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<p><span>Polyclonal antibody raised in rabbit against human p53 (tumor protein p53), using a KLH-conjugated synthetic peptide containing a sequence from the C-terminal part of the protein.</span></p>',
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP assays were performed using human U2OS cells, treated with camptothecin, the Diagenode antibody against p53 (Cat. No. C15410083) and optimized PCR primer sets for qPCR. ChIP was performed on sheared chromatin from 4 million cells. A titration of the antibody consisting of 1, 2, 5, and 10 µg per ChIP experiment was analysed. IgG (2 µg/IP) was used as negative IP control. qPCR was performed with primers for the p21 and GAS6 genes used as positive controls, and for GAPDH promoter and the Sat2 satellite repeat, used as negative controls. Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p>B. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-B.jpg" alt="p53 Antibody for ChIP-seq" style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>C. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-C.jpg" alt="p53 Antibody for ChIP-seq assay " style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>D. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-D.jpg" alt="p53 Antibody validated in ChIP-seq" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP was performed on sheared chromatin from 4 million U2OS cells using 1 µg of the Diagenode antibody against p53 (Cat. No. C15410083) as described above. The IP’d DNA was subsequently analysed on an Illumina HiSeq. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 51 bp tags were aligned to the human genome using the BWA algorithm. Figure 2 shows the peak distribution along the X-chromosome (fig 2A) and in 3 genomic regions of chromosome 6, 13 and 12, surrounding p21 (CDKN1A), GAS6 and MDM2, 3 known targets genes of p53 (fig 2B, C and D, respectively). </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410083_ELISA.jpg" alt="p53 Antibody ELISA validation " style="display: block; margin-left: auto; margin-right: auto;" /></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 Diagenode antibody directed against human p53 (Cat. No. C15410083), in antigen coated wells. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:308,000. </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410083_WB.jpg" alt="p53 Antibody validated in Western blot" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against p53</strong><br /> Nuclear extracts of HeLa cells (40 µg) were analysed by Western blot using the Diagenode antibody against p53 (Cat. No. C15410083) diluted 1:2,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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<td>Fig 1, 2</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 1-5 µg per IP.</small></p>',
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<p><span>Polyclonal antibody raised in rabbit against human p53 (tumor protein p53), using a KLH-conjugated synthetic peptide containing a sequence from the C-terminal part of the protein.</span></p>',
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410083-chip.jpg" alt="p53 Antibody ChIP Grade" caption="false" width="400" height="304" /></p>
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP assays were performed using human U2OS cells, treated with camptothecin, the Diagenode antibody against p53 (Cat. No. C15410083) and optimized PCR primer sets for qPCR. ChIP was performed on sheared chromatin from 4 million cells. A titration of the antibody consisting of 1, 2, 5, and 10 µg per ChIP experiment was analysed. IgG (2 µg/IP) was used as negative IP control. qPCR was performed with primers for the p21 and GAS6 genes used as positive controls, and for GAPDH promoter and the Sat2 satellite repeat, used as negative controls. Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p>A. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-A.jpg" alt="p53 Antibody ChIP-seq Grade" style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>B. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-B.jpg" alt="p53 Antibody for ChIP-seq" style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>C. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-C.jpg" alt="p53 Antibody for ChIP-seq assay " style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>D. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-D.jpg" alt="p53 Antibody validated in ChIP-seq" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP was performed on sheared chromatin from 4 million U2OS cells using 1 µg of the Diagenode antibody against p53 (Cat. No. C15410083) as described above. The IP’d DNA was subsequently analysed on an Illumina HiSeq. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 51 bp tags were aligned to the human genome using the BWA algorithm. Figure 2 shows the peak distribution along the X-chromosome (fig 2A) and in 3 genomic regions of chromosome 6, 13 and 12, surrounding p21 (CDKN1A), GAS6 and MDM2, 3 known targets genes of p53 (fig 2B, C and D, respectively). </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410083_ELISA.jpg" alt="p53 Antibody ELISA validation " style="display: block; margin-left: auto; margin-right: auto;" /></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 Diagenode antibody directed against human p53 (Cat. No. C15410083), in antigen coated wells. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:308,000. </small></p>
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<div class="small-9 columns">
<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against p53</strong><br /> Nuclear extracts of HeLa cells (40 µg) were analysed by Western blot using the Diagenode antibody against p53 (Cat. No. C15410083) diluted 1:2,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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<td>ChIP/ChIP-seq <sup>*</sup></td>
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<td>Fig 1, 2</td>
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<td>ELISA</td>
<td>1:4,000</td>
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP assays were performed using human U2OS cells, treated with camptothecin, the Diagenode antibody against p53 (Cat. No. C15410083) and optimized PCR primer sets for qPCR. ChIP was performed on sheared chromatin from 4 million cells. A titration of the antibody consisting of 1, 2, 5, and 10 µg per ChIP experiment was analysed. IgG (2 µg/IP) was used as negative IP control. qPCR was performed with primers for the p21 and GAS6 genes used as positive controls, and for GAPDH promoter and the Sat2 satellite repeat, used as negative controls. Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p>A. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-A.jpg" alt="p53 Antibody ChIP-seq Grade" style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>B. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-B.jpg" alt="p53 Antibody for ChIP-seq" style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>C. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-C.jpg" alt="p53 Antibody for ChIP-seq assay " style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>D. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-D.jpg" alt="p53 Antibody validated in ChIP-seq" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP was performed on sheared chromatin from 4 million U2OS cells using 1 µg of the Diagenode antibody against p53 (Cat. No. C15410083) as described above. The IP’d DNA was subsequently analysed on an Illumina HiSeq. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 51 bp tags were aligned to the human genome using the BWA algorithm. Figure 2 shows the peak distribution along the X-chromosome (fig 2A) and in 3 genomic regions of chromosome 6, 13 and 12, surrounding p21 (CDKN1A), GAS6 and MDM2, 3 known targets genes of p53 (fig 2B, C and D, respectively). </small></p>
