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong> Figure 3. Western blot analysis using the Diagenode antibody directed against H3K79me3 </strong><br />Western blot was performed on histone extracts from HeLa cells (15 μg) with the Diagenode antibody against H3K79me3 (Cat. No. CS-068-100), diluted 1:500 in TBS-Tween containing 5% skimmed milk. The molecular weight marker (Bio-Rad, broad range biotinylated SDS-PAGE standard) is shown on the left, the location of the protein of interest is indicated on the right. </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15310068_fig4.png" alt="Immunofluorescence" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong> Figure 4. Immunofluorescence using the Diagenode antibody directed against H3K79me3 </strong><br />Mouse fibroblasts (NIH3T3 cells) were stained with the Diagenode antibody against H3K79me3 (Cat. No. CS- 068-100) and with DAPI. Cells were formaldehyde fixed, permeabilized with Triton X100 and blocked with PBS containing 2.5% BSA. Figure 4A: cells were immunofluorescently labeled with the H3K79me3 antibody (diluted 1:200 and incubated for 1 hour at room temperature) followed by goat anti-rabbit antibody conjugated to FITC. Figure 1B: staining of the nuclei with DAPI, which specifically labels DNA. Both antibody and DAPI staining are restricted to the nucleus. </small></p>
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<td>Fig 1</td>
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'description' => '<p><span>As an alternative we offer the purified <a href="../p/h3k79me3-polyclonal-antibody-classic-50-ug-42-ul">H3K79me3 polyclonal antibody</a> (C15410068).<br /></span></p>
<p><span>Polyclonal antibody raised in rabbit against histone H3 containing the trimethylated lysine 79 (H3K79me3), using a KLH-conjugated synthetic peptide.</span></p>',
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15310068_fig1.png" alt="ELISA" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong> Figure 1. Determination of the antibody titer </strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of Diagenode antibody directed against H3K79me3 (Cat. No. CS-068-100) in antigen coated wells. The antigen used was a peptide containing the histone modification of interest. By plotting the absorbance against the antibody dilution (Figure 1), the titer of the antibody was estimated to be 1:70,000. </small></p>
</div>
</div>
<div class="row">
<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15310068_fig2.png" alt="Dot Blot" style="display: block; margin-left: auto; margin-right: auto;" /></p>
</div>
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<p><small><strong> Figure 2. Cross reactivity test of the Diagenode antibody directed against H3K79me3 </strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H3K79me3 (Cat. No. CS-068-100) with peptides containing other modifications of histone H3. These include mono- and dimethylation of the same lysine and mono-, di- and trimethylation of lysine 9, 27 and 36. One hundred to 0.2 pmol of the peptides were spotted on a membrane. The antibody was used at a dilution of 1:50,000. Figure 2 shows a high specificity of the antibody for the modification of interest. </small></p>
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<div class="row">
<div class="small-3 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15310068_fig3.png" alt="Western Blot" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong> Figure 3. Western blot analysis using the Diagenode antibody directed against H3K79me3 </strong><br />Western blot was performed on histone extracts from HeLa cells (15 μg) with the Diagenode antibody against H3K79me3 (Cat. No. CS-068-100), diluted 1:500 in TBS-Tween containing 5% skimmed milk. The molecular weight marker (Bio-Rad, broad range biotinylated SDS-PAGE standard) is shown on the left, the location of the protein of interest is indicated on the right. </small></p>
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<p><small><strong> Figure 4. Immunofluorescence using the Diagenode antibody directed against H3K79me3 </strong><br />Mouse fibroblasts (NIH3T3 cells) were stained with the Diagenode antibody against H3K79me3 (Cat. No. CS- 068-100) and with DAPI. Cells were formaldehyde fixed, permeabilized with Triton X100 and blocked with PBS containing 2.5% BSA. Figure 4A: cells were immunofluorescently labeled with the H3K79me3 antibody (diluted 1:200 and incubated for 1 hour at room temperature) followed by goat anti-rabbit antibody conjugated to FITC. Figure 1B: staining of the nuclei with DAPI, which specifically labels DNA. Both antibody and DAPI staining are restricted to the nucleus. </small></p>
