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<div id="abspara0010" role="paragraph">Control of stem cell-associated genes by Trithorax group (TrxG) and Polycomb group (PcG) proteins is frequently misregulated in cancer. In leukemia, oncogenic fusion proteins hijack the TrxG homolog KMT2A and disrupt PcG activity to maintain pro-leukemogenic gene expression, though the mechanisms by which oncofusion proteins antagonize PcG proteins remain unclear. Here, we define the relationship between NUP98 oncofusion proteins and the non-canonical polycomb repressive complex 1.1 (PRC1.1) in leukemia using Menin-KMT2A inhibitors and targeted degradation of NUP98 fusion proteins. Eviction of the NUP98 fusion-Menin-KMT2A complex from chromatin is not sufficient to silence pro-leukemogenic genes. In the absence of PRC1.1, key oncogenes remain transcriptionally active. Transition to a repressed chromatin state requires the accumulation of PRC1.1 and repressive histone modifications. We show that PRC1.1 loss leads to resistance to small-molecule Menin-KMT2A inhibitors<span> </span><i>in vivo</i>. Therefore, a critical function of oncofusion proteins that hijack Menin-KMT2A activity is antagonizing repressive chromatin complexes.</div>
</section>',
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'description' => '<p>Epithelial-to-mesenchymal transition (EMT) renders epithelial cells migratory properties. While epigenetic and splicing changes have been implicated in EMT, the mechanisms governing their crosstalk remain poorly understood. Here we discovered that a C2H2 zinc finger protein, ZNF827, is strongly induced during various contexts of EMT, including in brain development and breast cancer metastasis, and is required for the molecular and phenotypic changes underlying EMT in these processes. Mechanistically, ZNF827 mediated these responses by orchestrating a large-scale remodelling of the splicing landscape by recruiting HDAC1 for epigenetic modulation of distinct genomic loci, thereby slowing RNA polymerase II progression and altering the splicing of genes encoding key EMT regulators in cis. Our findings reveal an unprecedented complexity of crosstalk between epigenetic landscape and splicing programme in governing EMT and identify ZNF827 as a master regulator coupling these processes during EMT in brain development and breast cancer metastasis.</p>',
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'authors' => 'Koenis DS, Medzikovic L, van Loenen PB, van Weeghel M, Huveneers S, Vos M, Evers-van Gogh IJ, Van den Bossche J, Speijer D, Kim Y, Wessels L, Zelcer N, Zwart W, Kalkhoven E, de Vries CJ',
'description' => '<p>Activation of macrophages by inflammatory stimuli induces reprogramming of mitochondrial metabolism to support the production of pro-inflammatory cytokines and nitric oxide. Hallmarks of this metabolic rewiring are downregulation of α-ketoglutarate formation by isocitrate dehydrogenase (IDH) and accumulation of glutamine-derived succinate, which enhances the inflammatory response via the activity of succinate dehydrogenase (SDH). Here, we identify the nuclear receptor Nur77 (Nr4a1) as a key upstream transcriptional regulator of this pro-inflammatory metabolic switch in macrophages. Nur77-deficient macrophages fail to downregulate IDH expression and accumulate higher levels of succinate and other TCA cycle-derived metabolites in response to inflammatory stimulation in a glutamine-independent manner. Consequently, these macrophages produce more nitric oxide and pro-inflammatory cytokines in an SDH-dependent manner. In vivo, bone marrow Nur77 deficiency exacerbates atherosclerosis development and leads to increased circulating succinate levels. In summary, Nur77 induces an anti-inflammatory metabolic state in macrophages that protects against chronic inflammatory diseases such as atherosclerosis.</p>',
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<p><small><strong> Figure 1. Western blot analysis using the Diagenode monoclonal antibody against the HA protein tag </strong><br />Western blot was performed on whole cell extracts from HEK293 cells transfected with an HA-tagged expression vector using the Diagenode monoclonal antibody directed against HA (Cat. No. MAb-190-050). The antibody was used at a dilution of 1:1,000. Figure 1 shows the results for untransfected cells, used as a negative control (lane 1) and for cells transfected with a HA-tagged protein (lane 2). The MW marker (in kDa) is shown on the left. A single band is clearly visible in lane 2, but absent in lane 1 showing the high specificity of the HA antibody. </small></p>
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'description' => '<p><strong></strong></p>
