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<p><small><strong>A.</strong> ChIP-seq signals on chromosome 19</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2A.png" alt="RARA Antibody ChIP-seq Grade" /> <br /><small><strong>B.</strong> 50 kb region on chromosome 19 surrounding the HMHA1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2B.png" alt="RARA Antibody for ChIP-seq" /><br /><small><strong>C. </strong>50 kb region on chromosome 19 surrounding the PRAM1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2C.png" alt="RARA Antibody validated in ChIP-seq" /></p>
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<p><small><strong>Figure 1. ChIP-seq results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP was performed as described above and the IP’d DNA was analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 32 bp tags were aligned to the human reference genome (hg18) using the ELAND algorithm. Figure 2 shows the results of the complete chromosome 19 and two 50 kb region surrounding the HMHA1 and PRAM1 genes, respectively. </small></p>
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<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</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 human RARA (Cat. No. CS-155-100). The plates were coated with the peptides used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:2,400.</small></p>
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<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-wb.png" alt="RARA Antibody validated in Western Blot" /></p>
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<p><small> <strong>Figure 4. Western blot analysis using the Diagenode antibody directed against RARA</strong><br />Human embryonic kidney cells (293T) were transfected with a RARA construct (lane 2) or with a negative control construct (lane 1) and analysed by Western blot using the Diagenode antibody against RARA (Cat. No. CS-155-100), diluted 1:750 in BSA/PBS- Tween. The molecular weight marker (in kDa) 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>A.</strong> ChIP-seq signals on chromosome 19</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2A.png" alt="RARA Antibody ChIP-seq Grade" /> <br /><small><strong>B.</strong> 50 kb region on chromosome 19 surrounding the HMHA1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2B.png" alt="RARA Antibody for ChIP-seq" /><br /><small><strong>C. </strong>50 kb region on chromosome 19 surrounding the PRAM1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2C.png" alt="RARA Antibody validated in ChIP-seq" /></p>
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<p><small><strong>Figure 1. ChIP-seq results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP was performed as described above and the IP’d DNA was analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 32 bp tags were aligned to the human reference genome (hg18) using the ELAND algorithm. Figure 2 shows the results of the complete chromosome 19 and two 50 kb region surrounding the HMHA1 and PRAM1 genes, respectively. </small></p>
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<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-chip.png" alt="RARA Antibody ChIP Grade" /></p>
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<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</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 human RARA (Cat. No. CS-155-100). The plates were coated with the peptides used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:2,400.</small></p>
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<p><small> <strong>Figure 4. Western blot analysis using the Diagenode antibody directed against RARA</strong><br />Human embryonic kidney cells (293T) were transfected with a RARA construct (lane 2) or with a negative control construct (lane 1) and analysed by Western blot using the Diagenode antibody against RARA (Cat. No. CS-155-100), diluted 1:750 in BSA/PBS- Tween. The molecular weight marker (in kDa) is shown on the left; the location of the protein of interest is indicated on the right.</small></p>
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<td>ChIP/ChIP-seq <sup>*</sup></td>
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<p><small><strong>Figure 1. ChIP-seq results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP was performed as described above and the IP’d DNA was analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 32 bp tags were aligned to the human reference genome (hg18) using the ELAND algorithm. Figure 2 shows the results of the complete chromosome 19 and two 50 kb region surrounding the HMHA1 and PRAM1 genes, respectively. </small></p>
</div>
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<div class="row">
<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-chip.png" alt="RARA Antibody ChIP Grade" /></p>
<p class="text-center"></p>
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<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</small></p>
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<div class="row">
<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-elisa.png" alt="RARA Antibody ELISA validation" /></p>
<p class="text-center"></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 human RARA (Cat. No. CS-155-100). The plates were coated with the peptides used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:2,400.</small></p>
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<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-wb.png" alt="RARA Antibody validated in Western Blot" /></p>
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<div class="small-6 columns">
<p><small> <strong>Figure 4. Western blot analysis using the Diagenode antibody directed against RARA</strong><br />Human embryonic kidney cells (293T) were transfected with a RARA construct (lane 2) or with a negative control construct (lane 1) and analysed by Western blot using the Diagenode antibody against RARA (Cat. No. CS-155-100), diluted 1:750 in BSA/PBS- Tween. The molecular weight marker (in kDa) is shown on the left; the location of the protein of interest is indicated on the right.</small></p>
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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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'meta_keywords' => ' Western Blot Antibodies ,western blot protocol,Western Blotting Products,Polyclonal antibodies ,monoclonal antibodies ',
'meta_description' => 'Diagenode offers a wide range of antibodies and technical support for western blot applications',
'meta_title' => ' Western Blot - Monoclonal antibody - Polyclonal antibody | Diagenode',
'modified' => '2016-04-26 12:44:51',
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'slug' => 'chip-seq-antibodies',
'meta_keywords' => 'Chromatin Immunoprecipitation Sequencing,ChIP-Seq,ChIP-seq grade antibodies,DNA purification,qPCR,Shearing of chromatin',
'meta_description' => 'Diagenode offers a wide range of antibodies and technical support for ChIP Sequencing applications',
'meta_title' => 'ChIP Sequencing Antibodies (ChIP-Seq) | Diagenode',
'modified' => '2016-01-20 11:06:19',
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'slug' => 'chip-qpcr-antibodies',
'meta_keywords' => 'Chromatin Immunoprecipitation Sequencing,ChIP-Seq,ChIP-seq grade antibodies,DNA purification,qPCR,Shearing of chromatin',
'meta_description' => 'Diagenode offers a wide range of antibodies and technical support for ChIP-qPCR applications',
'meta_title' => 'ChIP Quantitative PCR Antibodies (ChIP-qPCR) | Diagenode',
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'description' => '<p><span style="font-weight: 400;">The list of Diagenode’s highly specific antibodies for transcription studies includes the antibodies against many transcription factors and nuclear receptors. Check the list below to see our targets.</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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'meta_keywords' => ' Transcription factor antibodies,monoclonal antibodies,polyclonal antibodies',
'meta_description' => 'Diagenode offers polyclonal and monoclonal antibodies for Transcription studie',
'meta_title' => 'Transcription factor Antibodies | Diagenode',
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'description' => '<p><b>Unparalleled ChIP-Seq results with the most rigorously validated antibodies</b></p>
<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>
</div>
</div>
<p>Diagenode’s highly validated antibodies:</p>
<ul>
<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>
<li>Expert technical support</li>
<li>Sample sizes available</li>
<li>100% satisfaction guarantee</li>
</ul>',
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'meta_keywords' => 'ChIP-seq grade antibodies,polyclonal antibody,WB, ELISA, ChIP-seq (ab), ChIP-qPCR (ab)',
'meta_description' => 'Diagenode Offers Wide Range of Validated ChIP-Seq Grade Antibodies for Unparalleled ChIP-Seq Results',
'meta_title' => 'Chromatin Immunoprecipitation ChIP-Seq Grade Antibodies | Diagenode',
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'name' => 'All antibodies',
'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>
<ul>
<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>
<li>Expert technical support</li>
<li>Sample sizes available</li>
<li>100% satisfaction guarantee</li>
</ul>',
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'slug' => 'all-antibodies',
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'meta_keywords' => 'Antibodies,Premium Antibodies,Classic,Pioneer',
'meta_description' => 'Diagenode Offers Strict quality standards with Rigorous QC and validated Antibodies. Classified based on level of validation for flexibility of Application. Comprehensive selection of histone and non-histone Antibodies',
'meta_title' => 'Diagenode's selection of Antibodies is exclusively dedicated for Epigenetic Research | Diagenode',
'modified' => '2019-07-03 10:55:44',
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'name' => 'ChIP-grade antibodies',
'description' => '<div class="row">
<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>
</div>
</div>
<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>
<div class="row">
<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>
<div class="small-12 medium-6 large-6 columns">
<p></p>
<p></p>
<p></p>
</div>
</div>
<p></p>
<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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'meta_description' => 'Diagenode Offers Extensively Validated ChIP-Grade Antibodies, Confirmed for their Specificity, and high level of Performance in Chromatin Immunoprecipitation ChIP',
'meta_title' => 'Chromatin immunoprecipitation ChIP-grade antibodies | Diagenode',
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'name' => 'Datasheet RARA CS-155-100',
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'type' => 'Datasheet',
'url' => 'files/products/antibodies/Datasheet-rara-C15310155.pdf',
'slug' => 'datasheet-rara-cs-155-100',
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'id' => '11',
'name' => 'Antibodies you can trust',
'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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'slug' => 'antibodies-you-can-trust-poster',
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(int) 2 => 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',
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'slug' => 'epigenetic-antibodies-brochure',
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'modified' => '2020-11-27 07:04:40',
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'id' => '4840',
'name' => 'ALDH1A1 promotes PARP inhibitor resistance by enhancing retinoic acidreceptor-mediated DNA polymerase θ expression.',
'authors' => 'Lavudi K. et al.',
'description' => '<p>Poly (ADP-ribose) Polymerase (PARP) inhibitors (PARPi) have been approved for both frontline and recurrent setting in ovarian cancer with homologous recombination (HR) repair deficiency. However, more than 40\% of BRCA1/2-mutated ovarian cancer lack the initial response to PARPi treatment, and the majority of those that initially respond eventually develop resistance. Our previous study has demonstrated that increased expression of aldehyde dehydrogenase 1A1 (ALDH1A1) contributes to PARPi resistance in BRCA2-mutated ovarian cancer cells by enhancing microhomology-mediated end joining (MMEJ) but the mechanism remains unknown. Here, we find that ALDH1A1 enhances the expression of DNA polymerase θ (Polθ, encoded by the POLQ gene) in ovarian cancer cells. Furthermore, we demonstrate that the retinoic acid (RA) pathway is involved in the transcription activation of the POLQ gene. The RA receptor (RAR) can bind to the retinoic acid response element (RARE) located in the promoter of the POLQ gene, promoting transcription activation-related histone modification in the presence of RA. Given that ALDH1A1 catalyzes the biosynthesis of RA, we conclude that ALDH1A1 promotes POLQ expression via the activation of the RA signaling pathway. Finally, using a clinically-relevant patient-derived organoid (PDO) model, we find that ALDH1A1 inhibition by the pharmacological inhibitor NCT-505 in combination with the PARP inhibitor olaparib synergistically reduce the cell viability of PDOs carrying BRCA1/2 mutation and positive ALDH1A1 expression. In summary, our study elucidates a new mechanism contributing to PARPi resistance in HR-deficient ovarian cancer and shows the therapeutic potential of combining PARPi and ALDH1A1 inhibition in treating these patients.</p>',