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<td>Fig 1</td>
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<td>Fig 2</td>
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<p>Learn more about: <a href="https://www.diagenode.com/applications/western-blot">Loading control, MW marker visualization</a><em>. <br /></em></p>
<p><em></em>Check our selection of antibodies validated in Western blot.</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>
<ul>
<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>
</ul>
<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><small><strong> Figure 1. Determination of the antibody titer </strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of Diagenode antibody directed against H3K79me3 (Cat. No. CS-068-100) in antigen coated wells. The antigen used was a peptide containing the histone modification of interest. By plotting the absorbance against the antibody dilution (Figure 1), the titer of the antibody was estimated to be 1:70,000. </small></p>
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<p><small><strong> Figure 3. Western blot analysis using the Diagenode antibody directed against H3K79me3 </strong><br />Western blot was performed on histone extracts from HeLa cells (15 μg) with the Diagenode antibody against H3K79me3 (Cat. No. CS-068-100), diluted 1:500 in TBS-Tween containing 5% skimmed milk. The molecular weight marker (Bio-Rad, broad range biotinylated SDS-PAGE standard) is shown on the left, the location of the protein of interest is indicated on the right. </small></p>
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<p><small><strong> Figure 4. Immunofluorescence using the Diagenode antibody directed against H3K79me3 </strong><br />Mouse fibroblasts (NIH3T3 cells) were stained with the Diagenode antibody against H3K79me3 (Cat. No. CS- 068-100) and with DAPI. Cells were formaldehyde fixed, permeabilized with Triton X100 and blocked with PBS containing 2.5% BSA. Figure 4A: cells were immunofluorescently labeled with the H3K79me3 antibody (diluted 1:200 and incubated for 1 hour at room temperature) followed by goat anti-rabbit antibody conjugated to FITC. Figure 1B: staining of the nuclei with DAPI, which specifically labels DNA. Both antibody and DAPI staining are restricted to the nucleus. </small></p>
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<td>Fig 1</td>
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<p><small><strong> Figure 2. Cross reactivity test of the Diagenode antibody directed against H3K79me3 </strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H3K79me3 (Cat. No. CS-068-100) with peptides containing other modifications of histone H3. These include mono- and dimethylation of the same lysine and mono-, di- and trimethylation of lysine 9, 27 and 36. One hundred to 0.2 pmol of the peptides were spotted on a membrane. The antibody was used at a dilution of 1:50,000. Figure 2 shows a high specificity of the antibody for the modification of interest. </small></p>
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<p><small><strong> Figure 3. Western blot analysis using the Diagenode antibody directed against H3K79me3 </strong><br />Western blot was performed on histone extracts from HeLa cells (15 μg) with the Diagenode antibody against H3K79me3 (Cat. No. CS-068-100), diluted 1:500 in TBS-Tween containing 5% skimmed milk. The molecular weight marker (Bio-Rad, broad range biotinylated SDS-PAGE standard) is shown on the left, the location of the protein of interest is indicated on the right. </small></p>
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<p><small><strong> Figure 4. Immunofluorescence using the Diagenode antibody directed against H3K79me3 </strong><br />Mouse fibroblasts (NIH3T3 cells) were stained with the Diagenode antibody against H3K79me3 (Cat. No. CS- 068-100) and with DAPI. Cells were formaldehyde fixed, permeabilized with Triton X100 and blocked with PBS containing 2.5% BSA. Figure 4A: cells were immunofluorescently labeled with the H3K79me3 antibody (diluted 1:200 and incubated for 1 hour at room temperature) followed by goat anti-rabbit antibody conjugated to FITC. Figure 1B: staining of the nuclei with DAPI, which specifically labels DNA. Both antibody and DAPI staining are restricted to the nucleus. </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. Trimethylation of histone H3 on K79 was shown to be more present at active promotors than at silent promotors.',
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<td>ELISA</td>
<td>1:500 - 1:1,000</td>
<td>Fig 1</td>
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<td>Dot Blotting</td>