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<div class="row">
<div class="small-6 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410083_ELISA.jpg" alt="p53 Antibody ELISA validation " style="display: block; margin-left: auto; margin-right: auto;" /></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 Diagenode antibody directed against human p53 (Cat. No. C15410083), in antigen coated wells. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:308,000. </small></p>
</div>
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<div class="row">
<div class="small-3 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410083_WB.jpg" alt="p53 Antibody validated in Western blot" style="display: block; margin-left: auto; margin-right: auto;" /></p>
</div>
<div class="small-9 columns">
<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against p53</strong><br /> Nuclear extracts of HeLa cells (40 µg) were analysed by Western blot using the Diagenode antibody against p53 (Cat. No. C15410083) diluted 1:2,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </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><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>
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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>
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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>
<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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<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>
<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>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' => 'Chitosan nano-vehicles as biocompatible delivering tools for a newAg(I)curcuminoid-Gboxin analog complex in cancer and inflammation therapy',
'authors' => 'Elbehairi, Serag Eldin I. and Ismail, Lamia A. and Alfaifi, Mohammad Y. andElshaarawy, Reda F.M. and Hafez, Hani S.',
'description' => '<p>A novel anticancer and anti-inflammatory agent based on hybrid curcuminoid-Gboxin analog (FLLL49-GbA) and its macromolecular silver(I) complex (Ag(I)FLLL49-GbA) have successfully synthesized. In addition, chitosan nanoparticles (CNPs) were used to encapsulate this macromolecular complex, targeting enhancing its therapeutic effect and minimizing its side impacts. The encapsulated Ag(I) complex was significantly triggered apoptosis (P < 0.05) with much more rapidly release of Ag(I)FLLL49-GbA from the CNPs at pH 5.3 than at pH 7.4, which is beneficial for cancer-targeted drug delivery. Free complex showed promising ability in preventing glucose uptake and lactate production coupled with cellular ATP depletion in cancer cells. Additionally, there was significant decrease in the inflammatory cytokines in breast cancer (MCF-7) and lung cancer (A549) cells with values of P < 0.01 and P < 0.001 after 24 h incubation. Furthermore, the death-inducing proteins have been significantly up-regulated (P < 0.01 to P < 0.001) after 36 h incubation of cancer cells. Consequently, the novel curcuminoid macromolecule showed significant feasibility in triggering the high expression of apoptotic caspases caspase 3, caspase 8, P53, and Bax (P < 0.01 to P < 0.001) after 48 h of chemotherapy. Noteworthy, the cytotoxicity of Ag(I)FLLL49-GbA was significantly increased toward cancer cells (MCF-7 > A549), while, reduced toward normal cells (HeLa) after loading on chitosan Nano-vehicles.</p>',
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'pmid' => 'https://doi.org/10.1016%2Fj.ijbiomac.2020.10.153',
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'authors' => 'Szołtysek K, Janus P, Zając G, Stokowy T, Walaszczyk A, Widłak W, Wojtaś B, Gielniewski B, Cockell S, Perkins ND, Kimmel M, Widlak P',
'description' => '<p>BACKGROUND: The cellular response to ionizing radiation involves activation of p53-dependent pathways and activation of the atypical NF-κB pathway. The crosstalk between these two transcriptional networks include (co)regulation of common gene targets. Here we looked for novel genes potentially (co)regulated by p53 and NF-κB using integrative genomics screening in human osteosarcoma U2-OS cells irradiated with a high dose (4 and 10 Gy). Radiation-induced expression in cells with silenced TP53 or RELA (coding the p65 NF-κB subunit) genes was analyzed by RNA-Seq while radiation-enhanced binding of p53 and RelA in putative regulatory regions was analyzed by ChIP-Seq, then selected candidates were validated by qPCR. RESULTS: We identified a subset of radiation-modulated genes whose expression was affected by silencing of both TP53 and RELA, and a subset of radiation-upregulated genes where radiation stimulated binding of both p53 and RelA. For three genes, namely IL4I1, SERPINE1, and CDKN1A, an antagonistic effect of the TP53 and RELA silencing was consistent with radiation-enhanced binding of both p53 and RelA. This suggested the possibility of a direct antagonistic (co)regulation by both factors: activation by NF-κB and inhibition by p53 of IL4I1, and activation by p53 and inhibition by NF-κB of CDKN1A and SERPINE1. On the other hand, radiation-enhanced binding of both p53 and RelA was observed in a putative regulatory region of the RRAD gene whose expression was downregulated both by TP53 and RELA silencing, which suggested a possibility of direct (co)activation by both factors. CONCLUSIONS: Four new candidates for genes directly co-regulated by NF-κB and p53 were revealed.</p>',
'date' => '2018-11-12',
'pmid' => 'http://www.pubmed.gov/30419821',
'doi' => '10.1186/s12864-018-5211-y',
