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<p><small><strong> Figure 1. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against human MycK323ac (Cat. No. C15410346). The plates were coated with the peptide used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 1), the titer of the antibody was estimated to be 1:8,000.</small></p>
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<p><small><strong> Figure 2. Immunofluorescence using the Diagenode antibody directed against MycK323ac</strong><br />HeLa cells were stained with the Diagenode antibody against MycK323ac (cat. No. C15410346) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 1% BSA. The cells were immunofluorescently labeled with the MycK323ac antibody (middle) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The left panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</small></p>
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<p>Polyclonal antibody raised in rabbit against Myc (v-myc myelocytomatosis viral oncogene homolog) acetylated at lysine 323 (MycK323ac) using a KLH-conjugated synthetic peptide.</p>',
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<p><small><strong> Figure 1. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against human MycK323ac (Cat. No. C15410346). The plates were coated with the peptide used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 1), the titer of the antibody was estimated to be 1:8,000.</small></p>
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<p><small><strong> Figure 2. Immunofluorescence using the Diagenode antibody directed against MycK323ac</strong><br />HeLa cells were stained with the Diagenode antibody against MycK323ac (cat. No. C15410346) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 1% BSA. The cells were immunofluorescently labeled with the MycK323ac antibody (middle) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The left panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</small></p>
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<p><small><strong> Figure 2. Immunofluorescence using the Diagenode antibody directed against MycK323ac</strong><br />HeLa cells were stained with the Diagenode antibody against MycK323ac (cat. No. C15410346) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 1% BSA. The cells were immunofluorescently labeled with the MycK323ac antibody (middle) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The left panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15200229-IF.jpg" alt="" height="245" width="256" /></p>
<p><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
<p><sup>HeLa cells transfected with a Cas9 expression vector (left) or untransfected cells (right) were fixed in methanol at -20°C, permeabilized with acetone at -20°C and blocked with PBS containing 2% BSA. The cells were stained with the Cas9 C-terminal antibody (Cat. No. C15200229) diluted 1:400, followed by incubation with an anti-mouse secondary antibody coupled to AF488. The bottom images show counter-staining of the nuclei with Hoechst 33342.</sup></p>
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<p><small><strong> Figure 1. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against human MycK323ac (Cat. No. C15410346). The plates were coated with the peptide used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 1), the titer of the antibody was estimated to be 1:8,000.</small></p>
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<p><small><strong> Figure 2. Immunofluorescence using the Diagenode antibody directed against MycK323ac</strong><br />HeLa cells were stained with the Diagenode antibody against MycK323ac (cat. No. C15410346) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 1% BSA. The cells were immunofluorescently labeled with the MycK323ac antibody (middle) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The left panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</small></p>
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<p><small><strong> Figure 1. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against human MycK323ac (Cat. No. C15410346). The plates were coated with the peptide used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 1), the titer of the antibody was estimated to be 1:8,000.</small></p>
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<p><small><strong> Figure 2. Immunofluorescence using the Diagenode antibody directed against MycK323ac</strong><br />HeLa cells were stained with the Diagenode antibody against MycK323ac (cat. No. C15410346) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 1% BSA. The cells were immunofluorescently labeled with the MycK323ac antibody (middle) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The left panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</small></p>