<section id="author-highlights-abstract" property="abstract" typeof="Text" role="doc-abstract">
<h2 property="name">Highlights</h2>
<div id="abspara0020" role="paragraph">
<div id="ulist0010" role="list">
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<div id="p0010" role="paragraph">Degradation of NUP98-fp halts nascent transcription of key oncogenes within 1 h</div>
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<div class="content">
<div id="p0020" role="paragraph">PRC1.1 is needed for stable gene repression but not for acute transcriptional changes</div>
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<div class="content">
<div id="p0025" role="paragraph">PRC1.1 is required for leukemia cell differentiation upon Menin inhibitor treatment</div>
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<div id="abspara0010" role="paragraph">Control of stem cell-associated genes by Trithorax group (TrxG) and Polycomb group (PcG) proteins is frequently misregulated in cancer. In leukemia, oncogenic fusion proteins hijack the TrxG homolog KMT2A and disrupt PcG activity to maintain pro-leukemogenic gene expression, though the mechanisms by which oncofusion proteins antagonize PcG proteins remain unclear. Here, we define the relationship between NUP98 oncofusion proteins and the non-canonical polycomb repressive complex 1.1 (PRC1.1) in leukemia using Menin-KMT2A inhibitors and targeted degradation of NUP98 fusion proteins. Eviction of the NUP98 fusion-Menin-KMT2A complex from chromatin is not sufficient to silence pro-leukemogenic genes. In the absence of PRC1.1, key oncogenes remain transcriptionally active. Transition to a repressed chromatin state requires the accumulation of PRC1.1 and repressive histone modifications. We show that PRC1.1 loss leads to resistance to small-molecule Menin-KMT2A inhibitors<span> </span><i>in vivo</i>. Therefore, a critical function of oncofusion proteins that hijack Menin-KMT2A activity is antagonizing repressive chromatin complexes.</div>
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'date' => '2024-11-26',
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'description' => '<p>Epithelial-to-mesenchymal transition (EMT) renders epithelial cells migratory properties. While epigenetic and splicing changes have been implicated in EMT, the mechanisms governing their crosstalk remain poorly understood. Here we discovered that a C2H2 zinc finger protein, ZNF827, is strongly induced during various contexts of EMT, including in brain development and breast cancer metastasis, and is required for the molecular and phenotypic changes underlying EMT in these processes. Mechanistically, ZNF827 mediated these responses by orchestrating a large-scale remodelling of the splicing landscape by recruiting HDAC1 for epigenetic modulation of distinct genomic loci, thereby slowing RNA polymerase II progression and altering the splicing of genes encoding key EMT regulators in cis. Our findings reveal an unprecedented complexity of crosstalk between epigenetic landscape and splicing programme in governing EMT and identify ZNF827 as a master regulator coupling these processes during EMT in brain development and breast cancer metastasis.</p>',
'date' => '2022-08-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/35941369',
'doi' => '10.1038/s41556-022-00971-3',
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'name' => 'Nuclear Receptor Nur77 Limits the Macrophage Inflammatory Response through Transcriptional Reprogramming of Mitochondrial Metabolism.',
'authors' => 'Koenis DS, Medzikovic L, van Loenen PB, van Weeghel M, Huveneers S, Vos M, Evers-van Gogh IJ, Van den Bossche J, Speijer D, Kim Y, Wessels L, Zelcer N, Zwart W, Kalkhoven E, de Vries CJ',
'description' => '<p>Activation of macrophages by inflammatory stimuli induces reprogramming of mitochondrial metabolism to support the production of pro-inflammatory cytokines and nitric oxide. Hallmarks of this metabolic rewiring are downregulation of α-ketoglutarate formation by isocitrate dehydrogenase (IDH) and accumulation of glutamine-derived succinate, which enhances the inflammatory response via the activity of succinate dehydrogenase (SDH). Here, we identify the nuclear receptor Nur77 (Nr4a1) as a key upstream transcriptional regulator of this pro-inflammatory metabolic switch in macrophages. Nur77-deficient macrophages fail to downregulate IDH expression and accumulate higher levels of succinate and other TCA cycle-derived metabolites in response to inflammatory stimulation in a glutamine-independent manner. Consequently, these macrophages produce more nitric oxide and pro-inflammatory cytokines in an SDH-dependent manner. In vivo, bone marrow Nur77 deficiency exacerbates atherosclerosis development and leads to increased circulating succinate levels. In summary, Nur77 induces an anti-inflammatory metabolic state in macrophages that protects against chronic inflammatory diseases such as atherosclerosis.</p>',