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'description' => '<p>TREM2 mutations evoke neurodegenerative disorders, and recently genetic variants of this gene were correlated to increased risk of Alzheimer's disease. The signaling cascade originating from the TREM2 membrane receptor includes its binding partner TYROBP, BLNK adapter protein, and SYK kinase, which can be activated by p53. Moreover, in silico identification of a putative p53 response element (RE) at the TREM2 promoter led us to hypothesize that TREM2 and other pathway elements may be regulated in p53-dependent manner. To stimulate p53 in synergistic fashion, we exposed A549 lung cancer cells to actinomycin D and nutlin-3a (A + N). In these cells, exposure to A + N triggered expression of TREM2, TYROBP, SYK and BLNK in p53-dependent manner. TREM2 was also activated by A + N in U-2 OS osteosarcoma and A375 melanoma cell lines. Interestingly, nutlin-3a, a specific activator of p53, acting alone stimulated TREM2 in U-2 OS cells. Using in vitro mutagenesis, chromatin immunoprecipitation, and luciferase reporter assays, we confirmed the presence of the p53 RE in TREM2 promoter. Furthermore, activation of TREM2 and TYROBP by p53 was strongly inhibited by CHIR-98014, a potent and specific inhibitor of glycogen synthase kinase-3 (GSK-3). We conclude that TREM2 is a direct p53-target gene, and that activation of TREM2 by A + N or nutlin-3a may be critically dependent on GSK-3 function.</p>',
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'pmid' => 'http://www.pubmed.gov/29842899',
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'description' => '<p><span>Alternative names: <strong>TP53</strong>, <strong>P53</strong>, <strong>TRP53</strong>, <strong>LSF1</strong></span></p>
<p><span>Polyclonal antibody raised in rabbit against human p53 (tumor protein p53), using a KLH-conjugated synthetic peptide containing a sequence from the C-terminal part of the protein.</span></p>',
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410083-chip.jpg" alt="p53 Antibody ChIP Grade" caption="false" width="400" height="304" /></p>
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP assays were performed using human U2OS cells, treated with camptothecin, the Diagenode antibody against p53 (Cat. No. C15410083) and optimized PCR primer sets for qPCR. ChIP was performed on sheared chromatin from 4 million cells. A titration of the antibody consisting of 1, 2, 5, and 10 µg per ChIP experiment was analysed. IgG (2 µg/IP) was used as negative IP control. qPCR was performed with primers for the p21 and GAS6 genes used as positive controls, and for GAPDH promoter and the Sat2 satellite repeat, used as negative controls. Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p>A. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-A.jpg" alt="p53 Antibody ChIP-seq Grade" style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>B. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-B.jpg" alt="p53 Antibody for ChIP-seq" style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>C. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-C.jpg" alt="p53 Antibody for ChIP-seq assay " style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>D. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-D.jpg" alt="p53 Antibody validated in ChIP-seq" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP was performed on sheared chromatin from 4 million U2OS cells using 1 µg of the Diagenode antibody against p53 (Cat. No. C15410083) as described above. The IP’d DNA was subsequently analysed on an Illumina HiSeq. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 51 bp tags were aligned to the human genome using the BWA algorithm. Figure 2 shows the peak distribution along the X-chromosome (fig 2A) and in 3 genomic regions of chromosome 6, 13 and 12, surrounding p21 (CDKN1A), GAS6 and MDM2, 3 known targets genes of p53 (fig 2B, C and D, respectively). </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 Diagenode antibody directed against human p53 (Cat. No. C15410083), in antigen coated wells. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:308,000. </small></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against p53</strong><br /> Nuclear extracts of HeLa cells (40 µg) were analysed by Western blot using the Diagenode antibody against p53 (Cat. No. C15410083) diluted 1:2,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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<p><span>Polyclonal antibody raised in rabbit against human p53 (tumor protein p53), using a KLH-conjugated synthetic peptide containing a sequence from the C-terminal part of the protein.</span></p>',
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP assays were performed using human U2OS cells, treated with camptothecin, the Diagenode antibody against p53 (Cat. No. C15410083) and optimized PCR primer sets for qPCR. ChIP was performed on sheared chromatin from 4 million cells. A titration of the antibody consisting of 1, 2, 5, and 10 µg per ChIP experiment was analysed. IgG (2 µg/IP) was used as negative IP control. qPCR was performed with primers for the p21 and GAS6 genes used as positive controls, and for GAPDH promoter and the Sat2 satellite repeat, used as negative controls. Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p>B. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-B.jpg" alt="p53 Antibody for ChIP-seq" style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>C. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-C.jpg" alt="p53 Antibody for ChIP-seq assay " style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP was performed on sheared chromatin from 4 million U2OS cells using 1 µg of the Diagenode antibody against p53 (Cat. No. C15410083) as described above. The IP’d DNA was subsequently analysed on an Illumina HiSeq. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 51 bp tags were aligned to the human genome using the BWA algorithm. Figure 2 shows the peak distribution along the X-chromosome (fig 2A) and in 3 genomic regions of chromosome 6, 13 and 12, surrounding p21 (CDKN1A), GAS6 and MDM2, 3 known targets genes of p53 (fig 2B, C and D, respectively). </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 Diagenode antibody directed against human p53 (Cat. No. C15410083), in antigen coated wells. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:308,000. </small></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against p53</strong><br /> Nuclear extracts of HeLa cells (40 µg) were analysed by Western blot using the Diagenode antibody against p53 (Cat. No. C15410083) diluted 1:2,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP assays were performed using human U2OS cells, treated with camptothecin, the Diagenode antibody against p53 (Cat. No. C15410083) and optimized PCR primer sets for qPCR. ChIP was performed on sheared chromatin from 4 million cells. A titration of the antibody consisting of 1, 2, 5, and 10 µg per ChIP experiment was analysed. IgG (2 µg/IP) was used as negative IP control. qPCR was performed with primers for the p21 and GAS6 genes used as positive controls, and for GAPDH promoter and the Sat2 satellite repeat, used as negative controls. Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p>A. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-A.jpg" alt="p53 Antibody ChIP-seq Grade" style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>B. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-B.jpg" alt="p53 Antibody for ChIP-seq" style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>C. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-C.jpg" alt="p53 Antibody for ChIP-seq assay " style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>D. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-D.jpg" alt="p53 Antibody validated in ChIP-seq" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP was performed on sheared chromatin from 4 million U2OS cells using 1 µg of the Diagenode antibody against p53 (Cat. No. C15410083) as described above. The IP’d DNA was subsequently analysed on an Illumina HiSeq. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 51 bp tags were aligned to the human genome using the BWA algorithm. Figure 2 shows the peak distribution along the X-chromosome (fig 2A) and in 3 genomic regions of chromosome 6, 13 and 12, surrounding p21 (CDKN1A), GAS6 and MDM2, 3 known targets genes of p53 (fig 2B, C and D, respectively). </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 Diagenode antibody directed against human p53 (Cat. No. C15410083), in antigen coated wells. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:308,000. </small></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against p53</strong><br /> Nuclear extracts of HeLa cells (40 µg) were analysed by Western blot using the Diagenode antibody against p53 (Cat. No. C15410083) diluted 1:2,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </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>
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'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>
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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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<li>Sample sizes available</li>
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'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>
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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>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' => 'Chitosan nano-vehicles as biocompatible delivering tools for a newAg(I)curcuminoid-Gboxin analog complex in cancer and inflammation therapy',
'authors' => 'Elbehairi, Serag Eldin I. and Ismail, Lamia A. and Alfaifi, Mohammad Y. andElshaarawy, Reda F.M. and Hafez, Hani S.',
'description' => '<p>A novel anticancer and anti-inflammatory agent based on hybrid curcuminoid-Gboxin analog (FLLL49-GbA) and its macromolecular silver(I) complex (Ag(I)FLLL49-GbA) have successfully synthesized. In addition, chitosan nanoparticles (CNPs) were used to encapsulate this macromolecular complex, targeting enhancing its therapeutic effect and minimizing its side impacts. The encapsulated Ag(I) complex was significantly triggered apoptosis (P < 0.05) with much more rapidly release of Ag(I)FLLL49-GbA from the CNPs at pH 5.3 than at pH 7.4, which is beneficial for cancer-targeted drug delivery. Free complex showed promising ability in preventing glucose uptake and lactate production coupled with cellular ATP depletion in cancer cells. Additionally, there was significant decrease in the inflammatory cytokines in breast cancer (MCF-7) and lung cancer (A549) cells with values of P < 0.01 and P < 0.001 after 24 h incubation. Furthermore, the death-inducing proteins have been significantly up-regulated (P < 0.01 to P < 0.001) after 36 h incubation of cancer cells. Consequently, the novel curcuminoid macromolecule showed significant feasibility in triggering the high expression of apoptotic caspases caspase 3, caspase 8, P53, and Bax (P < 0.01 to P < 0.001) after 48 h of chemotherapy. Noteworthy, the cytotoxicity of Ag(I)FLLL49-GbA was significantly increased toward cancer cells (MCF-7 > A549), while, reduced toward normal cells (HeLa) after loading on chitosan Nano-vehicles.</p>',
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'authors' => 'Szołtysek K, Janus P, Zając G, Stokowy T, Walaszczyk A, Widłak W, Wojtaś B, Gielniewski B, Cockell S, Perkins ND, Kimmel M, Widlak P',
'description' => '<p>BACKGROUND: The cellular response to ionizing radiation involves activation of p53-dependent pathways and activation of the atypical NF-κB pathway. The crosstalk between these two transcriptional networks include (co)regulation of common gene targets. Here we looked for novel genes potentially (co)regulated by p53 and NF-κB using integrative genomics screening in human osteosarcoma U2-OS cells irradiated with a high dose (4 and 10 Gy). Radiation-induced expression in cells with silenced TP53 or RELA (coding the p65 NF-κB subunit) genes was analyzed by RNA-Seq while radiation-enhanced binding of p53 and RelA in putative regulatory regions was analyzed by ChIP-Seq, then selected candidates were validated by qPCR. RESULTS: We identified a subset of radiation-modulated genes whose expression was affected by silencing of both TP53 and RELA, and a subset of radiation-upregulated genes where radiation stimulated binding of both p53 and RelA. For three genes, namely IL4I1, SERPINE1, and CDKN1A, an antagonistic effect of the TP53 and RELA silencing was consistent with radiation-enhanced binding of both p53 and RelA. This suggested the possibility of a direct antagonistic (co)regulation by both factors: activation by NF-κB and inhibition by p53 of IL4I1, and activation by p53 and inhibition by NF-κB of CDKN1A and SERPINE1. On the other hand, radiation-enhanced binding of both p53 and RelA was observed in a putative regulatory region of the RRAD gene whose expression was downregulated both by TP53 and RELA silencing, which suggested a possibility of direct (co)activation by both factors. CONCLUSIONS: Four new candidates for genes directly co-regulated by NF-κB and p53 were revealed.</p>',
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'description' => '<p>TREM2 mutations evoke neurodegenerative disorders, and recently genetic variants of this gene were correlated to increased risk of Alzheimer's disease. The signaling cascade originating from the TREM2 membrane receptor includes its binding partner TYROBP, BLNK adapter protein, and SYK kinase, which can be activated by p53. Moreover, in silico identification of a putative p53 response element (RE) at the TREM2 promoter led us to hypothesize that TREM2 and other pathway elements may be regulated in p53-dependent manner. To stimulate p53 in synergistic fashion, we exposed A549 lung cancer cells to actinomycin D and nutlin-3a (A + N). In these cells, exposure to A + N triggered expression of TREM2, TYROBP, SYK and BLNK in p53-dependent manner. TREM2 was also activated by A + N in U-2 OS osteosarcoma and A375 melanoma cell lines. Interestingly, nutlin-3a, a specific activator of p53, acting alone stimulated TREM2 in U-2 OS cells. Using in vitro mutagenesis, chromatin immunoprecipitation, and luciferase reporter assays, we confirmed the presence of the p53 RE in TREM2 promoter. Furthermore, activation of TREM2 and TYROBP by p53 was strongly inhibited by CHIR-98014, a potent and specific inhibitor of glycogen synthase kinase-3 (GSK-3). We conclude that TREM2 is a direct p53-target gene, and that activation of TREM2 by A + N or nutlin-3a may be critically dependent on GSK-3 function.</p>',