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<p><small><strong> Figure 2. Immunofluorescence using the Diagenode antibody directed against MycK323ac</strong><br />HeLa cells were stained with the Diagenode antibody against MycK323ac (cat. No. C15410346) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 1% BSA. The cells were immunofluorescently labeled with the MycK323ac antibody (middle) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The left panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</small></p>
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<p><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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<li><span style="font-weight: 400;"> Expert technical support</span></li>
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<h5><sup>Check our selection of antibodies validated in IF.</sup></h5>'
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'description' => '<p>Polyclonal antibody raised in rabbit against Myc (v-myc myelocytomatosis viral oncogene homolog) acetylated at lysine 323 (MycK323ac) using a KLH-conjugated synthetic peptide.</p>',
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'description' => '<p><span>High-fat diet (HFD)-induced obesity is a cause of resistant hypertension. We have shown a possible link between histone deacetylases (HDACs) and renal angiotensinogen (Agt) upregulation in the HFD-induced hypertension, whereas the underlying mechanisms remain to be elucidated. Here, using a HDAC1/2 inhibitor romidepsin (FK228) and siRNAs, we determined roles of HDAC1 and HDAC2 in HFD-induced hypertension and found the pathologic signaling axis between HDAC1 and Agt transcription. Treatment with FK228 canceled the increased blood pressure of male C57BL/6 mice induced by HFD. FK228 also blocked upregulation of renal Agt mRNA, protein, angiotensin II (Ang II) or serum Ang II. Activation and nuclear accumulation of both HDAC1 and HDAC2 occurred in the HFD group. The HFD-induced HDAC activation was associated with an increase in deacetylated c-Myc transcription factor. Silencing of HDAC1, HDAC2 or c-Myc in HRPTEpi cells decreased Agt expression. However, only HDAC1 knockdown, but not HDAC2, increased c-Myc acetylation, suggesting selective roles in two enzymes. Chromatin immunoprecipitation assay revealed that HFD induced the binding of HDAC1 and deacetylated c-Myc at the Agt gene promoter. A putative c-Myc binding sequence in the promotor region was necessary for Agt transcription. Inhibition of c-Myc downregulated Agt and Ang II levels in kidney and serum, ameliorating HFD-induced hypertension. Thus, the abnormal HDAC1/2 in the kidney may be responsible for the upregulation of the Agt gene expression and hypertension. The results expose the pathologic HDAC1/c-myc signaling axis in kidney as a promising therapeutic target for obesity-associated resistant hypertension.</span></p>',
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'doi' => '10.1016/j.biopha.2023.114926',
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<p><small><strong> Figure 1. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against human MycK323ac (Cat. No. C15410346). The plates were coated with the peptide used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 1), the titer of the antibody was estimated to be 1:8,000.</small></p>
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<p><small><strong> Figure 2. Immunofluorescence using the Diagenode antibody directed against MycK323ac</strong><br />HeLa cells were stained with the Diagenode antibody against MycK323ac (cat. No. C15410346) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 1% BSA. The cells were immunofluorescently labeled with the MycK323ac antibody (middle) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The left panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</small></p>
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<p><small><strong> Figure 1. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against human MycK323ac (Cat. No. C15410346). The plates were coated with the peptide used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 1), the titer of the antibody was estimated to be 1:8,000.</small></p>
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<p><small><strong> Figure 2. Immunofluorescence using the Diagenode antibody directed against MycK323ac</strong><br />HeLa cells were stained with the Diagenode antibody against MycK323ac (cat. No. C15410346) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 1% BSA. The cells were immunofluorescently labeled with the MycK323ac antibody (middle) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The left panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</small></p>