'date' => '2018-08-21',
'pmid' => 'http://www.pubmed.gov/30134173',
'doi' => '10.1016/j.celrep.2018.07.065',
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<p><small><strong> Figure 1. Western blot analysis using the Diagenode monoclonal antibody against the HA protein tag </strong><br />Western blot was performed on whole cell extracts from HEK293 cells transfected with an HA-tagged expression vector using the Diagenode monoclonal antibody directed against HA (Cat. No. MAb-190-050). The antibody was used at a dilution of 1:1,000. Figure 1 shows the results for untransfected cells, used as a negative control (lane 1) and for cells transfected with a HA-tagged protein (lane 2). The MW marker (in kDa) is shown on the left. A single band is clearly visible in lane 2, but absent in lane 1 showing the high specificity of the HA antibody. </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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<li>Cost-effective (requires less antibody per reaction)</li>
<li>Batch-specific data is available on the website</li>
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<section id="author-highlights-abstract" property="abstract" typeof="Text" role="doc-abstract">
<h2 property="name">Highlights</h2>
<div id="abspara0020" role="paragraph">
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<div id="u0015" role="listitem">
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<div id="p0015" role="paragraph">NUP98-fp loss results in accumulation of PRC1.1 and repressive histone modifications</div>
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<div id="u0020" role="listitem">
<div class="content">
<div id="p0020" role="paragraph">PRC1.1 is needed for stable gene repression but not for acute transcriptional changes</div>
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<div id="u0025" role="listitem">
<div class="content">
<div id="p0025" role="paragraph">PRC1.1 is required for leukemia cell differentiation upon Menin inhibitor treatment</div>
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<div id="abspara0010" role="paragraph">Control of stem cell-associated genes by Trithorax group (TrxG) and Polycomb group (PcG) proteins is frequently misregulated in cancer. In leukemia, oncogenic fusion proteins hijack the TrxG homolog KMT2A and disrupt PcG activity to maintain pro-leukemogenic gene expression, though the mechanisms by which oncofusion proteins antagonize PcG proteins remain unclear. Here, we define the relationship between NUP98 oncofusion proteins and the non-canonical polycomb repressive complex 1.1 (PRC1.1) in leukemia using Menin-KMT2A inhibitors and targeted degradation of NUP98 fusion proteins. Eviction of the NUP98 fusion-Menin-KMT2A complex from chromatin is not sufficient to silence pro-leukemogenic genes. In the absence of PRC1.1, key oncogenes remain transcriptionally active. Transition to a repressed chromatin state requires the accumulation of PRC1.1 and repressive histone modifications. We show that PRC1.1 loss leads to resistance to small-molecule Menin-KMT2A inhibitors<span> </span><i>in vivo</i>. Therefore, a critical function of oncofusion proteins that hijack Menin-KMT2A activity is antagonizing repressive chromatin complexes.</div>
</section>',
'date' => '2024-11-26',
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'description' => '<p>Epithelial-to-mesenchymal transition (EMT) renders epithelial cells migratory properties. While epigenetic and splicing changes have been implicated in EMT, the mechanisms governing their crosstalk remain poorly understood. Here we discovered that a C2H2 zinc finger protein, ZNF827, is strongly induced during various contexts of EMT, including in brain development and breast cancer metastasis, and is required for the molecular and phenotypic changes underlying EMT in these processes. Mechanistically, ZNF827 mediated these responses by orchestrating a large-scale remodelling of the splicing landscape by recruiting HDAC1 for epigenetic modulation of distinct genomic loci, thereby slowing RNA polymerase II progression and altering the splicing of genes encoding key EMT regulators in cis. Our findings reveal an unprecedented complexity of crosstalk between epigenetic landscape and splicing programme in governing EMT and identify ZNF827 as a master regulator coupling these processes during EMT in brain development and breast cancer metastasis.</p>',
