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<p><small><strong> Figure 1. ChIP </strong><br />RbAp48 antibody immunoprecipitates RbAp48 protein-DNA in ChIP experiments. ChIP Sample: HeLa chromatin extract A. 5 μg preimmune mouse IgG B. 5 μg of RbAp48 antibody (C15200206) The precipitated DNA was detected by PCR with primer set targeting to SOX9 gene locus. </small></p>
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<p><small><strong> Figure 2. Immunoprecipitation </strong><br />RbAp48 antibody immunoprecipitates RbAp48 protein in IP experiments. IP Sample: 1,000 μg HeLa whole cell extract A. 40 μg HeLa whole cell extract B. Control with 2.5 μg of preimmune mouse IgG C. Immunoprecipitation of RbAp48 protein with 2.5 μg of RbAp48 antibody (C15200206) The immunoprecipitated RbAp48 protein was detected by western blot with the RbAp48 antibody diluted 1:500. </small></p>
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<p><small><strong> Figure 3. Immunofluorescent analysis</strong><br />Immunofluorescence analysis of HeLa cells, using RbAp48 (Cat. No. C15200206) antibody at a 1:100 dilution. </small></p>
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<p><small><strong> Figure 4. Western blot </strong><br />Detection of RbAp48 in HeLa nuclear extract. </small></p>
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<p><small><strong> Figure 1. ChIP </strong><br />RbAp48 antibody immunoprecipitates RbAp48 protein-DNA in ChIP experiments. ChIP Sample: HeLa chromatin extract A. 5 μg preimmune mouse IgG B. 5 μg of RbAp48 antibody (C15200206) The precipitated DNA was detected by PCR with primer set targeting to SOX9 gene locus. </small></p>
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<p><small><strong> Figure 2. Immunoprecipitation </strong><br />RbAp48 antibody immunoprecipitates RbAp48 protein in IP experiments. IP Sample: 1,000 μg HeLa whole cell extract A. 40 μg HeLa whole cell extract B. Control with 2.5 μg of preimmune mouse IgG C. Immunoprecipitation of RbAp48 protein with 2.5 μg of RbAp48 antibody (C15200206) The immunoprecipitated RbAp48 protein was detected by western blot with the RbAp48 antibody diluted 1:500. </small></p>
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<p><small><strong> Figure 3. Immunofluorescent analysis</strong><br />Immunofluorescence analysis of HeLa cells, using RbAp48 (Cat. No. C15200206) antibody at a 1:100 dilution. </small></p>
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<p><small><strong> Figure 4. Western blot </strong><br />Detection of RbAp48 in HeLa nuclear extract. </small></p>
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<p><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
<p><sup>HeLa cells transfected with a Cas9 expression vector (left) or untransfected cells (right) were fixed in methanol at -20°C, permeabilized with acetone at -20°C and blocked with PBS containing 2% BSA. The cells were stained with the Cas9 C-terminal antibody (Cat. No. C15200229) diluted 1:400, followed by incubation with an anti-mouse secondary antibody coupled to AF488. The bottom images show counter-staining of the nuclei with Hoechst 33342.</sup></p>
<h5><sup>Check our selection of antibodies validated in IF.</sup></h5>',
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<p><br />Chromatin immunoprecipitation (<b>ChIP</b>) is a technique to study the associations of proteins with the specific genomic regions in intact cells. One of the most important steps of this protocol is the immunoprecipitation of targeted protein using the antibody specifically recognizing it. The quality of antibodies used in ChIP is essential for the success of the experiment. Diagenode offers extensively validated ChIP-grade antibodies, confirmed for their specificity, and high level of performance in ChIP. Each batch is validated, and batch-specific data are available on the website.</p>
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<p><strong>ChIP results</strong> obtained with the antibody directed against H3K4me3 (Cat. No. <a href="../p/h3k4me3-polyclonal-antibody-premium-50-ug-50-ul">C15410003</a>). </p>
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<p><small><strong> Figure 1. ChIP </strong><br />RbAp48 antibody immunoprecipitates RbAp48 protein-DNA in ChIP experiments. ChIP Sample: HeLa chromatin extract A. 5 μg preimmune mouse IgG B. 5 μg of RbAp48 antibody (C15200206) The precipitated DNA was detected by PCR with primer set targeting to SOX9 gene locus. </small></p>