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'description' => 'Myc (UniProtKB/Swiss-Prot entry P01106) participates in the regulation of gene transcription. Myc seems to activate the
transcription of growth-related genes. It specifically recognizes the core sequence 5’-CAC[GA]TG-3’ but also binds DNA in a
non-specific manner. Overexpression of MYC is implicated in the etiology of a variety of hematopoietic tumors.',
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<p><small><strong> Figure 1. Determination of the antibody titer</strong><br />To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against human MycK323ac (Cat. No. C15410346). The plates were coated with the peptide used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 1), the titer of the antibody was estimated to be 1:8,000.</small></p>
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<p><small><strong> Figure 2. Immunofluorescence using the Diagenode antibody directed against MycK323ac</strong><br />HeLa cells were stained with the Diagenode antibody against MycK323ac (cat. No. C15410346) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 1% BSA. The cells were immunofluorescently labeled with the MycK323ac antibody (middle) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The left panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</small></p>
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<p><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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'name' => 'MycK323ac polyclonal antibody',
'description' => '<p>Polyclonal antibody raised in rabbit against Myc (v-myc myelocytomatosis viral oncogene homolog) acetylated at lysine 323 (MycK323ac) using a KLH-conjugated synthetic peptide.</p>',
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'description' => '<p><span>High-fat diet (HFD)-induced obesity is a cause of resistant hypertension. We have shown a possible link between histone deacetylases (HDACs) and renal angiotensinogen (Agt) upregulation in the HFD-induced hypertension, whereas the underlying mechanisms remain to be elucidated. Here, using a HDAC1/2 inhibitor romidepsin (FK228) and siRNAs, we determined roles of HDAC1 and HDAC2 in HFD-induced hypertension and found the pathologic signaling axis between HDAC1 and Agt transcription. Treatment with FK228 canceled the increased blood pressure of male C57BL/6 mice induced by HFD. FK228 also blocked upregulation of renal Agt mRNA, protein, angiotensin II (Ang II) or serum Ang II. Activation and nuclear accumulation of both HDAC1 and HDAC2 occurred in the HFD group. The HFD-induced HDAC activation was associated with an increase in deacetylated c-Myc transcription factor. Silencing of HDAC1, HDAC2 or c-Myc in HRPTEpi cells decreased Agt expression. However, only HDAC1 knockdown, but not HDAC2, increased c-Myc acetylation, suggesting selective roles in two enzymes. Chromatin immunoprecipitation assay revealed that HFD induced the binding of HDAC1 and deacetylated c-Myc at the Agt gene promoter. A putative c-Myc binding sequence in the promotor region was necessary for Agt transcription. Inhibition of c-Myc downregulated Agt and Ang II levels in kidney and serum, ameliorating HFD-induced hypertension. Thus, the abnormal HDAC1/2 in the kidney may be responsible for the upregulation of the Agt gene expression and hypertension. The results expose the pathologic HDAC1/c-myc signaling axis in kidney as a promising therapeutic target for obesity-associated resistant hypertension.</span></p>',
'date' => '2023-05-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/37244179',
'doi' => '10.1016/j.biopha.2023.114926',
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<p><small><strong> Figure 2. Immunofluorescence using the Diagenode antibody directed against MycK323ac</strong><br />HeLa cells were stained with the Diagenode antibody against MycK323ac (cat. No. C15410346) and with DAPI. Cells were fixed with 4% formaldehyde for 10’ and blocked with PBS/TX-100 containing 1% BSA. The cells were immunofluorescently labeled with the MycK323ac antibody (middle) diluted 1:500 in blocking solution followed by an anti-rabbit antibody conjugated to Alexa488. The left panel shows staining of the nuclei with DAPI. A merge of the two stainings is shown on the right.</small></p>
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<p>Diagenode offers huge selection of highly sensitive antibodies validated in IF.</p>