'date' => '2023-07-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/37429899',
'doi' => '10.1038/s41698-023-00411-x',
'modified' => '2023-08-01 14:02:21',
'created' => '2023-08-01 15:59:38',
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(int) 1 => array(
'id' => '4479',
'name' => 'Systems-biology analysis of rheumatoid arthritis fibroblast-likesynoviocytes implicates cell line-specific transcription factor function.',
'authors' => 'Ainsworth R. I. et al.',
'description' => '<p>Rheumatoid arthritis (RA) is an immune-mediated disease affecting diarthrodial joints that remains an unmet medical need despite improved therapy. This limitation likely reflects the diversity of pathogenic pathways in RA, with individual patients demonstrating variable responses to targeted therapies. Better understanding of RA pathogenesis would be aided by a more complete characterization of the disease. To tackle this challenge, we develop and apply a systems biology approach to identify important transcription factors (TFs) in individual RA fibroblast-like synoviocyte (FLS) cell lines by integrating transcriptomic and epigenomic information. Based on the relative importance of the identified TFs, we stratify the RA FLS cell lines into two subtypes with distinct phenotypes and predicted active pathways. We biologically validate these predictions for the top subtype-specific TF RARα and demonstrate differential regulation of TGFβ signaling in the two subtypes. This study characterizes clusters of RA cell lines with distinctive TF biology by integrating transcriptomic and epigenomic data, which could pave the way towards a greater understanding of disease heterogeneity.</p>',
'date' => '2022-10-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/36266270',
'doi' => '10.1038/s41467-022-33785-w',
'modified' => '2022-11-18 12:24:55',
'created' => '2022-11-15 09:26:20',
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(int) 2 => array(
'id' => '4232',
'name' => 'Short-Chain Fatty Acids Calibrate RARα Activity RegulatingFood Sensitization',
'authors' => 'Yuan X. et al.',
'description' => '<p>Gut-microbiota dysbiosis links to allergic diseases. The mechanism of the exacerbation of food allergy caused by gut-microbiota dysbiosis remains unknown. Regulation of retinoic acid receptor alpha (RARα) signaling is critical for gut immune homeostasis. Here we clarified that RARα in dendritic cells (DCs) promotes Th2 cell differentiation. Antibiotics treatment stimulates retinoic acid signaling in mucosal DCs. We found microbiota metabolites short-chain fatty acids (SCFAs) maintain IGF-1 levels in serum and mesenteric lymph nodes. The IGF-1/Akt pathway is essential for regulating the transcription of genes targeted by RARα. And RARα in DCs affects type I interferon (IFN-I) responses through regulating transcription of IFN-α. Our study identifies SCFAs crosstalk with RARα in dendritic cells as a critical modulator that plays a core role in promoting Th2 cells differentiation at a state of modified/disturbed microbiome.</p>',
'date' => '2021-10-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/34721398',
'doi' => '10.3389/fimmu.2021.737658',
'modified' => '2022-05-19 16:52:41',
'created' => '2022-05-19 10:41:50',
'ProductsPublication' => array(
[maximum depth reached]
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),
(int) 3 => array(
'id' => '3614',
'name' => 'Retinoic Acid Receptor Alpha Represses a Th9 Transcriptional and Epigenomic Program to Reduce Allergic Pathology.',
'authors' => 'Schwartz DM, Farley TK, Richoz N, Yao C, Shih HY, Petermann F, Zhang Y, Sun HW, Hayes E, Mikami Y, Jiang K, Davis FP, Kanno Y, Milner JD, Siegel R, Laurence A, Meylan F, O'Shea JJ',
'description' => '<p>CD4 T helper (Th) differentiation is regulated by diverse inputs, including the vitamin A metabolite retinoic acid (RA). RA acts through its receptor RARα to repress transcription of inflammatory cytokines, but is also essential for Th-mediated immunity, indicating complex effects of RA on Th specification and the outcome of the immune response. We examined the impact of RA on the genome-wide transcriptional response during Th differentiation to multiple subsets. RA effects were subset-selective and were most significant in Th9 cells. RA globally antagonized Th9-promoting transcription factors and inhibited Th9 differentiation. RA directly targeted the extended Il9 locus and broadly modified the Th9 epigenome through RARα. RA-RARα activity limited murine Th9-associated pulmonary inflammation, and human allergic inflammation was associated with reduced expression of RA target genes. Thus, repression of the Th9 program is a major function of RA-RARα signaling in Th differentiation, arguing for a role for RA in interleukin 9 (IL-9) related diseases.</p>',
'date' => '2019-01-15',
'pmid' => 'http://www.pubmed.gov/30650370',
'doi' => '10.1016/j.immuni.2018.12.014',
'modified' => '2019-04-17 14:42:26',
'created' => '2019-04-16 12:25:30',
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[maximum depth reached]
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),
(int) 4 => array(
'id' => '3642',
'name' => 'Human retinoic acid-regulated CD161 regulatory T cells support wound repair in intestinal mucosa.',
'authors' => 'Povoleri GAM, Nova-Lamperti E, Scottà C, Fanelli G, Chen YC, Becker PD, Boardman D, Costantini B, Romano M, Pavlidis P, McGregor R, Pantazi E, Chauss D, Sun HW, Shih HY, Cousins DJ, Cooper N, Powell N, Kemper C, Pirooznia M, Laurence A, Kordasti S, Kazemi',
'description' => '<p>Repair of tissue damaged during inflammatory processes is key to the return of local homeostasis and restoration of epithelial integrity. Here we describe CD161 regulatory T (T) cells as a distinct, highly suppressive population of T cells that mediate wound healing. These T cells were enriched in intestinal lamina propria, particularly in Crohn's disease. CD161 T cells had an all-trans retinoic acid (ATRA)-regulated gene signature, and CD161 expression on T cells was induced by ATRA, which directly regulated the CD161 gene. CD161 was co-stimulatory, and ligation with the T cell antigen receptor induced cytokines that accelerated the wound healing of intestinal epithelial cells. We identified a transcription-factor network, including BACH2, RORγt, FOSL2, AP-1 and RUNX1, that controlled expression of the wound-healing program, and found a CD161 T cell signature in Crohn's disease mucosa associated with reduced inflammation. These findings identify CD161 T cells as a population involved in controlling the balance between inflammation and epithelial barrier healing in the gut.</p>',
'date' => '2018-12-01',
'pmid' => 'http://www.pubmed.gov/30397350',
'doi' => '10.1038/s41590-018-0230-z',
'modified' => '2019-06-07 10:19:42',
'created' => '2019-06-06 12:11:18',
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[maximum depth reached]
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),
(int) 5 => array(
'id' => '3158',
'name' => 'Elevated Fibroblast growth factor 21 (FGF21) in obese, insulin resistant states is normalised by the synthetic retinoid Fenretinide in mice',
'authors' => 'Morrice N. et al.',
'description' => '<p>Fibroblast growth factor 21 (FGF21) has emerged as an important beneficial regulator of glucose and lipid homeostasis but its levels are also abnormally increased in insulin-resistant states in rodents and humans. The synthetic retinoid Fenretinide inhibits obesity and improves glucose homeostasis in mice and has pleotropic effects on cellular pathways. To identify Fenretinide target genes, we performed unbiased RNA-seq analysis in liver from mice fed high-fat diet ± Fenretinide. Strikingly, Fgf21 was the most downregulated hepatic gene. Fenretinide normalised elevated levels of FGF21 in both high-fat diet-induced obese mice and in genetically obese-diabetic Lepr<sup>db</sup>mice. Moreover, Fenretinide-mediated suppression of FGF21 was independent of body weight loss or improved hepatic insulin sensitivity and importantly does not induce unhealthy metabolic complications. In mice which have substantially decreased endogenous retinoic acid biosynthesis, Fgf21 expression was increased, whereas acute pharmacological retinoid treatment decreased FGF21 levels. The repression of FGF21 levels by Fenretinide occurs by reduced binding of RARα and Pol-II at the Fgf21 promoter. We therefore establish Fgf21 as a novel gene target of Fenretinide signalling via a retinoid-dependent mechanism. These results may be of nutritional and therapeutic importance for the treatment of obesity and type-2 diabetes.</p>',
'date' => '2017-03-03',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/28256636',
'doi' => '',
'modified' => '2017-04-12 14:48:12',
'created' => '2017-04-12 14:48:12',
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[maximum depth reached]
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),
(int) 6 => array(
'id' => '2861',
'name' => 'The oncofusion protein FUS-ERG targets key hematopoietic regulators and modulates the all-trans retinoic acid signaling pathway in t(16;21) acute myeloid leukemia.',
'authors' => 'Sotoca AM1, Prange KH1, Reijnders B1, Mandoli A1, Nguyen LN1, Stunnenberg HG1, Martens JH',
'description' => '<p>The ETS transcription factor ERG has been implicated as a major regulator of both normal and aberrant hematopoiesis. In acute myeloid leukemias harboring t(16;21), ERG function is deregulated due to a fusion with FUS/TLS resulting in the expression of a FUS-ERG oncofusion protein. How this oncofusion protein deregulates the normal ERG transcription program is unclear. Here, we show that FUS-ERG acts in the context of a heptad of proteins (ERG, FLI1, GATA2, LYL1, LMO2, RUNX1 and TAL1) central to proper expression of genes involved in maintaining a stem cell hematopoietic phenotype. Moreover, in t(16;21) FUS-ERG co-occupies genomic regions bound by the nuclear receptor heterodimer RXR:RARA inhibiting target gene expression and interfering with hematopoietic differentiation. All-trans retinoic acid treatment of t(16;21) cells as well as FUS-ERG knockdown alleviate the myeloid-differentiation block. Together, the results suggest that FUS-ERG acts as a transcriptional repressor of the retinoic acid signaling pathway.</p>',
'date' => '2015-07-06',
'pmid' => 'http://www.ncbi.nlm.nih.gov/pubmed/26148230',
'doi' => '10.1038/onc.2015.261',
'modified' => '2016-03-17 10:01:30',
'created' => '2016-03-17 10:01:30',
'ProductsPublication' => array(
[maximum depth reached]
)
),
(int) 7 => array(
'id' => '2641',
'name' => 'Retinoic acid is essential for Th1 cell lineage stability and prevents transition to a Th17 cell program.',
'authors' => 'Brown CC, Esterhazy D, Sarde A, London M, Pullabhatla V, Osma-Garcia I, Al-Bader R, Ortiz C, Elgueta R, Arno M, de Rinaldis E, Mucida D, Lord GM, Noelle RJ',
'description' => 'CD4(+) T cells differentiate into phenotypically distinct T helper cells upon antigenic stimulation. Regulation of plasticity between these CD4(+) T-cell lineages is critical for immune homeostasis and prevention of autoimmune disease. However, the factors that regulate lineage stability are largely unknown. Here we investigate a role for retinoic acid (RA) in the regulation of lineage stability using T helper 1 (Th1) cells, traditionally considered the most phenotypically stable Th subset. We found that RA, through its receptor RARα, sustains stable expression of Th1 lineage specifying genes, as well as repressing genes that instruct Th17-cell fate. RA signaling is essential for limiting Th1-cell conversion into Th17 effectors and for preventing pathogenic Th17 responses in vivo. Our study identifies RA-RARα as a key component of the regulatory network governing maintenance and plasticity of Th1-cell fate and defines an additional pathway for the development of Th17 cells.',