<td>1:50,000</td>
<td>Fig 2</td>
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<p>Learn more about: <a href="https://www.diagenode.com/applications/western-blot">Loading control, MW marker visualization</a><em>. <br /></em></p>
<p><em></em>Check our selection of antibodies validated in Western blot.</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><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
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<p><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
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<p><small><strong> Figure 1. Determination of the antibody titer </strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of Diagenode antibody directed against H3K79me3 (Cat. No. CS-068-100) in antigen coated wells. The antigen used was a peptide containing the histone modification of interest. By plotting the absorbance against the antibody dilution (Figure 1), the titer of the antibody was estimated to be 1:70,000. </small></p>
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<p><small><strong> Figure 3. Western blot analysis using the Diagenode antibody directed against H3K79me3 </strong><br />Western blot was performed on histone extracts from HeLa cells (15 μg) with the Diagenode antibody against H3K79me3 (Cat. No. CS-068-100), diluted 1:500 in TBS-Tween containing 5% skimmed milk. The molecular weight marker (Bio-Rad, broad range biotinylated SDS-PAGE standard) is shown on the left, the location of the protein of interest is indicated on the right. </small></p>
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<p><small><strong> Figure 4. Immunofluorescence using the Diagenode antibody directed against H3K79me3 </strong><br />Mouse fibroblasts (NIH3T3 cells) were stained with the Diagenode antibody against H3K79me3 (Cat. No. CS- 068-100) and with DAPI. Cells were formaldehyde fixed, permeabilized with Triton X100 and blocked with PBS containing 2.5% BSA. Figure 4A: cells were immunofluorescently labeled with the H3K79me3 antibody (diluted 1:200 and incubated for 1 hour at room temperature) followed by goat anti-rabbit antibody conjugated to FITC. Figure 1B: staining of the nuclei with DAPI, which specifically labels DNA. Both antibody and DAPI staining are restricted to the nucleus. </small></p>
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<p><span>Polyclonal antibody raised in rabbit against histone H3 containing the trimethylated lysine 79 (H3K79me3), using a KLH-conjugated synthetic peptide.</span></p>',
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<p><small><strong> Figure 1. Determination of the antibody titer </strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of Diagenode antibody directed against H3K79me3 (Cat. No. CS-068-100) in antigen coated wells. The antigen used was a peptide containing the histone modification of interest. By plotting the absorbance against the antibody dilution (Figure 1), the titer of the antibody was estimated to be 1:70,000. </small></p>
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<div class="row">
<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15310068_fig2.png" alt="Dot Blot" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong> Figure 2. Cross reactivity test of the Diagenode antibody directed against H3K79me3 </strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H3K79me3 (Cat. No. CS-068-100) with peptides containing other modifications of histone H3. These include mono- and dimethylation of the same lysine and mono-, di- and trimethylation of lysine 9, 27 and 36. One hundred to 0.2 pmol of the peptides were spotted on a membrane. The antibody was used at a dilution of 1:50,000. Figure 2 shows a high specificity of the antibody for the modification of interest. </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15310068_fig3.png" alt="Western Blot" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong> Figure 3. Western blot analysis using the Diagenode antibody directed against H3K79me3 </strong><br />Western blot was performed on histone extracts from HeLa cells (15 μg) with the Diagenode antibody against H3K79me3 (Cat. No. CS-068-100), diluted 1:500 in TBS-Tween containing 5% skimmed milk. The molecular weight marker (Bio-Rad, broad range biotinylated SDS-PAGE standard) is shown on the left, the location of the protein of interest is indicated on the right. </small></p>