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<p><small><strong> Figure 2. Immunoprecipitation </strong><br />RbAp48 antibody immunoprecipitates RbAp48 protein in IP experiments. IP Sample: 1,000 μg HeLa whole cell extract A. 40 μg HeLa whole cell extract B. Control with 2.5 μg of preimmune mouse IgG C. Immunoprecipitation of RbAp48 protein with 2.5 μg of RbAp48 antibody (C15200206) The immunoprecipitated RbAp48 protein was detected by western blot with the RbAp48 antibody diluted 1:500. </small></p>
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<p><small><strong> Figure 3. Immunofluorescent analysis</strong><br />Immunofluorescence analysis of HeLa cells, using RbAp48 (Cat. No. C15200206) antibody at a 1:100 dilution. </small></p>
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<p><small><strong> Figure 1. ChIP </strong><br />RbAp48 antibody immunoprecipitates RbAp48 protein-DNA in ChIP experiments. ChIP Sample: HeLa chromatin extract A. 5 μg preimmune mouse IgG B. 5 μg of RbAp48 antibody (C15200206) The precipitated DNA was detected by PCR with primer set targeting to SOX9 gene locus. </small></p>
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<p><small><strong> Figure 3. Immunofluorescent analysis</strong><br />Immunofluorescence analysis of HeLa cells, using RbAp48 (Cat. No. C15200206) antibody at a 1:100 dilution. </small></p>
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<p><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
<p><sup>HeLa cells transfected with a Cas9 expression vector (left) or untransfected cells (right) were fixed in methanol at -20°C, permeabilized with acetone at -20°C and blocked with PBS containing 2% BSA. The cells were stained with the Cas9 C-terminal antibody (Cat. No. C15200229) diluted 1:400, followed by incubation with an anti-mouse secondary antibody coupled to AF488. The bottom images show counter-staining of the nuclei with Hoechst 33342.</sup></p>
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<p><br />Chromatin immunoprecipitation (<b>ChIP</b>) is a technique to study the associations of proteins with the specific genomic regions in intact cells. One of the most important steps of this protocol is the immunoprecipitation of targeted protein using the antibody specifically recognizing it. The quality of antibodies used in ChIP is essential for the success of the experiment. Diagenode offers extensively validated ChIP-grade antibodies, confirmed for their specificity, and high level of performance in ChIP. Each batch is validated, and batch-specific data are available on the website.</p>
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<p><strong>ChIP results</strong> obtained with the antibody directed against H3K4me3 (Cat. No. <a href="../p/h3k4me3-polyclonal-antibody-premium-50-ug-50-ul">C15410003</a>). </p>
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<p>Our aim at Diagenode is to offer the largest collection of highly specific <strong>ChIP-grade antibodies</strong>. We add new antibodies monthly. Find your ChIP-grade antibody in the list below and check more information about tested applications, extensive validation data, and product information.</p>',
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<p><small><strong> Figure 1. ChIP </strong><br />RbAp48 antibody immunoprecipitates RbAp48 protein-DNA in ChIP experiments. ChIP Sample: HeLa chromatin extract A. 5 μg preimmune mouse IgG B. 5 μg of RbAp48 antibody (C15200206) The precipitated DNA was detected by PCR with primer set targeting to SOX9 gene locus. </small></p>
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<p><small><strong> Figure 2. Immunoprecipitation </strong><br />RbAp48 antibody immunoprecipitates RbAp48 protein in IP experiments. IP Sample: 1,000 μg HeLa whole cell extract A. 40 μg HeLa whole cell extract B. Control with 2.5 μg of preimmune mouse IgG C. Immunoprecipitation of RbAp48 protein with 2.5 μg of RbAp48 antibody (C15200206) The immunoprecipitated RbAp48 protein was detected by western blot with the RbAp48 antibody diluted 1:500. </small></p>
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<p><small><strong> Figure 3. Immunofluorescent analysis</strong><br />Immunofluorescence analysis of HeLa cells, using RbAp48 (Cat. No. C15200206) antibody at a 1:100 dilution. </small></p>
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<p><small><strong> Figure 4. Western blot </strong><br />Detection of RbAp48 in HeLa nuclear extract. </small></p>