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'description' => 'Many different molecular mechanisms have been associated with PML-RARalpha-dependent transformation of hematopoietic progenitors. Here, we identified high confidence PML-RARalpha binding sites in an acute promyelocytic leukemia (APL) cell line and in two APL primary blasts. We found colocalization of PML-RARalpha with RXR to the vast majority of these binding regions. Genome-wide epigenetic studies revealed that treatment with pharmacological doses of all-trans retinoic acid induces changes in H3 acetylation, but not H3K27me3, H3K9me3, or DNA methylation at the PML-RARalpha/RXR binding sites or at nearby target genes. Our results suggest that PML-RARalpha/RXR functions as a local chromatin modulator and that specific recruitment of histone deacetylase activities to genes important for hematopoietic differentiation, RAR signaling, and epigenetic control is crucial to its transforming potential.',
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<p><small><strong>Figure 1. ChIP-seq results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP was performed as described above and the IP’d DNA was analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 32 bp tags were aligned to the human reference genome (hg18) using the ELAND algorithm. Figure 2 shows the results of the complete chromosome 19 and two 50 kb region surrounding the HMHA1 and PRAM1 genes, respectively. </small></p>
</div>
</div>
<div class="row">
<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-chip.png" alt="RARA Antibody ChIP Grade" /></p>
<p class="text-center"></p>
</div>
<div class="small-6 columns">
<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</small></p>
</div>
</div>
<div class="row">
<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-elisa.png" alt="RARA Antibody ELISA validation" /></p>
<p class="text-center"></p>
</div>
<div class="small-6 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 human RARA (Cat. No. CS-155-100). The plates were coated with the peptides used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:2,400.</small></p>
</div>
</div>
<div class="row">
<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-wb.png" alt="RARA Antibody validated in Western Blot" /></p>
</div>
<div class="small-6 columns">
<p><small> <strong>Figure 4. Western blot analysis using the Diagenode antibody directed against RARA</strong><br />Human embryonic kidney cells (293T) were transfected with a RARA construct (lane 2) or with a negative control construct (lane 1) and analysed by Western blot using the Diagenode antibody against RARA (Cat. No. CS-155-100), diluted 1:750 in BSA/PBS- Tween. The molecular weight marker (in kDa) is shown on the left; the location of the protein of interest is indicated on the right.</small></p>
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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><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>
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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>
<ul>
<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>
<li>Expert technical support</li>
<li>Sample sizes available</li>
<li>100% satisfaction guarantee</li>
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<p><span style="font-weight: 400;">Diagenode’s highly validated antibodies:</span></p>
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<li>Sample sizes available</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>
<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>
<div class="row">
<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>
<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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'name' => 'ALDH1A1 promotes PARP inhibitor resistance by enhancing retinoic acidreceptor-mediated DNA polymerase θ expression.',
'authors' => 'Lavudi K. et al.',
'description' => '<p>Poly (ADP-ribose) Polymerase (PARP) inhibitors (PARPi) have been approved for both frontline and recurrent setting in ovarian cancer with homologous recombination (HR) repair deficiency. However, more than 40\% of BRCA1/2-mutated ovarian cancer lack the initial response to PARPi treatment, and the majority of those that initially respond eventually develop resistance. Our previous study has demonstrated that increased expression of aldehyde dehydrogenase 1A1 (ALDH1A1) contributes to PARPi resistance in BRCA2-mutated ovarian cancer cells by enhancing microhomology-mediated end joining (MMEJ) but the mechanism remains unknown. Here, we find that ALDH1A1 enhances the expression of DNA polymerase θ (Polθ, encoded by the POLQ gene) in ovarian cancer cells. Furthermore, we demonstrate that the retinoic acid (RA) pathway is involved in the transcription activation of the POLQ gene. The RA receptor (RAR) can bind to the retinoic acid response element (RARE) located in the promoter of the POLQ gene, promoting transcription activation-related histone modification in the presence of RA. Given that ALDH1A1 catalyzes the biosynthesis of RA, we conclude that ALDH1A1 promotes POLQ expression via the activation of the RA signaling pathway. Finally, using a clinically-relevant patient-derived organoid (PDO) model, we find that ALDH1A1 inhibition by the pharmacological inhibitor NCT-505 in combination with the PARP inhibitor olaparib synergistically reduce the cell viability of PDOs carrying BRCA1/2 mutation and positive ALDH1A1 expression. In summary, our study elucidates a new mechanism contributing to PARPi resistance in HR-deficient ovarian cancer and shows the therapeutic potential of combining PARPi and ALDH1A1 inhibition in treating these patients.</p>',
'date' => '2023-07-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/37429899',
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'name' => 'Systems-biology analysis of rheumatoid arthritis fibroblast-likesynoviocytes implicates cell line-specific transcription factor function.',
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'description' => '<p>Rheumatoid arthritis (RA) is an immune-mediated disease affecting diarthrodial joints that remains an unmet medical need despite improved therapy. This limitation likely reflects the diversity of pathogenic pathways in RA, with individual patients demonstrating variable responses to targeted therapies. Better understanding of RA pathogenesis would be aided by a more complete characterization of the disease. To tackle this challenge, we develop and apply a systems biology approach to identify important transcription factors (TFs) in individual RA fibroblast-like synoviocyte (FLS) cell lines by integrating transcriptomic and epigenomic information. Based on the relative importance of the identified TFs, we stratify the RA FLS cell lines into two subtypes with distinct phenotypes and predicted active pathways. We biologically validate these predictions for the top subtype-specific TF RARα and demonstrate differential regulation of TGFβ signaling in the two subtypes. This study characterizes clusters of RA cell lines with distinctive TF biology by integrating transcriptomic and epigenomic data, which could pave the way towards a greater understanding of disease heterogeneity.</p>',
'date' => '2022-10-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/36266270',
'doi' => '10.1038/s41467-022-33785-w',
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'id' => '4232',
'name' => 'Short-Chain Fatty Acids Calibrate RARα Activity RegulatingFood Sensitization',
'authors' => 'Yuan X. et al.',
'description' => '<p>Gut-microbiota dysbiosis links to allergic diseases. The mechanism of the exacerbation of food allergy caused by gut-microbiota dysbiosis remains unknown. Regulation of retinoic acid receptor alpha (RARα) signaling is critical for gut immune homeostasis. Here we clarified that RARα in dendritic cells (DCs) promotes Th2 cell differentiation. Antibiotics treatment stimulates retinoic acid signaling in mucosal DCs. We found microbiota metabolites short-chain fatty acids (SCFAs) maintain IGF-1 levels in serum and mesenteric lymph nodes. The IGF-1/Akt pathway is essential for regulating the transcription of genes targeted by RARα. And RARα in DCs affects type I interferon (IFN-I) responses through regulating transcription of IFN-α. Our study identifies SCFAs crosstalk with RARα in dendritic cells as a critical modulator that plays a core role in promoting Th2 cells differentiation at a state of modified/disturbed microbiome.</p>',
'date' => '2021-10-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/34721398',
'doi' => '10.3389/fimmu.2021.737658',
'modified' => '2022-05-19 16:52:41',
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(int) 3 => array(
'id' => '3614',
'name' => 'Retinoic Acid Receptor Alpha Represses a Th9 Transcriptional and Epigenomic Program to Reduce Allergic Pathology.',
'authors' => 'Schwartz DM, Farley TK, Richoz N, Yao C, Shih HY, Petermann F, Zhang Y, Sun HW, Hayes E, Mikami Y, Jiang K, Davis FP, Kanno Y, Milner JD, Siegel R, Laurence A, Meylan F, O'Shea JJ',
'description' => '<p>CD4 T helper (Th) differentiation is regulated by diverse inputs, including the vitamin A metabolite retinoic acid (RA). RA acts through its receptor RARα to repress transcription of inflammatory cytokines, but is also essential for Th-mediated immunity, indicating complex effects of RA on Th specification and the outcome of the immune response. We examined the impact of RA on the genome-wide transcriptional response during Th differentiation to multiple subsets. RA effects were subset-selective and were most significant in Th9 cells. RA globally antagonized Th9-promoting transcription factors and inhibited Th9 differentiation. RA directly targeted the extended Il9 locus and broadly modified the Th9 epigenome through RARα. RA-RARα activity limited murine Th9-associated pulmonary inflammation, and human allergic inflammation was associated with reduced expression of RA target genes. Thus, repression of the Th9 program is a major function of RA-RARα signaling in Th differentiation, arguing for a role for RA in interleukin 9 (IL-9) related diseases.</p>',
'date' => '2019-01-15',
'pmid' => 'http://www.pubmed.gov/30650370',
'doi' => '10.1016/j.immuni.2018.12.014',
'modified' => '2019-04-17 14:42:26',
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'id' => '3642',
'name' => 'Human retinoic acid-regulated CD161 regulatory T cells support wound repair in intestinal mucosa.',
'authors' => 'Povoleri GAM, Nova-Lamperti E, Scottà C, Fanelli G, Chen YC, Becker PD, Boardman D, Costantini B, Romano M, Pavlidis P, McGregor R, Pantazi E, Chauss D, Sun HW, Shih HY, Cousins DJ, Cooper N, Powell N, Kemper C, Pirooznia M, Laurence A, Kordasti S, Kazemi',
'description' => '<p>Repair of tissue damaged during inflammatory processes is key to the return of local homeostasis and restoration of epithelial integrity. Here we describe CD161 regulatory T (T) cells as a distinct, highly suppressive population of T cells that mediate wound healing. These T cells were enriched in intestinal lamina propria, particularly in Crohn's disease. CD161 T cells had an all-trans retinoic acid (ATRA)-regulated gene signature, and CD161 expression on T cells was induced by ATRA, which directly regulated the CD161 gene. CD161 was co-stimulatory, and ligation with the T cell antigen receptor induced cytokines that accelerated the wound healing of intestinal epithelial cells. We identified a transcription-factor network, including BACH2, RORγt, FOSL2, AP-1 and RUNX1, that controlled expression of the wound-healing program, and found a CD161 T cell signature in Crohn's disease mucosa associated with reduced inflammation. These findings identify CD161 T cells as a population involved in controlling the balance between inflammation and epithelial barrier healing in the gut.</p>',
'date' => '2018-12-01',
'pmid' => 'http://www.pubmed.gov/30397350',
'doi' => '10.1038/s41590-018-0230-z',
'modified' => '2019-06-07 10:19:42',
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'name' => 'Elevated Fibroblast growth factor 21 (FGF21) in obese, insulin resistant states is normalised by the synthetic retinoid Fenretinide in mice',
'authors' => 'Morrice N. et al.',
'description' => '<p>Fibroblast growth factor 21 (FGF21) has emerged as an important beneficial regulator of glucose and lipid homeostasis but its levels are also abnormally increased in insulin-resistant states in rodents and humans. The synthetic retinoid Fenretinide inhibits obesity and improves glucose homeostasis in mice and has pleotropic effects on cellular pathways. To identify Fenretinide target genes, we performed unbiased RNA-seq analysis in liver from mice fed high-fat diet ± Fenretinide. Strikingly, Fgf21 was the most downregulated hepatic gene. Fenretinide normalised elevated levels of FGF21 in both high-fat diet-induced obese mice and in genetically obese-diabetic Lepr<sup>db</sup>mice. Moreover, Fenretinide-mediated suppression of FGF21 was independent of body weight loss or improved hepatic insulin sensitivity and importantly does not induce unhealthy metabolic complications. In mice which have substantially decreased endogenous retinoic acid biosynthesis, Fgf21 expression was increased, whereas acute pharmacological retinoid treatment decreased FGF21 levels. The repression of FGF21 levels by Fenretinide occurs by reduced binding of RARα and Pol-II at the Fgf21 promoter. We therefore establish Fgf21 as a novel gene target of Fenretinide signalling via a retinoid-dependent mechanism. These results may be of nutritional and therapeutic importance for the treatment of obesity and type-2 diabetes.</p>',