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<p><small><strong> Figure 4. Immunofluorescence using the Diagenode antibody directed against H3K79me3 </strong><br />Mouse fibroblasts (NIH3T3 cells) were stained with the Diagenode antibody against H3K79me3 (Cat. No. CS- 068-100) and with DAPI. Cells were formaldehyde fixed, permeabilized with Triton X100 and blocked with PBS containing 2.5% BSA. Figure 4A: cells were immunofluorescently labeled with the H3K79me3 antibody (diluted 1:200 and incubated for 1 hour at room temperature) followed by goat anti-rabbit antibody conjugated to FITC. Figure 1B: staining of the nuclei with DAPI, which specifically labels DNA. Both antibody and DAPI staining are restricted to the nucleus. </small></p>
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<td>Fig 1</td>
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<p>Learn more about: <a href="https://www.diagenode.com/applications/western-blot">Loading control, MW marker visualization</a><em>. <br /></em></p>
<p><em></em>Check our selection of antibodies validated in Western blot.</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>
<ul>
<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>
</ul>
<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><small><strong> Figure 1. Determination of the antibody titer </strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of Diagenode antibody directed against H3K79me3 (Cat. No. CS-068-100) in antigen coated wells. The antigen used was a peptide containing the histone modification of interest. By plotting the absorbance against the antibody dilution (Figure 1), the titer of the antibody was estimated to be 1:70,000. </small></p>
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<p><small><strong> Figure 2. Cross reactivity test of the Diagenode antibody directed against H3K79me3 </strong><br />A Dot Blot analysis was performed to test the cross reactivity of the Diagenode antibody against H3K79me3 (Cat. No. CS-068-100) with peptides containing other modifications of histone H3. These include mono- and dimethylation of the same lysine and mono-, di- and trimethylation of lysine 9, 27 and 36. One hundred to 0.2 pmol of the peptides were spotted on a membrane. The antibody was used at a dilution of 1:50,000. Figure 2 shows a high specificity of the antibody for the modification of interest. </small></p>
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<p><small><strong> Figure 3. Western blot analysis using the Diagenode antibody directed against H3K79me3 </strong><br />Western blot was performed on histone extracts from HeLa cells (15 μg) with the Diagenode antibody against H3K79me3 (Cat. No. CS-068-100), diluted 1:500 in TBS-Tween containing 5% skimmed milk. The molecular weight marker (Bio-Rad, broad range biotinylated SDS-PAGE standard) is shown on the left, the location of the protein of interest is indicated on the right. </small></p>
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<p><small><strong> Figure 4. Immunofluorescence using the Diagenode antibody directed against H3K79me3 </strong><br />Mouse fibroblasts (NIH3T3 cells) were stained with the Diagenode antibody against H3K79me3 (Cat. No. CS- 068-100) and with DAPI. Cells were formaldehyde fixed, permeabilized with Triton X100 and blocked with PBS containing 2.5% BSA. Figure 4A: cells were immunofluorescently labeled with the H3K79me3 antibody (diluted 1:200 and incubated for 1 hour at room temperature) followed by goat anti-rabbit antibody conjugated to FITC. Figure 1B: staining of the nuclei with DAPI, which specifically labels DNA. Both antibody and DAPI staining are restricted to the nucleus. </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15310068_fig3.png" alt="Western Blot" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong> Figure 3. Western blot analysis using the Diagenode antibody directed against H3K79me3 </strong><br />Western blot was performed on histone extracts from HeLa cells (15 μg) with the Diagenode antibody against H3K79me3 (Cat. No. CS-068-100), diluted 1:500 in TBS-Tween containing 5% skimmed milk. The molecular weight marker (Bio-Rad, broad range biotinylated SDS-PAGE standard) is shown on the left, the location of the protein of interest is indicated on the right. </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15310068_fig4.png" alt="Immunofluorescence" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong> Figure 4. Immunofluorescence using the Diagenode antibody directed against H3K79me3 </strong><br />Mouse fibroblasts (NIH3T3 cells) were stained with the Diagenode antibody against H3K79me3 (Cat. No. CS- 068-100) and with DAPI. Cells were formaldehyde fixed, permeabilized with Triton X100 and blocked with PBS containing 2.5% BSA. Figure 4A: cells were immunofluorescently labeled with the H3K79me3 antibody (diluted 1:200 and incubated for 1 hour at room temperature) followed by goat anti-rabbit antibody conjugated to FITC. Figure 1B: staining of the nuclei with DAPI, which specifically labels DNA. Both antibody and DAPI staining are restricted to the nucleus. </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. Trimethylation of histone H3 on K79 was shown to be more present at active promotors than at silent promotors.',