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'name' => 'The Alzheimer's disease-associated TREM2 gene is regulated by p53 tumor suppressor protein.',
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<p><span>Polyclonal antibody raised in rabbit against human p53 (tumor protein p53), using a KLH-conjugated synthetic peptide containing a sequence from the C-terminal part of the protein.</span></p>',
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP assays were performed using human U2OS cells, treated with camptothecin, the Diagenode antibody against p53 (Cat. No. C15410083) and optimized PCR primer sets for qPCR. ChIP was performed on sheared chromatin from 4 million cells. A titration of the antibody consisting of 1, 2, 5, and 10 µg per ChIP experiment was analysed. IgG (2 µg/IP) was used as negative IP control. qPCR was performed with primers for the p21 and GAS6 genes used as positive controls, and for GAPDH promoter and the Sat2 satellite repeat, used as negative controls. Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p><small><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP was performed on sheared chromatin from 4 million U2OS cells using 1 µg of the Diagenode antibody against p53 (Cat. No. C15410083) as described above. The IP’d DNA was subsequently analysed on an Illumina HiSeq. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 51 bp tags were aligned to the human genome using the BWA algorithm. Figure 2 shows the peak distribution along the X-chromosome (fig 2A) and in 3 genomic regions of chromosome 6, 13 and 12, surrounding p21 (CDKN1A), GAS6 and MDM2, 3 known targets genes of p53 (fig 2B, C and D, respectively). </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 Diagenode antibody directed against human p53 (Cat. No. C15410083), in antigen coated wells. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:308,000. </small></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against p53</strong><br /> Nuclear extracts of HeLa cells (40 µg) were analysed by Western blot using the Diagenode antibody against p53 (Cat. No. C15410083) diluted 1:2,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP assays were performed using human U2OS cells, treated with camptothecin, the Diagenode antibody against p53 (Cat. No. C15410083) and optimized PCR primer sets for qPCR. ChIP was performed on sheared chromatin from 4 million cells. A titration of the antibody consisting of 1, 2, 5, and 10 µg per ChIP experiment was analysed. IgG (2 µg/IP) was used as negative IP control. qPCR was performed with primers for the p21 and GAS6 genes used as positive controls, and for GAPDH promoter and the Sat2 satellite repeat, used as negative controls. Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p>B. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-B.jpg" alt="p53 Antibody for ChIP-seq" style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>C. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-C.jpg" alt="p53 Antibody for ChIP-seq assay " style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against p53</strong><br /> Nuclear extracts of HeLa cells (40 µg) were analysed by Western blot using the Diagenode antibody against p53 (Cat. No. C15410083) diluted 1:2,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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'description' => '<p><span>Alternative names: <strong>TP53</strong>, <strong>P53</strong>, <strong>TRP53</strong>, <strong>LSF1</strong></span></p>
<p><span>Polyclonal antibody raised in rabbit against human <strong>p53 (tumor protein p53)</strong>, using a KLH-conjugated synthetic peptide containing a sequence from the C-terminal part of the protein.</span></p>',
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410083-chip.jpg" alt="p53 Antibody ChIP Grade" caption="false" width="400" height="304" /></p>
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP assays were performed using human U2OS cells, treated with camptothecin, the Diagenode antibody against p53 (Cat. No. C15410083) and optimized PCR primer sets for qPCR. ChIP was performed on sheared chromatin from 4 million cells. A titration of the antibody consisting of 1, 2, 5, and 10 µg per ChIP experiment was analysed. IgG (2 µg/IP) was used as negative IP control. qPCR was performed with primers for the p21 and GAS6 genes used as positive controls, and for GAPDH promoter and the Sat2 satellite repeat, used as negative controls. Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p>A. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-A.jpg" alt="p53 Antibody ChIP-seq Grade" style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>B. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-B.jpg" alt="p53 Antibody for ChIP-seq" style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>C. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-C.jpg" alt="p53 Antibody for ChIP-seq assay " style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>D. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-D.jpg" alt="p53 Antibody validated in ChIP-seq" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP was performed on sheared chromatin from 4 million U2OS cells using 1 µg of the Diagenode antibody against p53 (Cat. No. C15410083) as described above. The IP’d DNA was subsequently analysed on an Illumina HiSeq. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 51 bp tags were aligned to the human genome using the BWA algorithm. Figure 2 shows the peak distribution along the X-chromosome (fig 2A) and in 3 genomic regions of chromosome 6, 13 and 12, surrounding p21 (CDKN1A), GAS6 and MDM2, 3 known targets genes of p53 (fig 2B, C and D, respectively). </small></p>
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<div class="small-6 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410083_ELISA.jpg" alt="p53 Antibody ELISA validation " style="display: block; margin-left: auto; margin-right: auto;" /></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 Diagenode antibody directed against human p53 (Cat. No. C15410083), in antigen coated wells. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:308,000. </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410083_WB.jpg" alt="p53 Antibody validated in Western blot" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<div class="small-9 columns">
<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against p53</strong><br /> Nuclear extracts of HeLa cells (40 µg) were analysed by Western blot using the Diagenode antibody against p53 (Cat. No. C15410083) diluted 1:2,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </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>