'date' => '2017-03-03',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/28256636',
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'description' => '<p>The ETS transcription factor ERG has been implicated as a major regulator of both normal and aberrant hematopoiesis. In acute myeloid leukemias harboring t(16;21), ERG function is deregulated due to a fusion with FUS/TLS resulting in the expression of a FUS-ERG oncofusion protein. How this oncofusion protein deregulates the normal ERG transcription program is unclear. Here, we show that FUS-ERG acts in the context of a heptad of proteins (ERG, FLI1, GATA2, LYL1, LMO2, RUNX1 and TAL1) central to proper expression of genes involved in maintaining a stem cell hematopoietic phenotype. Moreover, in t(16;21) FUS-ERG co-occupies genomic regions bound by the nuclear receptor heterodimer RXR:RARA inhibiting target gene expression and interfering with hematopoietic differentiation. All-trans retinoic acid treatment of t(16;21) cells as well as FUS-ERG knockdown alleviate the myeloid-differentiation block. Together, the results suggest that FUS-ERG acts as a transcriptional repressor of the retinoic acid signaling pathway.</p>',
'date' => '2015-07-06',
'pmid' => 'http://www.ncbi.nlm.nih.gov/pubmed/26148230',
'doi' => '10.1038/onc.2015.261',
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'name' => 'Retinoic acid is essential for Th1 cell lineage stability and prevents transition to a Th17 cell program.',
'authors' => 'Brown CC, Esterhazy D, Sarde A, London M, Pullabhatla V, Osma-Garcia I, Al-Bader R, Ortiz C, Elgueta R, Arno M, de Rinaldis E, Mucida D, Lord GM, Noelle RJ',
'description' => 'CD4(+) T cells differentiate into phenotypically distinct T helper cells upon antigenic stimulation. Regulation of plasticity between these CD4(+) T-cell lineages is critical for immune homeostasis and prevention of autoimmune disease. However, the factors that regulate lineage stability are largely unknown. Here we investigate a role for retinoic acid (RA) in the regulation of lineage stability using T helper 1 (Th1) cells, traditionally considered the most phenotypically stable Th subset. We found that RA, through its receptor RARα, sustains stable expression of Th1 lineage specifying genes, as well as repressing genes that instruct Th17-cell fate. RA signaling is essential for limiting Th1-cell conversion into Th17 effectors and for preventing pathogenic Th17 responses in vivo. Our study identifies RA-RARα as a key component of the regulatory network governing maintenance and plasticity of Th1-cell fate and defines an additional pathway for the development of Th17 cells.',
'date' => '2015-03-17',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/25769610',
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'description' => 'Many different molecular mechanisms have been associated with PML-RARalpha-dependent transformation of hematopoietic progenitors. Here, we identified high confidence PML-RARalpha binding sites in an acute promyelocytic leukemia (APL) cell line and in two APL primary blasts. We found colocalization of PML-RARalpha with RXR to the vast majority of these binding regions. Genome-wide epigenetic studies revealed that treatment with pharmacological doses of all-trans retinoic acid induces changes in H3 acetylation, but not H3K27me3, H3K9me3, or DNA methylation at the PML-RARalpha/RXR binding sites or at nearby target genes. Our results suggest that PML-RARalpha/RXR functions as a local chromatin modulator and that specific recruitment of histone deacetylase activities to genes important for hematopoietic differentiation, RAR signaling, and epigenetic control is crucial to its transforming potential.',
'date' => '2010-02-17',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/20159609',
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<p><span>Polyclonal antibody raised in rabbit against human RARA (Retinoic Acid Receptor alpha) using two KLH-conjugated synthetic peptides containing sequences from the C-terminal region of the protein.</span></p>',
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<p><small><strong>A.</strong> ChIP-seq signals on chromosome 19</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2A.png" alt="RARA Antibody ChIP-seq Grade" /> <br /><small><strong>B.</strong> 50 kb region on chromosome 19 surrounding the HMHA1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2B.png" alt="RARA Antibody for ChIP-seq" /><br /><small><strong>C. </strong>50 kb region on chromosome 19 surrounding the PRAM1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2C.png" alt="RARA Antibody validated in ChIP-seq" /></p>
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<p><small><strong>Figure 1. ChIP-seq results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP was performed as described above and the IP’d DNA was analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 32 bp tags were aligned to the human reference genome (hg18) using the ELAND algorithm. Figure 2 shows the results of the complete chromosome 19 and two 50 kb region surrounding the HMHA1 and PRAM1 genes, respectively. </small></p>
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<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</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 human RARA (Cat. No. CS-155-100). The plates were coated with the peptides used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:2,400.</small></p>
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<p><small> <strong>Figure 4. Western blot analysis using the Diagenode antibody directed against RARA</strong><br />Human embryonic kidney cells (293T) were transfected with a RARA construct (lane 2) or with a negative control construct (lane 1) and analysed by Western blot using the Diagenode antibody against RARA (Cat. No. CS-155-100), diluted 1:750 in BSA/PBS- Tween. The molecular weight marker (in kDa) 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 1. ChIP-seq results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP was performed as described above and the IP’d DNA was analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 32 bp tags were aligned to the human reference genome (hg18) using the ELAND algorithm. Figure 2 shows the results of the complete chromosome 19 and two 50 kb region surrounding the HMHA1 and PRAM1 genes, respectively. </small></p>
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<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</small></p>
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<p><small><strong>A.</strong> ChIP-seq signals on chromosome 19</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2A.png" alt="RARA Antibody ChIP-seq Grade" /> <br /><small><strong>B.</strong> 50 kb region on chromosome 19 surrounding the HMHA1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2B.png" alt="RARA Antibody for ChIP-seq" /><br /><small><strong>C. </strong>50 kb region on chromosome 19 surrounding the PRAM1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2C.png" alt="RARA Antibody validated in ChIP-seq" /></p>
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<p><small><strong>Figure 1. ChIP-seq results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP was performed as described above and the IP’d DNA was analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 32 bp tags were aligned to the human reference genome (hg18) using the ELAND algorithm. Figure 2 shows the results of the complete chromosome 19 and two 50 kb region surrounding the HMHA1 and PRAM1 genes, respectively. </small></p>
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<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</small></p>
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<p><small> <strong>Figure 4. Western blot analysis using the Diagenode antibody directed against RARA</strong><br />Human embryonic kidney cells (293T) were transfected with a RARA construct (lane 2) or with a negative control construct (lane 1) and analysed by Western blot using the Diagenode antibody against RARA (Cat. No. CS-155-100), diluted 1:750 in BSA/PBS- Tween. The molecular weight marker (in kDa) 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>A.</strong> ChIP-seq signals on chromosome 19</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2A.png" alt="RARA Antibody ChIP-seq Grade" /> <br /><small><strong>B.</strong> 50 kb region on chromosome 19 surrounding the HMHA1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2B.png" alt="RARA Antibody for ChIP-seq" /><br /><small><strong>C. </strong>50 kb region on chromosome 19 surrounding the PRAM1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2C.png" alt="RARA Antibody validated in ChIP-seq" /></p>
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<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</small></p>
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<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</small></p>
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'description' => 'RARA (UniProtKB/Swiss-Prot entry P10276) is a receptor for retinoic acid, a vitamin A metabolite, which directly regulates gene expression in target cells by binding to specific DNA response elements. In the absence of its ligand, this receptor represses transcription through the recruitment of specific corepressors and of HDAC’s, whereas binding of retinioc acid causes the recruitment of coactivators and HAT’s. Translocations involving the RARA gene, often leading to a RARA/PML fusion protein, are a major cause of acute promyelocytic leukemia.',
'clonality' => '',
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'application_table' => '<table>
<thead>
<tr>
<th>Applications</th>
<th>Suggested dilution</th>
<th>References</th>
</tr>
</thead>
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<tr>
<td>ChIP/ChIP-seq <sup>*</sup></td>
<td>4 μl/ChIP</td>
<td>Fig 1, 2</td>
</tr>
<tr>
<td>ELISA</td>
<td>1:50</td>
<td>Fig 3</td>
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<tr>
<td>Western Blotting</td>
<td>1:750</td>
<td>Fig 4</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 1-10 μl per IP.</small></p>',
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'description' => '<p><span>Alternative names: <strong>RAR</strong>, <strong>RARalpha</strong>, <strong>NR1B1</strong></span></p>
<p><span>Polyclonal antibody raised in rabbit against human <strong>RARA (Retinoic Acid Receptor alpha)</strong> using two KLH-conjugated synthetic peptides containing sequences from the C-terminal region of the protein.</span></p>',
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<div class="small-6 columns">
<p><small><strong>A.</strong> ChIP-seq signals on chromosome 19</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2A.png" alt="RARA Antibody ChIP-seq Grade" /> <br /><small><strong>B.</strong> 50 kb region on chromosome 19 surrounding the HMHA1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2B.png" alt="RARA Antibody for ChIP-seq" /><br /><small><strong>C. </strong>50 kb region on chromosome 19 surrounding the PRAM1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2C.png" alt="RARA Antibody validated in ChIP-seq" /></p>
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<p><small><strong>Figure 1. ChIP-seq results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP was performed as described above and the IP’d DNA was analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 32 bp tags were aligned to the human reference genome (hg18) using the ELAND algorithm. Figure 2 shows the results of the complete chromosome 19 and two 50 kb region surrounding the HMHA1 and PRAM1 genes, respectively. </small></p>
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<div class="row">
<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-chip.png" alt="RARA Antibody ChIP Grade" /></p>
<p class="text-center"></p>
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<div class="small-6 columns">
<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</small></p>
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<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-elisa.png" alt="RARA Antibody ELISA validation" /></p>