<p><img src="https://www.diagenode.com/img/product/antibodies/C15200229-IF.jpg" alt="" height="245" width="256" /></p>
<p><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
<p><sup>HeLa cells transfected with a Cas9 expression vector (left) or untransfected cells (right) were fixed in methanol at -20°C, permeabilized with acetone at -20°C and blocked with PBS containing 2% BSA. The cells were stained with the Cas9 C-terminal antibody (Cat. No. C15200229) diluted 1:400, followed by incubation with an anti-mouse secondary antibody coupled to AF488. The bottom images show counter-staining of the nuclei with Hoechst 33342.</sup></p>
<h5><sup>Check our selection of antibodies validated in IF.</sup></h5>'
$name = 'IF'
$document = array(
'id' => '984',
'name' => 'MycK323ac polyclonal antibody',
'description' => '<p>Polyclonal antibody raised in rabbit against Myc (v-myc myelocytomatosis viral oncogene homolog) acetylated at lysine 323 (MycK323ac) using a KLH-conjugated synthetic peptide.</p>',
'image_id' => null,
'type' => 'Datasheet',
'url' => 'files/products/antibodies/Datasheet_MycK323ac_C15410346.pdf',
'slug' => 'myck323ac-polyclonal-antibody',
'meta_keywords' => '',
'meta_description' => '',
'modified' => '2018-01-03 11:16:25',
'created' => '2018-01-03 11:16:25',
'ProductsDocument' => array(
'id' => '2492',
'product_id' => '2925',
'document_id' => '984'
)
)
$sds = array(
'id' => '2196',
'name' => 'MycK323ac Antibody SDS ES es',
'language' => 'es',
'url' => 'files/SDS/MycK323ac/SDS-C15410346-MycK323ac_Antibody-ES-es-GHS_2_0.pdf',
'countries' => 'ES',
'modified' => '2022-08-29 09:48:44',
'created' => '2022-08-29 09:48:44',
'ProductsSafetySheet' => array(
'id' => '3838',
'product_id' => '2925',
'safety_sheet_id' => '2196'
)
)
$publication = array(
'id' => '4797',
'name' => 'Pathologic HDAC1/c-Myc signaling axis is responsible forangiotensinogen transcription and hypertension induced by high-fat diet.',
'authors' => 'Youn E.K. et al.',
'description' => '<p><span>High-fat diet (HFD)-induced obesity is a cause of resistant hypertension. We have shown a possible link between histone deacetylases (HDACs) and renal angiotensinogen (Agt) upregulation in the HFD-induced hypertension, whereas the underlying mechanisms remain to be elucidated. Here, using a HDAC1/2 inhibitor romidepsin (FK228) and siRNAs, we determined roles of HDAC1 and HDAC2 in HFD-induced hypertension and found the pathologic signaling axis between HDAC1 and Agt transcription. Treatment with FK228 canceled the increased blood pressure of male C57BL/6 mice induced by HFD. FK228 also blocked upregulation of renal Agt mRNA, protein, angiotensin II (Ang II) or serum Ang II. Activation and nuclear accumulation of both HDAC1 and HDAC2 occurred in the HFD group. The HFD-induced HDAC activation was associated with an increase in deacetylated c-Myc transcription factor. Silencing of HDAC1, HDAC2 or c-Myc in HRPTEpi cells decreased Agt expression. However, only HDAC1 knockdown, but not HDAC2, increased c-Myc acetylation, suggesting selective roles in two enzymes. Chromatin immunoprecipitation assay revealed that HFD induced the binding of HDAC1 and deacetylated c-Myc at the Agt gene promoter. A putative c-Myc binding sequence in the promotor region was necessary for Agt transcription. Inhibition of c-Myc downregulated Agt and Ang II levels in kidney and serum, ameliorating HFD-induced hypertension. Thus, the abnormal HDAC1/2 in the kidney may be responsible for the upregulation of the Agt gene expression and hypertension. The results expose the pathologic HDAC1/c-myc signaling axis in kidney as a promising therapeutic target for obesity-associated resistant hypertension.</span></p>',
'date' => '2023-05-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/37244179',
'doi' => '10.1016/j.biopha.2023.114926',
'modified' => '2023-06-15 08:37:22',
'created' => '2023-06-13 21:11:31',
'ProductsPublication' => array(
'id' => '6942',
'product_id' => '2925',
'publication_id' => '4797'
)
)
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View::_evaluate() - CORE/Cake/View/View.php, line 971
View::_render() - CORE/Cake/View/View.php, line 933
View::render() - CORE/Cake/View/View.php, line 473
Controller::render() - CORE/Cake/Controller/Controller.php, line 963
ProductsController::slug() - APP/Controller/ProductsController.php, line 1052
ReflectionMethod::invokeArgs() - [internal], line ??
Controller::invokeAction() - CORE/Cake/Controller/Controller.php, line 491
Dispatcher::_invoke() - CORE/Cake/Routing/Dispatcher.php, line 193
Dispatcher::dispatch() - CORE/Cake/Routing/Dispatcher.php, line 167
[main] - APP/webroot/index.php, line 118
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