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<p id="p-2">Our results unveil Ser2 phosphorylation as a new BCL11B post-translational modification linking PKC signalling pathway to TCR activation and define a simple model for the functional switch of BCL11B from a transcriptional repressor to an activator during TCR activation of human CD4<sup>+</sup> T cells.</p>',
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<p><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
<p><sup>HeLa cells transfected with a Cas9 expression vector (left) or untransfected cells (right) were fixed in methanol at -20°C, permeabilized with acetone at -20°C and blocked with PBS containing 2% BSA. The cells were stained with the Cas9 C-terminal antibody (Cat. No. C15200229) diluted 1:400, followed by incubation with an anti-mouse secondary antibody coupled to AF488. The bottom images show counter-staining of the nuclei with Hoechst 33342.</sup></p>
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'description' => '<p>More than in any other immuoprecipitation assays, quality antibodies are critical tools in many epigenetics experiments. Since 10 years, Diagenode has developed the most stringent quality production available on the market for antibodies exclusively focused on epigenetic uses. All our antibodies have been qualified to work in epigenetic applications.</p>',
'image_id' => null,
'type' => 'Brochure',
'url' => 'files/brochures/Epigenetic_Antibodies_Brochure.pdf',
'slug' => 'epigenetic-antibodies-brochure',
'meta_keywords' => '',
'meta_description' => '',
'modified' => '2016-06-15 11:24:06',
'created' => '2015-07-03 16:05:27',
'ProductsDocument' => array(
'id' => '1502',
'product_id' => '2016',
'document_id' => '38'
)
)
$publication = array(
'id' => '2955',
'name' => 'PKC-mediated phosphorylation of BCL11B at Serine 2 negatively regulates its interaction with NuRD complexes during CD4+ T cell activation',
'authors' => 'Dubuissez M et al.',
'description' => '<p id="p-1">The transcription factor BCL11B/CTIP2 is a major regulatory protein implicated in various aspects of development, function and survival of T cells. MAPK-mediated phosphorylation and SUMOylation modulate BCL11B transcriptional activity, switching it from a repressor in naïve murine thymocytes to a transcriptional activator in activated thymocytes. Here, we show that BCL11B interacts via its conserved N-terminal MSRRKQ motif with endogenous MTA1 and MTA3 proteins to recruit various NuRD complexes. Furthermore, we demonstrate that PKC-mediated phosphorylation of BCL11B Ser2 does not significantly impact on BCL11B SUMOylation but negatively regulates NuRD recruitment by dampening the interaction with MTA1/3 and RbAp46 proteins. We detected increased phosphorylation of BCL11B Ser2 upon <em>in vivo</em> activation of transformed and primary human CD4<sup>+</sup> T cells. We show that following activation of CD4<sup>+</sup> T cells, BCL11B still binds to <em>IL2</em> and <em>Id2</em> promoters but activates their transcription by recruiting P300 instead of MTA1. Prolonged stimulation results in the direct transcriptional repression of <em>BCL11B</em> by KLF4.</p>
<p id="p-2">Our results unveil Ser2 phosphorylation as a new BCL11B post-translational modification linking PKC signalling pathway to TCR activation and define a simple model for the functional switch of BCL11B from a transcriptional repressor to an activator during TCR activation of human CD4<sup>+</sup> T cells.</p>',
'date' => '2016-05-09',
'pmid' => 'http://mcb.asm.org/content/early/2016/05/03/MCB.00062-16.abstract?cited-by=yes&legid=mcb;MCB.00062-16v1',
'doi' => '10.1128/MCB.00062-16 ',
'modified' => '2016-06-15 15:42:48',
'created' => '2016-06-15 15:42:48',
'ProductsPublication' => array(
'id' => '1336',
'product_id' => '2016',
'publication_id' => '2955'
)
)
$externalLink = ' <a href="http://mcb.asm.org/content/early/2016/05/03/MCB.00062-16.abstract?cited-by=yes&legid=mcb;MCB.00062-16v1" target="_blank"><i class="fa fa-external-link"></i></a>'include - APP/View/Products/view.ctp, line 755
View::_evaluate() - CORE/Cake/View/View.php, line 971
View::_render() - CORE/Cake/View/View.php, line 933
View::render() - CORE/Cake/View/View.php, line 473
Controller::render() - CORE/Cake/Controller/Controller.php, line 963
ProductsController::slug() - APP/Controller/ProductsController.php, line 1052
ReflectionMethod::invokeArgs() - [internal], line ??
Controller::invokeAction() - CORE/Cake/Controller/Controller.php, line 491
Dispatcher::_invoke() - CORE/Cake/Routing/Dispatcher.php, line 193
Dispatcher::dispatch() - CORE/Cake/Routing/Dispatcher.php, line 167
[main] - APP/webroot/index.php, line 118
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