<p class="text-center"></p>
</div>
<div class="small-6 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 human RARA (Cat. No. CS-155-100). The plates were coated with the peptides used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:2,400.</small></p>
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<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-wb.png" alt="RARA Antibody validated in Western Blot" /></p>
</div>
<div class="small-6 columns">
<p><small> <strong>Figure 4. Western blot analysis using the Diagenode antibody directed against RARA</strong><br />Human embryonic kidney cells (293T) were transfected with a RARA construct (lane 2) or with a negative control construct (lane 1) and analysed by Western blot using the Diagenode antibody against RARA (Cat. No. CS-155-100), diluted 1:750 in BSA/PBS- Tween. The molecular weight marker (in kDa) is shown on the left; the location of the protein of interest is indicated on the right.</small></p>
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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>
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<li><span style="font-weight: 400;"> Batch-specific data is available on the website</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>
<ul>
<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>
<li>Expert technical support</li>
<li>Sample sizes available</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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'name' => 'ALDH1A1 promotes PARP inhibitor resistance by enhancing retinoic acidreceptor-mediated DNA polymerase θ expression.',
'authors' => 'Lavudi K. et al.',
'description' => '<p>Poly (ADP-ribose) Polymerase (PARP) inhibitors (PARPi) have been approved for both frontline and recurrent setting in ovarian cancer with homologous recombination (HR) repair deficiency. However, more than 40\% of BRCA1/2-mutated ovarian cancer lack the initial response to PARPi treatment, and the majority of those that initially respond eventually develop resistance. Our previous study has demonstrated that increased expression of aldehyde dehydrogenase 1A1 (ALDH1A1) contributes to PARPi resistance in BRCA2-mutated ovarian cancer cells by enhancing microhomology-mediated end joining (MMEJ) but the mechanism remains unknown. Here, we find that ALDH1A1 enhances the expression of DNA polymerase θ (Polθ, encoded by the POLQ gene) in ovarian cancer cells. Furthermore, we demonstrate that the retinoic acid (RA) pathway is involved in the transcription activation of the POLQ gene. The RA receptor (RAR) can bind to the retinoic acid response element (RARE) located in the promoter of the POLQ gene, promoting transcription activation-related histone modification in the presence of RA. Given that ALDH1A1 catalyzes the biosynthesis of RA, we conclude that ALDH1A1 promotes POLQ expression via the activation of the RA signaling pathway. Finally, using a clinically-relevant patient-derived organoid (PDO) model, we find that ALDH1A1 inhibition by the pharmacological inhibitor NCT-505 in combination with the PARP inhibitor olaparib synergistically reduce the cell viability of PDOs carrying BRCA1/2 mutation and positive ALDH1A1 expression. In summary, our study elucidates a new mechanism contributing to PARPi resistance in HR-deficient ovarian cancer and shows the therapeutic potential of combining PARPi and ALDH1A1 inhibition in treating these patients.</p>',
'date' => '2023-07-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/37429899',
'doi' => '10.1038/s41698-023-00411-x',
'modified' => '2023-08-01 14:02:21',
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'id' => '4479',
'name' => 'Systems-biology analysis of rheumatoid arthritis fibroblast-likesynoviocytes implicates cell line-specific transcription factor function.',
'authors' => 'Ainsworth R. I. et al.',
'description' => '<p>Rheumatoid arthritis (RA) is an immune-mediated disease affecting diarthrodial joints that remains an unmet medical need despite improved therapy. This limitation likely reflects the diversity of pathogenic pathways in RA, with individual patients demonstrating variable responses to targeted therapies. Better understanding of RA pathogenesis would be aided by a more complete characterization of the disease. To tackle this challenge, we develop and apply a systems biology approach to identify important transcription factors (TFs) in individual RA fibroblast-like synoviocyte (FLS) cell lines by integrating transcriptomic and epigenomic information. Based on the relative importance of the identified TFs, we stratify the RA FLS cell lines into two subtypes with distinct phenotypes and predicted active pathways. We biologically validate these predictions for the top subtype-specific TF RARα and demonstrate differential regulation of TGFβ signaling in the two subtypes. This study characterizes clusters of RA cell lines with distinctive TF biology by integrating transcriptomic and epigenomic data, which could pave the way towards a greater understanding of disease heterogeneity.</p>',
'date' => '2022-10-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/36266270',
'doi' => '10.1038/s41467-022-33785-w',
'modified' => '2022-11-18 12:24:55',
'created' => '2022-11-15 09:26:20',
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(int) 2 => array(
'id' => '4232',
'name' => 'Short-Chain Fatty Acids Calibrate RARα Activity RegulatingFood Sensitization',
'authors' => 'Yuan X. et al.',
'description' => '<p>Gut-microbiota dysbiosis links to allergic diseases. The mechanism of the exacerbation of food allergy caused by gut-microbiota dysbiosis remains unknown. Regulation of retinoic acid receptor alpha (RARα) signaling is critical for gut immune homeostasis. Here we clarified that RARα in dendritic cells (DCs) promotes Th2 cell differentiation. Antibiotics treatment stimulates retinoic acid signaling in mucosal DCs. We found microbiota metabolites short-chain fatty acids (SCFAs) maintain IGF-1 levels in serum and mesenteric lymph nodes. The IGF-1/Akt pathway is essential for regulating the transcription of genes targeted by RARα. And RARα in DCs affects type I interferon (IFN-I) responses through regulating transcription of IFN-α. Our study identifies SCFAs crosstalk with RARα in dendritic cells as a critical modulator that plays a core role in promoting Th2 cells differentiation at a state of modified/disturbed microbiome.</p>',
'date' => '2021-10-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/34721398',
'doi' => '10.3389/fimmu.2021.737658',
'modified' => '2022-05-19 16:52:41',
'created' => '2022-05-19 10:41:50',
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(int) 3 => array(
'id' => '3614',
'name' => 'Retinoic Acid Receptor Alpha Represses a Th9 Transcriptional and Epigenomic Program to Reduce Allergic Pathology.',
'authors' => 'Schwartz DM, Farley TK, Richoz N, Yao C, Shih HY, Petermann F, Zhang Y, Sun HW, Hayes E, Mikami Y, Jiang K, Davis FP, Kanno Y, Milner JD, Siegel R, Laurence A, Meylan F, O'Shea JJ',
'description' => '<p>CD4 T helper (Th) differentiation is regulated by diverse inputs, including the vitamin A metabolite retinoic acid (RA). RA acts through its receptor RARα to repress transcription of inflammatory cytokines, but is also essential for Th-mediated immunity, indicating complex effects of RA on Th specification and the outcome of the immune response. We examined the impact of RA on the genome-wide transcriptional response during Th differentiation to multiple subsets. RA effects were subset-selective and were most significant in Th9 cells. RA globally antagonized Th9-promoting transcription factors and inhibited Th9 differentiation. RA directly targeted the extended Il9 locus and broadly modified the Th9 epigenome through RARα. RA-RARα activity limited murine Th9-associated pulmonary inflammation, and human allergic inflammation was associated with reduced expression of RA target genes. Thus, repression of the Th9 program is a major function of RA-RARα signaling in Th differentiation, arguing for a role for RA in interleukin 9 (IL-9) related diseases.</p>',
'date' => '2019-01-15',
'pmid' => 'http://www.pubmed.gov/30650370',
'doi' => '10.1016/j.immuni.2018.12.014',
'modified' => '2019-04-17 14:42:26',
'created' => '2019-04-16 12:25:30',
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(int) 4 => array(
'id' => '3642',
'name' => 'Human retinoic acid-regulated CD161 regulatory T cells support wound repair in intestinal mucosa.',
'authors' => 'Povoleri GAM, Nova-Lamperti E, Scottà C, Fanelli G, Chen YC, Becker PD, Boardman D, Costantini B, Romano M, Pavlidis P, McGregor R, Pantazi E, Chauss D, Sun HW, Shih HY, Cousins DJ, Cooper N, Powell N, Kemper C, Pirooznia M, Laurence A, Kordasti S, Kazemi',
'description' => '<p>Repair of tissue damaged during inflammatory processes is key to the return of local homeostasis and restoration of epithelial integrity. Here we describe CD161 regulatory T (T) cells as a distinct, highly suppressive population of T cells that mediate wound healing. These T cells were enriched in intestinal lamina propria, particularly in Crohn's disease. CD161 T cells had an all-trans retinoic acid (ATRA)-regulated gene signature, and CD161 expression on T cells was induced by ATRA, which directly regulated the CD161 gene. CD161 was co-stimulatory, and ligation with the T cell antigen receptor induced cytokines that accelerated the wound healing of intestinal epithelial cells. We identified a transcription-factor network, including BACH2, RORγt, FOSL2, AP-1 and RUNX1, that controlled expression of the wound-healing program, and found a CD161 T cell signature in Crohn's disease mucosa associated with reduced inflammation. These findings identify CD161 T cells as a population involved in controlling the balance between inflammation and epithelial barrier healing in the gut.</p>',
'date' => '2018-12-01',
'pmid' => 'http://www.pubmed.gov/30397350',
'doi' => '10.1038/s41590-018-0230-z',
'modified' => '2019-06-07 10:19:42',
'created' => '2019-06-06 12:11:18',
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(int) 5 => array(
'id' => '3158',
'name' => 'Elevated Fibroblast growth factor 21 (FGF21) in obese, insulin resistant states is normalised by the synthetic retinoid Fenretinide in mice',
'authors' => 'Morrice N. et al.',
'description' => '<p>Fibroblast growth factor 21 (FGF21) has emerged as an important beneficial regulator of glucose and lipid homeostasis but its levels are also abnormally increased in insulin-resistant states in rodents and humans. The synthetic retinoid Fenretinide inhibits obesity and improves glucose homeostasis in mice and has pleotropic effects on cellular pathways. To identify Fenretinide target genes, we performed unbiased RNA-seq analysis in liver from mice fed high-fat diet ± Fenretinide. Strikingly, Fgf21 was the most downregulated hepatic gene. Fenretinide normalised elevated levels of FGF21 in both high-fat diet-induced obese mice and in genetically obese-diabetic Lepr<sup>db</sup>mice. Moreover, Fenretinide-mediated suppression of FGF21 was independent of body weight loss or improved hepatic insulin sensitivity and importantly does not induce unhealthy metabolic complications. In mice which have substantially decreased endogenous retinoic acid biosynthesis, Fgf21 expression was increased, whereas acute pharmacological retinoid treatment decreased FGF21 levels. The repression of FGF21 levels by Fenretinide occurs by reduced binding of RARα and Pol-II at the Fgf21 promoter. We therefore establish Fgf21 as a novel gene target of Fenretinide signalling via a retinoid-dependent mechanism. These results may be of nutritional and therapeutic importance for the treatment of obesity and type-2 diabetes.</p>',
'date' => '2017-03-03',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/28256636',
'doi' => '',
'modified' => '2017-04-12 14:48:12',
'created' => '2017-04-12 14:48:12',
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[maximum depth reached]
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(int) 6 => array(
'id' => '2861',
'name' => 'The oncofusion protein FUS-ERG targets key hematopoietic regulators and modulates the all-trans retinoic acid signaling pathway in t(16;21) acute myeloid leukemia.',
'authors' => 'Sotoca AM1, Prange KH1, Reijnders B1, Mandoli A1, Nguyen LN1, Stunnenberg HG1, Martens JH',