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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>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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<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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'authors' => 'Elbehairi, Serag Eldin I. and Ismail, Lamia A. and Alfaifi, Mohammad Y. andElshaarawy, Reda F.M. and Hafez, Hani S.',
'description' => '<p>A novel anticancer and anti-inflammatory agent based on hybrid curcuminoid-Gboxin analog (FLLL49-GbA) and its macromolecular silver(I) complex (Ag(I)FLLL49-GbA) have successfully synthesized. In addition, chitosan nanoparticles (CNPs) were used to encapsulate this macromolecular complex, targeting enhancing its therapeutic effect and minimizing its side impacts. The encapsulated Ag(I) complex was significantly triggered apoptosis (P < 0.05) with much more rapidly release of Ag(I)FLLL49-GbA from the CNPs at pH 5.3 than at pH 7.4, which is beneficial for cancer-targeted drug delivery. Free complex showed promising ability in preventing glucose uptake and lactate production coupled with cellular ATP depletion in cancer cells. Additionally, there was significant decrease in the inflammatory cytokines in breast cancer (MCF-7) and lung cancer (A549) cells with values of P < 0.01 and P < 0.001 after 24 h incubation. Furthermore, the death-inducing proteins have been significantly up-regulated (P < 0.01 to P < 0.001) after 36 h incubation of cancer cells. Consequently, the novel curcuminoid macromolecule showed significant feasibility in triggering the high expression of apoptotic caspases caspase 3, caspase 8, P53, and Bax (P < 0.01 to P < 0.001) after 48 h of chemotherapy. Noteworthy, the cytotoxicity of Ag(I)FLLL49-GbA was significantly increased toward cancer cells (MCF-7 > A549), while, reduced toward normal cells (HeLa) after loading on chitosan Nano-vehicles.</p>',
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'description' => '<p>BACKGROUND: The cellular response to ionizing radiation involves activation of p53-dependent pathways and activation of the atypical NF-κB pathway. The crosstalk between these two transcriptional networks include (co)regulation of common gene targets. Here we looked for novel genes potentially (co)regulated by p53 and NF-κB using integrative genomics screening in human osteosarcoma U2-OS cells irradiated with a high dose (4 and 10 Gy). Radiation-induced expression in cells with silenced TP53 or RELA (coding the p65 NF-κB subunit) genes was analyzed by RNA-Seq while radiation-enhanced binding of p53 and RelA in putative regulatory regions was analyzed by ChIP-Seq, then selected candidates were validated by qPCR. RESULTS: We identified a subset of radiation-modulated genes whose expression was affected by silencing of both TP53 and RELA, and a subset of radiation-upregulated genes where radiation stimulated binding of both p53 and RelA. For three genes, namely IL4I1, SERPINE1, and CDKN1A, an antagonistic effect of the TP53 and RELA silencing was consistent with radiation-enhanced binding of both p53 and RelA. This suggested the possibility of a direct antagonistic (co)regulation by both factors: activation by NF-κB and inhibition by p53 of IL4I1, and activation by p53 and inhibition by NF-κB of CDKN1A and SERPINE1. On the other hand, radiation-enhanced binding of both p53 and RelA was observed in a putative regulatory region of the RRAD gene whose expression was downregulated both by TP53 and RELA silencing, which suggested a possibility of direct (co)activation by both factors. CONCLUSIONS: Four new candidates for genes directly co-regulated by NF-κB and p53 were revealed.</p>',
'date' => '2018-11-12',
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View::render() - CORE/Cake/View/View.php, line 473
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'description' => '<p><span>Alternative names: <strong>TP53</strong>, <strong>P53</strong>, <strong>TRP53</strong>, <strong>LSF1</strong></span></p>
<p><span>Polyclonal antibody raised in rabbit against human p53 (tumor protein p53), using a KLH-conjugated synthetic peptide containing a sequence from the C-terminal part of the protein.</span></p>',
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<div class="small-6 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410083-chip.jpg" alt="p53 Antibody ChIP Grade" caption="false" width="400" height="304" /></p>
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<div class="small-6 columns">
<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP assays were performed using human U2OS cells, treated with camptothecin, the Diagenode antibody against p53 (Cat. No. C15410083) and optimized PCR primer sets for qPCR. ChIP was performed on sheared chromatin from 4 million cells. A titration of the antibody consisting of 1, 2, 5, and 10 µg per ChIP experiment was analysed. IgG (2 µg/IP) was used as negative IP control. qPCR was performed with primers for the p21 and GAS6 genes used as positive controls, and for GAPDH promoter and the Sat2 satellite repeat, used as negative controls. Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<div class="small-12 columns">
<p>A. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-A.jpg" alt="p53 Antibody ChIP-seq Grade" style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>B. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-B.jpg" alt="p53 Antibody for ChIP-seq" style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>C. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-C.jpg" alt="p53 Antibody for ChIP-seq assay " style="display: block; margin-left: auto; margin-right: auto;" /></p>
<p>D. <img src="https://www.diagenode.com/img/product/antibodies/C15410083_ChIPSeq-D.jpg" alt="p53 Antibody validated in ChIP-seq" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<div class="small-12 columns">
<p><small><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP was performed on sheared chromatin from 4 million U2OS cells using 1 µg of the Diagenode antibody against p53 (Cat. No. C15410083) as described above. The IP’d DNA was subsequently analysed on an Illumina HiSeq. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 51 bp tags were aligned to the human genome using the BWA algorithm. Figure 2 shows the peak distribution along the X-chromosome (fig 2A) and in 3 genomic regions of chromosome 6, 13 and 12, surrounding p21 (CDKN1A), GAS6 and MDM2, 3 known targets genes of p53 (fig 2B, C and D, respectively). </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410083_ELISA.jpg" alt="p53 Antibody ELISA validation " style="display: block; margin-left: auto; margin-right: auto;" /></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 Diagenode antibody directed against human p53 (Cat. No. C15410083), in antigen coated wells. By plotting the absorbance against the antibody dilution (Figure 3), the titer of the antibody was estimated to be 1:308,000. </small></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against p53</strong><br /> Nuclear extracts of HeLa cells (40 µg) were analysed by Western blot using the Diagenode antibody against p53 (Cat. No. C15410083) diluted 1:2,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP assays were performed using human U2OS cells, treated with camptothecin, the Diagenode antibody against p53 (Cat. No. C15410083) and optimized PCR primer sets for qPCR. ChIP was performed on sheared chromatin from 4 million cells. A titration of the antibody consisting of 1, 2, 5, and 10 µg per ChIP experiment was analysed. IgG (2 µg/IP) was used as negative IP control. qPCR was performed with primers for the p21 and GAS6 genes used as positive controls, and for GAPDH promoter and the Sat2 satellite repeat, used as negative controls. Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p><small><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP was performed on sheared chromatin from 4 million U2OS cells using 1 µg of the Diagenode antibody against p53 (Cat. No. C15410083) as described above. The IP’d DNA was subsequently analysed on an Illumina HiSeq. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 51 bp tags were aligned to the human genome using the BWA algorithm. Figure 2 shows the peak distribution along the X-chromosome (fig 2A) and in 3 genomic regions of chromosome 6, 13 and 12, surrounding p21 (CDKN1A), GAS6 and MDM2, 3 known targets genes of p53 (fig 2B, C and D, respectively). </small></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against p53</strong><br /> Nuclear extracts of HeLa cells (40 µg) were analysed by Western blot using the Diagenode antibody against p53 (Cat. No. C15410083) diluted 1:2,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP assays were performed using human U2OS cells, treated with camptothecin, the Diagenode antibody against p53 (Cat. No. C15410083) and optimized PCR primer sets for qPCR. ChIP was performed on sheared chromatin from 4 million cells. A titration of the antibody consisting of 1, 2, 5, and 10 µg per ChIP experiment was analysed. IgG (2 µg/IP) was used as negative IP control. qPCR was performed with primers for the p21 and GAS6 genes used as positive controls, and for GAPDH promoter and the Sat2 satellite repeat, used as negative controls. Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p><small><strong>Figure 2. ChIP-seq results obtained with the Diagenode antibody directed against p53</strong><br /> ChIP was performed on sheared chromatin from 4 million U2OS cells using 1 µg of the Diagenode antibody against p53 (Cat. No. C15410083) as described above. The IP’d DNA was subsequently analysed on an Illumina HiSeq. Library preparation, cluster generation and sequencing were performed according to the manufacturer’s instructions. The 51 bp tags were aligned to the human genome using the BWA algorithm. Figure 2 shows the peak distribution along the X-chromosome (fig 2A) and in 3 genomic regions of chromosome 6, 13 and 12, surrounding p21 (CDKN1A), GAS6 and MDM2, 3 known targets genes of p53 (fig 2B, C and D, respectively). </small></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against p53</strong><br /> Nuclear extracts of HeLa cells (40 µg) were analysed by Western blot using the Diagenode antibody against p53 (Cat. No. C15410083) diluted 1:2,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></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;"> 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>
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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>
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<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><span style="font-weight: 400;">Diagenode’s highly validated antibodies:</span></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>
<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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'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' => 'Chitosan nano-vehicles as biocompatible delivering tools for a newAg(I)curcuminoid-Gboxin analog complex in cancer and inflammation therapy',
'authors' => 'Elbehairi, Serag Eldin I. and Ismail, Lamia A. and Alfaifi, Mohammad Y. andElshaarawy, Reda F.M. and Hafez, Hani S.',
'description' => '<p>A novel anticancer and anti-inflammatory agent based on hybrid curcuminoid-Gboxin analog (FLLL49-GbA) and its macromolecular silver(I) complex (Ag(I)FLLL49-GbA) have successfully synthesized. In addition, chitosan nanoparticles (CNPs) were used to encapsulate this macromolecular complex, targeting enhancing its therapeutic effect and minimizing its side impacts. The encapsulated Ag(I) complex was significantly triggered apoptosis (P < 0.05) with much more rapidly release of Ag(I)FLLL49-GbA from the CNPs at pH 5.3 than at pH 7.4, which is beneficial for cancer-targeted drug delivery. Free complex showed promising ability in preventing glucose uptake and lactate production coupled with cellular ATP depletion in cancer cells. Additionally, there was significant decrease in the inflammatory cytokines in breast cancer (MCF-7) and lung cancer (A549) cells with values of P < 0.01 and P < 0.001 after 24 h incubation. Furthermore, the death-inducing proteins have been significantly up-regulated (P < 0.01 to P < 0.001) after 36 h incubation of cancer cells. Consequently, the novel curcuminoid macromolecule showed significant feasibility in triggering the high expression of apoptotic caspases caspase 3, caspase 8, P53, and Bax (P < 0.01 to P < 0.001) after 48 h of chemotherapy. Noteworthy, the cytotoxicity of Ag(I)FLLL49-GbA was significantly increased toward cancer cells (MCF-7 > A549), while, reduced toward normal cells (HeLa) after loading on chitosan Nano-vehicles.</p>',
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'authors' => 'Szołtysek K, Janus P, Zając G, Stokowy T, Walaszczyk A, Widłak W, Wojtaś B, Gielniewski B, Cockell S, Perkins ND, Kimmel M, Widlak P',
'description' => '<p>BACKGROUND: The cellular response to ionizing radiation involves activation of p53-dependent pathways and activation of the atypical NF-κB pathway. The crosstalk between these two transcriptional networks include (co)regulation of common gene targets. Here we looked for novel genes potentially (co)regulated by p53 and NF-κB using integrative genomics screening in human osteosarcoma U2-OS cells irradiated with a high dose (4 and 10 Gy). Radiation-induced expression in cells with silenced TP53 or RELA (coding the p65 NF-κB subunit) genes was analyzed by RNA-Seq while radiation-enhanced binding of p53 and RelA in putative regulatory regions was analyzed by ChIP-Seq, then selected candidates were validated by qPCR. RESULTS: We identified a subset of radiation-modulated genes whose expression was affected by silencing of both TP53 and RELA, and a subset of radiation-upregulated genes where radiation stimulated binding of both p53 and RelA. For three genes, namely IL4I1, SERPINE1, and CDKN1A, an antagonistic effect of the TP53 and RELA silencing was consistent with radiation-enhanced binding of both p53 and RelA. This suggested the possibility of a direct antagonistic (co)regulation by both factors: activation by NF-κB and inhibition by p53 of IL4I1, and activation by p53 and inhibition by NF-κB of CDKN1A and SERPINE1. On the other hand, radiation-enhanced binding of both p53 and RelA was observed in a putative regulatory region of the RRAD gene whose expression was downregulated both by TP53 and RELA silencing, which suggested a possibility of direct (co)activation by both factors. CONCLUSIONS: Four new candidates for genes directly co-regulated by NF-κB and p53 were revealed.</p>',