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'description' => '<p>Activation of macrophages by inflammatory stimuli induces reprogramming of mitochondrial metabolism to support the production of pro-inflammatory cytokines and nitric oxide. Hallmarks of this metabolic rewiring are downregulation of α-ketoglutarate formation by isocitrate dehydrogenase (IDH) and accumulation of glutamine-derived succinate, which enhances the inflammatory response via the activity of succinate dehydrogenase (SDH). Here, we identify the nuclear receptor Nur77 (Nr4a1) as a key upstream transcriptional regulator of this pro-inflammatory metabolic switch in macrophages. Nur77-deficient macrophages fail to downregulate IDH expression and accumulate higher levels of succinate and other TCA cycle-derived metabolites in response to inflammatory stimulation in a glutamine-independent manner. Consequently, these macrophages produce more nitric oxide and pro-inflammatory cytokines in an SDH-dependent manner. In vivo, bone marrow Nur77 deficiency exacerbates atherosclerosis development and leads to increased circulating succinate levels. In summary, Nur77 induces an anti-inflammatory metabolic state in macrophages that protects against chronic inflammatory diseases such as atherosclerosis.</p>',
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<p><small><strong> Figure 1. Western blot analysis using the Diagenode monoclonal antibody against the HA protein tag </strong><br />Western blot was performed on whole cell extracts from HEK293 cells transfected with an HA-tagged expression vector using the Diagenode monoclonal antibody directed against HA (Cat. No. MAb-190-050). The antibody was used at a dilution of 1:1,000. Figure 1 shows the results for untransfected cells, used as a negative control (lane 1) and for cells transfected with a HA-tagged protein (lane 2). The MW marker (in kDa) is shown on the left. A single band is clearly visible in lane 2, but absent in lane 1 showing the high specificity of the HA antibody. </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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<p><span style="font-weight: 400;">Diagenode’s highly validated antibodies:</span></p>
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<li>Cost-effective (requires less antibody per reaction)</li>
<li>Batch-specific data is available on the website</li>
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<div id="u0015" role="listitem">
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<div class="content">
<div id="p0020" role="paragraph">PRC1.1 is needed for stable gene repression but not for acute transcriptional changes</div>
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<div id="u0025" role="listitem">
<div class="content">
<div id="p0025" role="paragraph">PRC1.1 is required for leukemia cell differentiation upon Menin inhibitor treatment</div>
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'description' => '<p>Activation of macrophages by inflammatory stimuli induces reprogramming of mitochondrial metabolism to support the production of pro-inflammatory cytokines and nitric oxide. Hallmarks of this metabolic rewiring are downregulation of α-ketoglutarate formation by isocitrate dehydrogenase (IDH) and accumulation of glutamine-derived succinate, which enhances the inflammatory response via the activity of succinate dehydrogenase (SDH). Here, we identify the nuclear receptor Nur77 (Nr4a1) as a key upstream transcriptional regulator of this pro-inflammatory metabolic switch in macrophages. Nur77-deficient macrophages fail to downregulate IDH expression and accumulate higher levels of succinate and other TCA cycle-derived metabolites in response to inflammatory stimulation in a glutamine-independent manner. Consequently, these macrophages produce more nitric oxide and pro-inflammatory cytokines in an SDH-dependent manner. In vivo, bone marrow Nur77 deficiency exacerbates atherosclerosis development and leads to increased circulating succinate levels. In summary, Nur77 induces an anti-inflammatory metabolic state in macrophages that protects against chronic inflammatory diseases such as atherosclerosis.</p>',
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)
$chipseq_service = array(
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)
$labelize = object(Closure) {
}
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'antibody_id' => '188',
'name' => 'HA tag Antibody (sample size)',
'description' => '',
'label1' => '',
'info1' => '',
'label2' => '',
'info2' => '',
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'info3' => '',