'description' => '<p>The ETS transcription factor ERG has been implicated as a major regulator of both normal and aberrant hematopoiesis. In acute myeloid leukemias harboring t(16;21), ERG function is deregulated due to a fusion with FUS/TLS resulting in the expression of a FUS-ERG oncofusion protein. How this oncofusion protein deregulates the normal ERG transcription program is unclear. Here, we show that FUS-ERG acts in the context of a heptad of proteins (ERG, FLI1, GATA2, LYL1, LMO2, RUNX1 and TAL1) central to proper expression of genes involved in maintaining a stem cell hematopoietic phenotype. Moreover, in t(16;21) FUS-ERG co-occupies genomic regions bound by the nuclear receptor heterodimer RXR:RARA inhibiting target gene expression and interfering with hematopoietic differentiation. All-trans retinoic acid treatment of t(16;21) cells as well as FUS-ERG knockdown alleviate the myeloid-differentiation block. Together, the results suggest that FUS-ERG acts as a transcriptional repressor of the retinoic acid signaling pathway.</p>',
'date' => '2015-07-06',
'pmid' => 'http://www.ncbi.nlm.nih.gov/pubmed/26148230',
'doi' => '10.1038/onc.2015.261',
'modified' => '2016-03-17 10:01:30',
'created' => '2016-03-17 10:01:30',
'ProductsPublication' => array(
[maximum depth reached]
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),
(int) 7 => array(
'id' => '2641',
'name' => 'Retinoic acid is essential for Th1 cell lineage stability and prevents transition to a Th17 cell program.',
'authors' => 'Brown CC, Esterhazy D, Sarde A, London M, Pullabhatla V, Osma-Garcia I, Al-Bader R, Ortiz C, Elgueta R, Arno M, de Rinaldis E, Mucida D, Lord GM, Noelle RJ',
'description' => 'CD4(+) T cells differentiate into phenotypically distinct T helper cells upon antigenic stimulation. Regulation of plasticity between these CD4(+) T-cell lineages is critical for immune homeostasis and prevention of autoimmune disease. However, the factors that regulate lineage stability are largely unknown. Here we investigate a role for retinoic acid (RA) in the regulation of lineage stability using T helper 1 (Th1) cells, traditionally considered the most phenotypically stable Th subset. We found that RA, through its receptor RARα, sustains stable expression of Th1 lineage specifying genes, as well as repressing genes that instruct Th17-cell fate. RA signaling is essential for limiting Th1-cell conversion into Th17 effectors and for preventing pathogenic Th17 responses in vivo. Our study identifies RA-RARα as a key component of the regulatory network governing maintenance and plasticity of Th1-cell fate and defines an additional pathway for the development of Th17 cells.',
'date' => '2015-03-17',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/25769610',
'doi' => '',
'modified' => '2015-07-24 15:39:05',
'created' => '2015-07-24 15:39:05',
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[maximum depth reached]
)
),
(int) 8 => array(
'id' => '116',
'name' => 'PML-RARalpha/RXR Alters the Epigenetic Landscape in Acute Promyelocytic Leukemia.',
'authors' => 'Martens JH, Brinkman AB, Simmer F, Francoijs KJ, Nebbioso A, Ferrara F, Altucci L, Stunnenberg HG',
'description' => 'Many different molecular mechanisms have been associated with PML-RARalpha-dependent transformation of hematopoietic progenitors. Here, we identified high confidence PML-RARalpha binding sites in an acute promyelocytic leukemia (APL) cell line and in two APL primary blasts. We found colocalization of PML-RARalpha with RXR to the vast majority of these binding regions. Genome-wide epigenetic studies revealed that treatment with pharmacological doses of all-trans retinoic acid induces changes in H3 acetylation, but not H3K27me3, H3K9me3, or DNA methylation at the PML-RARalpha/RXR binding sites or at nearby target genes. Our results suggest that PML-RARalpha/RXR functions as a local chromatin modulator and that specific recruitment of histone deacetylase activities to genes important for hematopoietic differentiation, RAR signaling, and epigenetic control is crucial to its transforming potential.',
'date' => '2010-02-17',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/20159609',
'doi' => '',
'modified' => '2015-07-24 15:38:57',
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'id' => '2131',
'antibody_id' => '252',
'name' => 'RARA Antibody (sample size)',
'description' => '<p><span>Alternative names: <strong>RAR</strong>, <strong>RARalpha</strong>, <strong>NR1B1</strong></span></p>
<p><span>Polyclonal antibody raised in rabbit against human RARA (Retinoic Acid Receptor alpha) using two KLH-conjugated synthetic peptides containing sequences from the C-terminal region of the protein.</span></p>',
'label1' => 'Validation Data',
'info1' => '<div class="row">
<div class="small-6 columns">
<p><small><strong>A.</strong> ChIP-seq signals on chromosome 19</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2A.png" alt="RARA Antibody ChIP-seq Grade" /> <br /><small><strong>B.</strong> 50 kb region on chromosome 19 surrounding the HMHA1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2B.png" alt="RARA Antibody for ChIP-seq" /><br /><small><strong>C. </strong>50 kb region on chromosome 19 surrounding the PRAM1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2C.png" alt="RARA Antibody validated in ChIP-seq" /></p>
<p></p>
</div>
<div class="small-6 columns">
<p><small><strong>Figure 1. ChIP-seq results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP was performed as described above and the IP’d DNA was analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 32 bp tags were aligned to the human reference genome (hg18) using the ELAND algorithm. Figure 2 shows the results of the complete chromosome 19 and two 50 kb region surrounding the HMHA1 and PRAM1 genes, respectively. </small></p>
</div>
</div>
<div class="row">
<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-chip.png" alt="RARA Antibody ChIP Grade" /></p>
<p class="text-center"></p>
</div>
<div class="small-6 columns">
<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</small></p>
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</div>
<div class="row">
<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-elisa.png" alt="RARA Antibody ELISA validation" /></p>
<p class="text-center"></p>
</div>
<div class="small-6 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 human RARA (Cat. No. CS-155-100). The plates were coated with the peptides used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:2,400.</small></p>
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<div class="row">
<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-wb.png" alt="RARA Antibody validated in Western Blot" /></p>
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<div class="small-6 columns">
<p><small> <strong>Figure 4. Western blot analysis using the Diagenode antibody directed against RARA</strong><br />Human embryonic kidney cells (293T) were transfected with a RARA construct (lane 2) or with a negative control construct (lane 1) and analysed by Western blot using the Diagenode antibody against RARA (Cat. No. CS-155-100), diluted 1:750 in BSA/PBS- Tween. The molecular weight marker (in kDa) is shown on the left; the location of the protein of interest is indicated on the right.</small></p>
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'meta_keywords' => '',
'meta_description' => 'RARA (Retinoic Acid Receptor alpha) Polyclonal Antibody validated in ChIP-seq, ChIP-qPCR, ELISA and WB. Batch-specific data available on the website. Sample size available.',
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'name' => 'RARA Antibody (sample size)',
'description' => '<p><span>Alternative names: <strong>RAR</strong>, <strong>RARalpha</strong>, <strong>NR1B1</strong></span></p>
<p><span>Polyclonal antibody raised in rabbit against human RARA (Retinoic Acid Receptor alpha) using two KLH-conjugated synthetic peptides containing sequences from the C-terminal region of the protein.</span></p>',
'label1' => 'Validation Data',
'info1' => '<div class="row">
<div class="small-6 columns">
<p><small><strong>A.</strong> ChIP-seq signals on chromosome 19</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2A.png" alt="RARA Antibody ChIP-seq Grade" /> <br /><small><strong>B.</strong> 50 kb region on chromosome 19 surrounding the HMHA1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2B.png" alt="RARA Antibody for ChIP-seq" /><br /><small><strong>C. </strong>50 kb region on chromosome 19 surrounding the PRAM1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2C.png" alt="RARA Antibody validated in ChIP-seq" /></p>
<p></p>
</div>
<div class="small-6 columns">
<p><small><strong>Figure 1. ChIP-seq results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP was performed as described above and the IP’d DNA was analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 32 bp tags were aligned to the human reference genome (hg18) using the ELAND algorithm. Figure 2 shows the results of the complete chromosome 19 and two 50 kb region surrounding the HMHA1 and PRAM1 genes, respectively. </small></p>
</div>
</div>
<div class="row">
<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-chip.png" alt="RARA Antibody ChIP Grade" /></p>
<p class="text-center"></p>
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<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</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 human RARA (Cat. No. CS-155-100). The plates were coated with the peptides used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:2,400.</small></p>
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<p><small> <strong>Figure 4. Western blot analysis using the Diagenode antibody directed against RARA</strong><br />Human embryonic kidney cells (293T) were transfected with a RARA construct (lane 2) or with a negative control construct (lane 1) and analysed by Western blot using the Diagenode antibody against RARA (Cat. No. CS-155-100), diluted 1:750 in BSA/PBS- Tween. The molecular weight marker (in kDa) 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>A.</strong> ChIP-seq signals on chromosome 19</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2A.png" alt="RARA Antibody ChIP-seq Grade" /> <br /><small><strong>B.</strong> 50 kb region on chromosome 19 surrounding the HMHA1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2B.png" alt="RARA Antibody for ChIP-seq" /><br /><small><strong>C. </strong>50 kb region on chromosome 19 surrounding the PRAM1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2C.png" alt="RARA Antibody validated in ChIP-seq" /></p>
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<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</small></p>
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'description' => '<p><span>Alternative names: <strong>RAR</strong>, <strong>RARalpha</strong>, <strong>NR1B1</strong></span></p>
<p><span>Polyclonal antibody raised in rabbit against human RARA (Retinoic Acid Receptor alpha) using two KLH-conjugated synthetic peptides containing sequences from the C-terminal region of the protein.</span></p>',
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<p><small><strong>A.</strong> ChIP-seq signals on chromosome 19</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2A.png" alt="RARA Antibody ChIP-seq Grade" /> <br /><small><strong>B.</strong> 50 kb region on chromosome 19 surrounding the HMHA1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2B.png" alt="RARA Antibody for ChIP-seq" /><br /><small><strong>C. </strong>50 kb region on chromosome 19 surrounding the PRAM1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2C.png" alt="RARA Antibody validated in ChIP-seq" /></p>
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<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</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 human RARA (Cat. No. CS-155-100). The plates were coated with the peptides used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:2,400.</small></p>
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<p><small> <strong>Figure 4. Western blot analysis using the Diagenode antibody directed against RARA</strong><br />Human embryonic kidney cells (293T) were transfected with a RARA construct (lane 2) or with a negative control construct (lane 1) and analysed by Western blot using the Diagenode antibody against RARA (Cat. No. CS-155-100), diluted 1:750 in BSA/PBS- Tween. The molecular weight marker (in kDa) is shown on the left; the location of the protein of interest is indicated on the right.</small></p>
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<p><span>Polyclonal antibody raised in rabbit against human RARA (Retinoic Acid Receptor alpha) using two KLH-conjugated synthetic peptides containing sequences from the C-terminal region of the protein.</span></p>',
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<p><small><strong>A.</strong> ChIP-seq signals on chromosome 19</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2A.png" alt="RARA Antibody ChIP-seq Grade" /> <br /><small><strong>B.</strong> 50 kb region on chromosome 19 surrounding the HMHA1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2B.png" alt="RARA Antibody for ChIP-seq" /><br /><small><strong>C. </strong>50 kb region on chromosome 19 surrounding the PRAM1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2C.png" alt="RARA Antibody validated in ChIP-seq" /></p>