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'pmid' => 'http://www.pubmed.gov/30419821',
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'description' => '<p>TREM2 mutations evoke neurodegenerative disorders, and recently genetic variants of this gene were correlated to increased risk of Alzheimer's disease. The signaling cascade originating from the TREM2 membrane receptor includes its binding partner TYROBP, BLNK adapter protein, and SYK kinase, which can be activated by p53. Moreover, in silico identification of a putative p53 response element (RE) at the TREM2 promoter led us to hypothesize that TREM2 and other pathway elements may be regulated in p53-dependent manner. To stimulate p53 in synergistic fashion, we exposed A549 lung cancer cells to actinomycin D and nutlin-3a (A + N). In these cells, exposure to A + N triggered expression of TREM2, TYROBP, SYK and BLNK in p53-dependent manner. TREM2 was also activated by A + N in U-2 OS osteosarcoma and A375 melanoma cell lines. Interestingly, nutlin-3a, a specific activator of p53, acting alone stimulated TREM2 in U-2 OS cells. Using in vitro mutagenesis, chromatin immunoprecipitation, and luciferase reporter assays, we confirmed the presence of the p53 RE in TREM2 promoter. Furthermore, activation of TREM2 and TYROBP by p53 was strongly inhibited by CHIR-98014, a potent and specific inhibitor of glycogen synthase kinase-3 (GSK-3). We conclude that TREM2 is a direct p53-target gene, and that activation of TREM2 by A + N or nutlin-3a may be critically dependent on GSK-3 function.</p>',
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$chipseq_service = array(
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(int) 3 => (int) 2684,
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'label2' => '',
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'price_JPY' => '16450',
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'country' => 'ALL',
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'slug' => 'p53-polyclonal-antibody-classic-10-ug',
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'meta_keywords' => '',
'meta_description' => 'p53 (Tumor protein p53) Polyclonal Antibody validated in ChIP-seq, ChIP-qPCR, ELISA and WB. Batch-specific data available on the website. Alternative names: TP53, P53, TRP53, LSF1. Sample size available',
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'created' => '2017-10-18 17:05:32',
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'meta_description' => 'Diagenode offers a wide range of antibodies and technical support for ChIP-qPCR applications',
'meta_title' => 'ChIP Quantitative PCR Antibodies (ChIP-qPCR) | Diagenode',
'modified' => '2016-01-20 11:30:24',
'created' => '2015-10-20 11:45:36',
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)
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'id' => '43',
'position' => '10',
'parent_id' => '40',
'name' => 'ChIP-qPCR (ab)',
'description' => '',
'in_footer' => false,
'in_menu' => false,
'online' => true,
'tabular' => true,
'slug' => 'chip-qpcr-antibodies',
'meta_keywords' => 'Chromatin Immunoprecipitation Sequencing,ChIP-Seq,ChIP-seq grade antibodies,DNA purification,qPCR,Shearing of chromatin',
'meta_description' => 'Diagenode offers a wide range of antibodies and technical support for ChIP-qPCR applications',
'meta_title' => 'ChIP Quantitative PCR Antibodies (ChIP-qPCR) | Diagenode',
'modified' => '2016-01-20 11:30:24',
'created' => '2015-10-20 11:45:36',
'locale' => 'zho'
)
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$document = 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>',
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'type' => 'Brochure',
'url' => 'files/brochures/Epigenetic_Antibodies_Brochure.pdf',
'slug' => 'epigenetic-antibodies-brochure',
'meta_keywords' => '',
'meta_description' => '',
'modified' => '2016-06-15 11:24:06',
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'document_id' => '38'
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'name' => 'p53 Antibody SDS BE nl',
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'url' => 'files/SDS/p53/SDS-C15410083-p53_Antibody-BE-nl-GHS_1_0.pdf',
'countries' => 'BE',
'modified' => '2023-01-26 10:33:44',
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'name' => 'The Alzheimer's disease-associated TREM2 gene is regulated by p53 tumor suppressor protein.',
'authors' => 'Zajkowicz A, Gdowicz-Kłosok A, Krześniak M, Janus P, Łasut B, Rusin M',
'description' => '<p>TREM2 mutations evoke neurodegenerative disorders, and recently genetic variants of this gene were correlated to increased risk of Alzheimer's disease. The signaling cascade originating from the TREM2 membrane receptor includes its binding partner TYROBP, BLNK adapter protein, and SYK kinase, which can be activated by p53. Moreover, in silico identification of a putative p53 response element (RE) at the TREM2 promoter led us to hypothesize that TREM2 and other pathway elements may be regulated in p53-dependent manner. To stimulate p53 in synergistic fashion, we exposed A549 lung cancer cells to actinomycin D and nutlin-3a (A + N). In these cells, exposure to A + N triggered expression of TREM2, TYROBP, SYK and BLNK in p53-dependent manner. TREM2 was also activated by A + N in U-2 OS osteosarcoma and A375 melanoma cell lines. Interestingly, nutlin-3a, a specific activator of p53, acting alone stimulated TREM2 in U-2 OS cells. Using in vitro mutagenesis, chromatin immunoprecipitation, and luciferase reporter assays, we confirmed the presence of the p53 RE in TREM2 promoter. Furthermore, activation of TREM2 and TYROBP by p53 was strongly inhibited by CHIR-98014, a potent and specific inhibitor of glycogen synthase kinase-3 (GSK-3). We conclude that TREM2 is a direct p53-target gene, and that activation of TREM2 by A + N or nutlin-3a may be critically dependent on GSK-3 function.</p>',
'date' => '2018-08-10',
'pmid' => 'http://www.pubmed.gov/29842899',
'doi' => '10.1016/j.neulet.2018.05.037',
'modified' => '2019-04-17 15:23:53',
'created' => '2019-04-16 12:25:30',
'ProductsPublication' => array(
'id' => '3504',
'product_id' => '2240',
'publication_id' => '3588'
)
)
$externalLink = ' <a href="http://www.pubmed.gov/29842899" 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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