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<td>ELISA</td>
<td>1:500 - 1:1,000</td>
<td>Fig 1</td>
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<td>Dot Blotting</td>
<td>1:50,000</td>
<td>Fig 2</td>
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'description' => '<p><strong>Western blot</strong> : The quality of antibodies used in this technique is crucial for correct and specific protein identification. Diagenode offers huge selection of highly sensitive and specific western blot-validated antibodies.</p>
<p>Learn more about: <a href="https://www.diagenode.com/applications/western-blot">Loading control, MW marker visualization</a><em>. <br /></em></p>
<p><em></em>Check our selection of antibodies validated in Western blot.</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><span style="font-weight: 400;">Diagenode’s highly validated antibodies:</span></p>
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'description' => '<p>Chromatin structure and function is regulated by reader proteins recognizing histone modifications and/or histone variants. We recently identified that PWWP2A tightly binds to H2A.Z-containing nucleosomes and is involved in mitotic progression and cranial-facial development. Here, using in vitro assays, we show that distinct domains of PWWP2A mediate binding to free linker DNA as well as H3K36me3 nucleosomes. In vivo, PWWP2A strongly recognizes H2A.Z-containing regulatory regions and weakly binds H3K36me3-containing gene bodies. Further, PWWP2A binds to an MTA1-specific subcomplex of the NuRD complex (M1HR), which consists solely of MTA1, HDAC1, and RBBP4/7, and excludes CHD, GATAD2 and MBD proteins. Depletion of PWWP2A leads to an increase of acetylation levels on H3K27 as well as H2A.Z, presumably by impaired chromatin recruitment of M1HR. Thus, this study identifies PWWP2A as a complex chromatin-binding protein that serves to direct the deacetylase complex M1HR to H2A.Z-containing chromatin, thereby promoting changes in histone acetylation levels.</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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<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>
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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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'name' => 'PWWP2A binds distinct chromatin moieties and interacts with an MTA1-specific core NuRD complex.',
'authors' => 'Link S, Spitzer RMM, Sana M, Torrado M, Völker-Albert MC, Keilhauer EC, Burgold T, Pünzeler S, Low JKK, Lindström I, Nist A, Regnard C, Stiewe T, Hendrich B, Imhof A, Mann M, Mackay JP, Bartkuhn M, Hake SB',
'description' => '<p>Chromatin structure and function is regulated by reader proteins recognizing histone modifications and/or histone variants. We recently identified that PWWP2A tightly binds to H2A.Z-containing nucleosomes and is involved in mitotic progression and cranial-facial development. Here, using in vitro assays, we show that distinct domains of PWWP2A mediate binding to free linker DNA as well as H3K36me3 nucleosomes. In vivo, PWWP2A strongly recognizes H2A.Z-containing regulatory regions and weakly binds H3K36me3-containing gene bodies. Further, PWWP2A binds to an MTA1-specific subcomplex of the NuRD complex (M1HR), which consists solely of MTA1, HDAC1, and RBBP4/7, and excludes CHD, GATAD2 and MBD proteins. Depletion of PWWP2A leads to an increase of acetylation levels on H3K27 as well as H2A.Z, presumably by impaired chromatin recruitment of M1HR. Thus, this study identifies PWWP2A as a complex chromatin-binding protein that serves to direct the deacetylase complex M1HR to H2A.Z-containing chromatin, thereby promoting changes in histone acetylation levels.</p>',
'date' => '2018-10-16',
'pmid' => 'http://www.pubmed.gov/30327463',
'doi' => '10.1038/s41467-018-06665-5',
'modified' => '2019-07-22 09:17:39',
'created' => '2019-03-21 14:12:08',
'ProductsPublication' => array(
'id' => '3364',
'product_id' => '2069',
'publication_id' => '3556'
)
)
$externalLink = ' <a href="http://www.pubmed.gov/30327463" target="_blank"><i class="fa fa-external-link"></i></a>'include - APP/View/Products/view.ctp, line 755
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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