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<p><small><strong>Figure 1. ChIP-seq results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP was performed as described above and the IP’d DNA was analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 32 bp tags were aligned to the human reference genome (hg18) using the ELAND algorithm. Figure 2 shows the results of the complete chromosome 19 and two 50 kb region surrounding the HMHA1 and PRAM1 genes, respectively. </small></p>
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<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</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 human RARA (Cat. No. CS-155-100). The plates were coated with the peptides used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:2,400.</small></p>
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<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-wb.png" alt="RARA Antibody validated in Western Blot" /></p>
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<p><small> <strong>Figure 4. Western blot analysis using the Diagenode antibody directed against RARA</strong><br />Human embryonic kidney cells (293T) were transfected with a RARA construct (lane 2) or with a negative control construct (lane 1) and analysed by Western blot using the Diagenode antibody against RARA (Cat. No. CS-155-100), diluted 1:750 in BSA/PBS- Tween. The molecular weight marker (in kDa) is shown on the left; the location of the protein of interest is indicated on the right.</small></p>
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<td>4 μl/ChIP</td>
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<p><small><strong>A.</strong> ChIP-seq signals on chromosome 19</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2A.png" alt="RARA Antibody ChIP-seq Grade" /> <br /><small><strong>B.</strong> 50 kb region on chromosome 19 surrounding the HMHA1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2B.png" alt="RARA Antibody for ChIP-seq" /><br /><small><strong>C. </strong>50 kb region on chromosome 19 surrounding the PRAM1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2C.png" alt="RARA Antibody validated in ChIP-seq" /></p>
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<p><small><strong>Figure 1. ChIP-seq results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP was performed as described above and the IP’d DNA was analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 32 bp tags were aligned to the human reference genome (hg18) using the ELAND algorithm. Figure 2 shows the results of the complete chromosome 19 and two 50 kb region surrounding the HMHA1 and PRAM1 genes, respectively. </small></p>
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<div class="row">
<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-chip.png" alt="RARA Antibody ChIP Grade" /></p>
<p class="text-center"></p>
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<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</small></p>
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<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-elisa.png" alt="RARA Antibody ELISA validation" /></p>
<p class="text-center"></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 human RARA (Cat. No. CS-155-100). The plates were coated with the peptides used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:2,400.</small></p>
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<div class="row">
<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-wb.png" alt="RARA Antibody validated in Western Blot" /></p>
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<p><small> <strong>Figure 4. Western blot analysis using the Diagenode antibody directed against RARA</strong><br />Human embryonic kidney cells (293T) were transfected with a RARA construct (lane 2) or with a negative control construct (lane 1) and analysed by Western blot using the Diagenode antibody against RARA (Cat. No. CS-155-100), diluted 1:750 in BSA/PBS- Tween. The molecular weight marker (in kDa) is shown on the left; the location of the protein of interest is indicated on the right.</small></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><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></p>
<p></p>
<p></p>
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<p></p>
<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' => 'ALDH1A1 promotes PARP inhibitor resistance by enhancing retinoic acidreceptor-mediated DNA polymerase θ expression.',
'authors' => 'Lavudi K. et al.',
'description' => '<p>Poly (ADP-ribose) Polymerase (PARP) inhibitors (PARPi) have been approved for both frontline and recurrent setting in ovarian cancer with homologous recombination (HR) repair deficiency. However, more than 40\% of BRCA1/2-mutated ovarian cancer lack the initial response to PARPi treatment, and the majority of those that initially respond eventually develop resistance. Our previous study has demonstrated that increased expression of aldehyde dehydrogenase 1A1 (ALDH1A1) contributes to PARPi resistance in BRCA2-mutated ovarian cancer cells by enhancing microhomology-mediated end joining (MMEJ) but the mechanism remains unknown. Here, we find that ALDH1A1 enhances the expression of DNA polymerase θ (Polθ, encoded by the POLQ gene) in ovarian cancer cells. Furthermore, we demonstrate that the retinoic acid (RA) pathway is involved in the transcription activation of the POLQ gene. The RA receptor (RAR) can bind to the retinoic acid response element (RARE) located in the promoter of the POLQ gene, promoting transcription activation-related histone modification in the presence of RA. Given that ALDH1A1 catalyzes the biosynthesis of RA, we conclude that ALDH1A1 promotes POLQ expression via the activation of the RA signaling pathway. Finally, using a clinically-relevant patient-derived organoid (PDO) model, we find that ALDH1A1 inhibition by the pharmacological inhibitor NCT-505 in combination with the PARP inhibitor olaparib synergistically reduce the cell viability of PDOs carrying BRCA1/2 mutation and positive ALDH1A1 expression. In summary, our study elucidates a new mechanism contributing to PARPi resistance in HR-deficient ovarian cancer and shows the therapeutic potential of combining PARPi and ALDH1A1 inhibition in treating these patients.</p>',
'date' => '2023-07-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/37429899',
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'name' => 'Systems-biology analysis of rheumatoid arthritis fibroblast-likesynoviocytes implicates cell line-specific transcription factor function.',
'authors' => 'Ainsworth R. I. et al.',
'description' => '<p>Rheumatoid arthritis (RA) is an immune-mediated disease affecting diarthrodial joints that remains an unmet medical need despite improved therapy. This limitation likely reflects the diversity of pathogenic pathways in RA, with individual patients demonstrating variable responses to targeted therapies. Better understanding of RA pathogenesis would be aided by a more complete characterization of the disease. To tackle this challenge, we develop and apply a systems biology approach to identify important transcription factors (TFs) in individual RA fibroblast-like synoviocyte (FLS) cell lines by integrating transcriptomic and epigenomic information. Based on the relative importance of the identified TFs, we stratify the RA FLS cell lines into two subtypes with distinct phenotypes and predicted active pathways. We biologically validate these predictions for the top subtype-specific TF RARα and demonstrate differential regulation of TGFβ signaling in the two subtypes. This study characterizes clusters of RA cell lines with distinctive TF biology by integrating transcriptomic and epigenomic data, which could pave the way towards a greater understanding of disease heterogeneity.</p>',
'date' => '2022-10-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/36266270',
'doi' => '10.1038/s41467-022-33785-w',
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'name' => 'Short-Chain Fatty Acids Calibrate RARα Activity RegulatingFood Sensitization',
'authors' => 'Yuan X. et al.',
'description' => '<p>Gut-microbiota dysbiosis links to allergic diseases. The mechanism of the exacerbation of food allergy caused by gut-microbiota dysbiosis remains unknown. Regulation of retinoic acid receptor alpha (RARα) signaling is critical for gut immune homeostasis. Here we clarified that RARα in dendritic cells (DCs) promotes Th2 cell differentiation. Antibiotics treatment stimulates retinoic acid signaling in mucosal DCs. We found microbiota metabolites short-chain fatty acids (SCFAs) maintain IGF-1 levels in serum and mesenteric lymph nodes. The IGF-1/Akt pathway is essential for regulating the transcription of genes targeted by RARα. And RARα in DCs affects type I interferon (IFN-I) responses through regulating transcription of IFN-α. Our study identifies SCFAs crosstalk with RARα in dendritic cells as a critical modulator that plays a core role in promoting Th2 cells differentiation at a state of modified/disturbed microbiome.</p>',
'date' => '2021-10-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/34721398',
'doi' => '10.3389/fimmu.2021.737658',
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'name' => 'Retinoic Acid Receptor Alpha Represses a Th9 Transcriptional and Epigenomic Program to Reduce Allergic Pathology.',
'authors' => 'Schwartz DM, Farley TK, Richoz N, Yao C, Shih HY, Petermann F, Zhang Y, Sun HW, Hayes E, Mikami Y, Jiang K, Davis FP, Kanno Y, Milner JD, Siegel R, Laurence A, Meylan F, O'Shea JJ',
'description' => '<p>CD4 T helper (Th) differentiation is regulated by diverse inputs, including the vitamin A metabolite retinoic acid (RA). RA acts through its receptor RARα to repress transcription of inflammatory cytokines, but is also essential for Th-mediated immunity, indicating complex effects of RA on Th specification and the outcome of the immune response. We examined the impact of RA on the genome-wide transcriptional response during Th differentiation to multiple subsets. RA effects were subset-selective and were most significant in Th9 cells. RA globally antagonized Th9-promoting transcription factors and inhibited Th9 differentiation. RA directly targeted the extended Il9 locus and broadly modified the Th9 epigenome through RARα. RA-RARα activity limited murine Th9-associated pulmonary inflammation, and human allergic inflammation was associated with reduced expression of RA target genes. Thus, repression of the Th9 program is a major function of RA-RARα signaling in Th differentiation, arguing for a role for RA in interleukin 9 (IL-9) related diseases.</p>',
'date' => '2019-01-15',
'pmid' => 'http://www.pubmed.gov/30650370',
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'description' => '<p>Repair of tissue damaged during inflammatory processes is key to the return of local homeostasis and restoration of epithelial integrity. Here we describe CD161 regulatory T (T) cells as a distinct, highly suppressive population of T cells that mediate wound healing. These T cells were enriched in intestinal lamina propria, particularly in Crohn's disease. CD161 T cells had an all-trans retinoic acid (ATRA)-regulated gene signature, and CD161 expression on T cells was induced by ATRA, which directly regulated the CD161 gene. CD161 was co-stimulatory, and ligation with the T cell antigen receptor induced cytokines that accelerated the wound healing of intestinal epithelial cells. We identified a transcription-factor network, including BACH2, RORγt, FOSL2, AP-1 and RUNX1, that controlled expression of the wound-healing program, and found a CD161 T cell signature in Crohn's disease mucosa associated with reduced inflammation. These findings identify CD161 T cells as a population involved in controlling the balance between inflammation and epithelial barrier healing in the gut.</p>',
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'pmid' => 'http://www.pubmed.gov/30397350',
'doi' => '10.1038/s41590-018-0230-z',
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'name' => 'Elevated Fibroblast growth factor 21 (FGF21) in obese, insulin resistant states is normalised by the synthetic retinoid Fenretinide in mice',
'authors' => 'Morrice N. et al.',