'format' => '10 µg',
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'price_USD' => '115',
'price_GBP' => '100',
'price_JPY' => '16450',
'price_CNY' => '',
'price_AUD' => '288',
'country' => 'ALL',
'except_countries' => 'None',
'quote' => false,
'in_stock' => false,
'featured' => false,
'no_promo' => false,
'online' => true,
'master' => false,
'last_datasheet_update' => '0000-00-00',
'slug' => 'ha-tag-monoclonal-antibody-classic-10-ug',
'meta_title' => 'HA tag Monoclonal Antibody | Diagenode',
'meta_keywords' => 'HA tag monoclonal antibody - Classic (sample size)',
'meta_description' => 'HA tag Monoclonal Antibody validated in IP, WB and ChIP-qPCR . Batch-specific data available on the website. ',
'modified' => '2022-01-05 15:44:01',
'created' => '2016-06-22 10:18:33',
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'id' => '200',
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)
)
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$label = '<img src="/img/banners/banner-customizer-back.png" alt=""/>'
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'position' => '10',
'parent_id' => '40',
'name' => 'ChIP-qPCR (ab)',
'description' => '',
'in_footer' => false,
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'online' => true,
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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',
'modified' => '2016-01-20 11:30:24',
'created' => '2015-10-20 11:45:36',
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'id' => '5066',
'product_id' => '2005',
'application_id' => '43'
)
)
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(int) 0 => 'chip-qpcr-antibodies'
)
$applications = array(
'id' => '43',
'position' => '10',
'parent_id' => '40',
'name' => 'ChIP-qPCR (ab)',
'description' => '',
'in_footer' => false,
'in_menu' => false,
'online' => true,
'tabular' => true,
'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',
'modified' => '2016-01-20 11:30:24',
'created' => '2015-10-20 11:45:36',
'locale' => 'zho'
)
$description = ''
$name = 'ChIP-qPCR (ab)'
$document = array(
'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>',
'image_id' => null,
'type' => 'Poster',
'url' => 'files/posters/Antibodies_you_can_trust_Poster.pdf',
'slug' => 'antibodies-you-can-trust-poster',
'meta_keywords' => '',
'meta_description' => '',
'modified' => '2015-10-01 20:18:31',
'created' => '2015-07-03 16:05:15',
'ProductsDocument' => array(
'id' => '2115',
'product_id' => '2005',
'document_id' => '11'
)
)
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'id' => '772',
'name' => 'HA tag antibody SDS ES es',
'language' => 'es',
'url' => 'files/SDS/HA/SDS-C15200190-HA_tag_Antibody-ES-es-GHS_2_0.pdf',
'countries' => 'ES',
'modified' => '2020-09-21 15:30:14',
'created' => '2020-09-21 15:30:14',
'ProductsSafetySheet' => array(
'id' => '1406',
'product_id' => '2005',
'safety_sheet_id' => '772'
)
)
$publication = array(
'id' => '3313',
'name' => 'FBXO32 promotes microenvironment underlying epithelial-mesenchymal transition via CtBP1 during tumour metastasis and brain development',
'authors' => 'Sahu S.K. et al.',
'description' => '<p>The set of events that convert adherent epithelial cells into migratory cells are collectively known as epithelial-mesenchymal transition (EMT). EMT is involved during development, for example, in triggering neural crest migration, and in pathogenesis such as metastasis. Here we discover FBXO32, an E3 ubiquitin ligase, to be critical for hallmark gene expression and phenotypic changes underlying EMT. Interestingly, FBXO32 directly ubiquitinates CtBP1, which is required for its stability and nuclear retention. This is essential for epigenetic remodeling and transcriptional induction of CtBP1 target genes, which create a suitable microenvironment for EMT progression. FBXO32 is also amplified in metastatic cancers and its depletion in a NSG mouse xenograft model inhibits tumor growth and metastasis. In addition, FBXO32 is essential for neuronal EMT during brain development. Together, these findings establish that FBXO32 acts as an upstream regulator of EMT by governing the gene expression program underlying this process during development and disease.</p>',
'date' => '2017-11-15',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/29142217',
'doi' => '',
'modified' => '2018-01-12 17:29:21',
'created' => '2018-01-12 17:29:21',
'ProductsPublication' => array(
'id' => '2570',
'product_id' => '2005',
'publication_id' => '3313'
)
)
$externalLink = ' <a href="https://www.ncbi.nlm.nih.gov/pubmed/29142217" 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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