'description' => '<p>Fibroblast growth factor 21 (FGF21) has emerged as an important beneficial regulator of glucose and lipid homeostasis but its levels are also abnormally increased in insulin-resistant states in rodents and humans. The synthetic retinoid Fenretinide inhibits obesity and improves glucose homeostasis in mice and has pleotropic effects on cellular pathways. To identify Fenretinide target genes, we performed unbiased RNA-seq analysis in liver from mice fed high-fat diet ± Fenretinide. Strikingly, Fgf21 was the most downregulated hepatic gene. Fenretinide normalised elevated levels of FGF21 in both high-fat diet-induced obese mice and in genetically obese-diabetic Lepr<sup>db</sup>mice. Moreover, Fenretinide-mediated suppression of FGF21 was independent of body weight loss or improved hepatic insulin sensitivity and importantly does not induce unhealthy metabolic complications. In mice which have substantially decreased endogenous retinoic acid biosynthesis, Fgf21 expression was increased, whereas acute pharmacological retinoid treatment decreased FGF21 levels. The repression of FGF21 levels by Fenretinide occurs by reduced binding of RARα and Pol-II at the Fgf21 promoter. We therefore establish Fgf21 as a novel gene target of Fenretinide signalling via a retinoid-dependent mechanism. These results may be of nutritional and therapeutic importance for the treatment of obesity and type-2 diabetes.</p>',
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'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/28256636',
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'name' => 'The oncofusion protein FUS-ERG targets key hematopoietic regulators and modulates the all-trans retinoic acid signaling pathway in t(16;21) acute myeloid leukemia.',
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'description' => '<p>The ETS transcription factor ERG has been implicated as a major regulator of both normal and aberrant hematopoiesis. In acute myeloid leukemias harboring t(16;21), ERG function is deregulated due to a fusion with FUS/TLS resulting in the expression of a FUS-ERG oncofusion protein. How this oncofusion protein deregulates the normal ERG transcription program is unclear. Here, we show that FUS-ERG acts in the context of a heptad of proteins (ERG, FLI1, GATA2, LYL1, LMO2, RUNX1 and TAL1) central to proper expression of genes involved in maintaining a stem cell hematopoietic phenotype. Moreover, in t(16;21) FUS-ERG co-occupies genomic regions bound by the nuclear receptor heterodimer RXR:RARA inhibiting target gene expression and interfering with hematopoietic differentiation. All-trans retinoic acid treatment of t(16;21) cells as well as FUS-ERG knockdown alleviate the myeloid-differentiation block. Together, the results suggest that FUS-ERG acts as a transcriptional repressor of the retinoic acid signaling pathway.</p>',
'date' => '2015-07-06',
'pmid' => 'http://www.ncbi.nlm.nih.gov/pubmed/26148230',
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'name' => 'Retinoic acid is essential for Th1 cell lineage stability and prevents transition to a Th17 cell program.',
'authors' => 'Brown CC, Esterhazy D, Sarde A, London M, Pullabhatla V, Osma-Garcia I, Al-Bader R, Ortiz C, Elgueta R, Arno M, de Rinaldis E, Mucida D, Lord GM, Noelle RJ',
'description' => 'CD4(+) T cells differentiate into phenotypically distinct T helper cells upon antigenic stimulation. Regulation of plasticity between these CD4(+) T-cell lineages is critical for immune homeostasis and prevention of autoimmune disease. However, the factors that regulate lineage stability are largely unknown. Here we investigate a role for retinoic acid (RA) in the regulation of lineage stability using T helper 1 (Th1) cells, traditionally considered the most phenotypically stable Th subset. We found that RA, through its receptor RARα, sustains stable expression of Th1 lineage specifying genes, as well as repressing genes that instruct Th17-cell fate. RA signaling is essential for limiting Th1-cell conversion into Th17 effectors and for preventing pathogenic Th17 responses in vivo. Our study identifies RA-RARα as a key component of the regulatory network governing maintenance and plasticity of Th1-cell fate and defines an additional pathway for the development of Th17 cells.',
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'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/25769610',
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'name' => 'PML-RARalpha/RXR Alters the Epigenetic Landscape in Acute Promyelocytic Leukemia.',
'authors' => 'Martens JH, Brinkman AB, Simmer F, Francoijs KJ, Nebbioso A, Ferrara F, Altucci L, Stunnenberg HG',
'description' => 'Many different molecular mechanisms have been associated with PML-RARalpha-dependent transformation of hematopoietic progenitors. Here, we identified high confidence PML-RARalpha binding sites in an acute promyelocytic leukemia (APL) cell line and in two APL primary blasts. We found colocalization of PML-RARalpha with RXR to the vast majority of these binding regions. Genome-wide epigenetic studies revealed that treatment with pharmacological doses of all-trans retinoic acid induces changes in H3 acetylation, but not H3K27me3, H3K9me3, or DNA methylation at the PML-RARalpha/RXR binding sites or at nearby target genes. Our results suggest that PML-RARalpha/RXR functions as a local chromatin modulator and that specific recruitment of histone deacetylase activities to genes important for hematopoietic differentiation, RAR signaling, and epigenetic control is crucial to its transforming potential.',
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'name' => 'RARA Antibody (sample size)',
'description' => '<p><span>Alternative names: <strong>RAR</strong>, <strong>RARalpha</strong>, <strong>NR1B1</strong></span></p>
<p><span>Polyclonal antibody raised in rabbit against human RARA (Retinoic Acid Receptor alpha) using two KLH-conjugated synthetic peptides containing sequences from the C-terminal region of the protein.</span></p>',
'label1' => 'Validation Data',
'info1' => '<div class="row">
<div class="small-6 columns">
<p><small><strong>A.</strong> ChIP-seq signals on chromosome 19</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2A.png" alt="RARA Antibody ChIP-seq Grade" /> <br /><small><strong>B.</strong> 50 kb region on chromosome 19 surrounding the HMHA1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2B.png" alt="RARA Antibody for ChIP-seq" /><br /><small><strong>C. </strong>50 kb region on chromosome 19 surrounding the PRAM1 gene</small><br /> <img src="https://www.diagenode.com/img/product/antibodies/C15310155-Fig2C.png" alt="RARA Antibody validated in ChIP-seq" /></p>
<p></p>
</div>
<div class="small-6 columns">
<p><small><strong>Figure 1. ChIP-seq results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP was performed as described above and the IP’d DNA was analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 32 bp tags were aligned to the human reference genome (hg18) using the ELAND algorithm. Figure 2 shows the results of the complete chromosome 19 and two 50 kb region surrounding the HMHA1 and PRAM1 genes, respectively. </small></p>
</div>
</div>
<div class="row">
<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-chip.png" alt="RARA Antibody ChIP Grade" /></p>
<p class="text-center"></p>
</div>
<div class="small-6 columns">
<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</small></p>
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<div class="row">
<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-elisa.png" alt="RARA Antibody ELISA validation" /></p>
<p class="text-center"></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 human RARA (Cat. No. CS-155-100). The plates were coated with the peptides used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:2,400.</small></p>
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<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-wb.png" alt="RARA Antibody validated in Western Blot" /></p>
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<p><small> <strong>Figure 4. Western blot analysis using the Diagenode antibody directed against RARA</strong><br />Human embryonic kidney cells (293T) were transfected with a RARA construct (lane 2) or with a negative control construct (lane 1) and analysed by Western blot using the Diagenode antibody against RARA (Cat. No. CS-155-100), diluted 1:750 in BSA/PBS- Tween. The molecular weight marker (in kDa) is shown on the left; the location of the protein of interest is indicated on the right.</small></p>
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<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-chip.png" alt="RARA Antibody ChIP Grade" /></p>
<p class="text-center"></p>
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<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</small></p>
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<div class="row">
<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-elisa.png" alt="RARA Antibody ELISA validation" /></p>
<p class="text-center"></p>
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<div class="small-6 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 human RARA (Cat. No. CS-155-100). The plates were coated with the peptides used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:2,400.</small></p>
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<div class="row">
<div class="small-6 columns">
<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-wb.png" alt="RARA Antibody validated in Western Blot" /></p>
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<p><small> <strong>Figure 4. Western blot analysis using the Diagenode antibody directed against RARA</strong><br />Human embryonic kidney cells (293T) were transfected with a RARA construct (lane 2) or with a negative control construct (lane 1) and analysed by Western blot using the Diagenode antibody against RARA (Cat. No. CS-155-100), diluted 1:750 in BSA/PBS- Tween. The molecular weight marker (in kDa) 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 1. ChIP-seq results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP was performed as described above and the IP’d DNA was analysed with an Illumina Genome Analyzer. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 32 bp tags were aligned to the human reference genome (hg18) using the ELAND algorithm. Figure 2 shows the results of the complete chromosome 19 and two 50 kb region surrounding the HMHA1 and PRAM1 genes, respectively. </small></p>
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<p><small> <strong>Figure 2. ChIP results obtained with the Diagenode antibody directed against RARA</strong><br />ChIP assays were performed using NB4 cells, the Diagenode antibody against RARA (Cat. No. CS-155-100) and optimized primer pairs for qPCR. Sheared chromatin from 6 million cells and 4 μl of antibody were used per ChIP experiment. QPCR was performed using primers specific for the TGM2, HMHA1, PRAM1 and H2B genes. Figure 1 shows the relative occupancy, calculated as the ratio + control/background for which the second exon of the MB gene was used.</small></p>
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<p class="text-center"><img src="https://www.diagenode.com/img/product/antibodies/C15310155-wb.png" alt="RARA Antibody validated in Western Blot" /></p>
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<p><small> <strong>Figure 4. Western blot analysis using the Diagenode antibody directed against RARA</strong><br />Human embryonic kidney cells (293T) were transfected with a RARA construct (lane 2) or with a negative control construct (lane 1) and analysed by Western blot using the Diagenode antibody against RARA (Cat. No. CS-155-100), diluted 1:750 in BSA/PBS- Tween. The molecular weight marker (in kDa) is shown on the left; the location of the protein of interest is indicated on the right.</small></p>
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'description' => 'Many different molecular mechanisms have been associated with PML-RARalpha-dependent transformation of hematopoietic progenitors. Here, we identified high confidence PML-RARalpha binding sites in an acute promyelocytic leukemia (APL) cell line and in two APL primary blasts. We found colocalization of PML-RARalpha with RXR to the vast majority of these binding regions. Genome-wide epigenetic studies revealed that treatment with pharmacological doses of all-trans retinoic acid induces changes in H3 acetylation, but not H3K27me3, H3K9me3, or DNA methylation at the PML-RARalpha/RXR binding sites or at nearby target genes. Our results suggest that PML-RARalpha/RXR functions as a local chromatin modulator and that specific recruitment of histone deacetylase activities to genes important for hematopoietic differentiation, RAR signaling, and epigenetic control is crucial to its transforming potential.',
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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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