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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against SMYD3</strong><br /> ChIP was performed on HepG2 cells with 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253). IgG (5 µg/IP) was used as negative IP control. QPCR was performed with primers for the 5’ flanking region of Nkx2.8. Figure 1 shows the fold enrichment over the IgG negative control.</small></p>
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<p><small><strong>Figure 2. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts from 293T cells (30 µg) transfected with a SMYD3 expression vector (lane 2, partial fragment) and untransfected control cells (lane 1) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1,000. 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 3. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts (30 µg) from 293T, A431, HeLa and HepG2 cells (lane 1, 2, 3 and 4, respectively) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1.000. 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 4. Immunoprecipitation using the Diagenode antibody directed against SMYD3</strong><br /> Immunoprecipitation was performed on whole cell extracts from 293T cells using 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253) (lane 2) or with an equal amount of rabbit IgG (lane 1). The immunoprecipitated SMYD3 protein was detected by western blot with the SMYD3 antibody diluted 1:1,000.</small></p>
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<p><small><strong>Figure 5. Immunofluorescence using the Diagenode antibody directed against SMYD33</strong><br /> HCT116 cells were stained with the Diagenode antibody against SMYD3 (Cat. No. C15410253). Cells were fixed with ice-cold methanol for 5 min and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labeled with the SMYD3 antibody (left) diluted 1:500 in blocking solution. The right panel shows costaining with Hoechst 33342.</small></p>
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<p><small><strong>Figure 2. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts from 293T cells (30 µg) transfected with a SMYD3 expression vector (lane 2, partial fragment) and untransfected control cells (lane 1) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1,000. 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 3. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts (30 µg) from 293T, A431, HeLa and HepG2 cells (lane 1, 2, 3 and 4, respectively) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1.000. 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 4. Immunoprecipitation using the Diagenode antibody directed against SMYD3</strong><br /> Immunoprecipitation was performed on whole cell extracts from 293T cells using 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253) (lane 2) or with an equal amount of rabbit IgG (lane 1). The immunoprecipitated SMYD3 protein was detected by western blot with the SMYD3 antibody diluted 1:1,000.</small></p>
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<p><small><strong>Figure 5. Immunofluorescence using the Diagenode antibody directed against SMYD33</strong><br /> HCT116 cells were stained with the Diagenode antibody against SMYD3 (Cat. No. C15410253). Cells were fixed with ice-cold methanol for 5 min and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labeled with the SMYD3 antibody (left) diluted 1:500 in blocking solution. The right panel shows costaining with Hoechst 33342.</small></p>
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<p><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
<p><sup>HeLa cells transfected with a Cas9 expression vector (left) or untransfected cells (right) were fixed in methanol at -20°C, permeabilized with acetone at -20°C and blocked with PBS containing 2% BSA. The cells were stained with the Cas9 C-terminal antibody (Cat. No. C15200229) diluted 1:400, followed by incubation with an anti-mouse secondary antibody coupled to AF488. The bottom images show counter-staining of the nuclei with Hoechst 33342.</sup></p>
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<p><br />Chromatin immunoprecipitation (<b>ChIP</b>) is a technique to study the associations of proteins with the specific genomic regions in intact cells. One of the most important steps of this protocol is the immunoprecipitation of targeted protein using the antibody specifically recognizing it. The quality of antibodies used in ChIP is essential for the success of the experiment. Diagenode offers extensively validated ChIP-grade antibodies, confirmed for their specificity, and high level of performance in ChIP. Each batch is validated, and batch-specific data are available on the website.</p>
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<p><strong>ChIP results</strong> obtained with the antibody directed against H3K4me3 (Cat. No. <a href="../p/h3k4me3-polyclonal-antibody-premium-50-ug-50-ul">C15410003</a>). </p>
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<p>Polyclonal antibody raised in rabbit against <strong>SMYD3 (SET and MYND domain containing 3)</strong>, using a recombinant protein.</p>',
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against SMYD3</strong><br /> ChIP was performed on HepG2 cells with 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253). IgG (5 µg/IP) was used as negative IP control. QPCR was performed with primers for the 5’ flanking region of Nkx2.8. Figure 1 shows the fold enrichment over the IgG negative control.</small></p>
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<p><small><strong>Figure 2. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts from 293T cells (30 µg) transfected with a SMYD3 expression vector (lane 2, partial fragment) and untransfected control cells (lane 1) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1,000. 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 3. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts (30 µg) from 293T, A431, HeLa and HepG2 cells (lane 1, 2, 3 and 4, respectively) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1.000. 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 4. Immunoprecipitation using the Diagenode antibody directed against SMYD3</strong><br /> Immunoprecipitation was performed on whole cell extracts from 293T cells using 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253) (lane 2) or with an equal amount of rabbit IgG (lane 1). The immunoprecipitated SMYD3 protein was detected by western blot with the SMYD3 antibody diluted 1:1,000.</small></p>
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<p><small><strong>Figure 5. Immunofluorescence using the Diagenode antibody directed against SMYD33</strong><br /> HCT116 cells were stained with the Diagenode antibody against SMYD3 (Cat. No. C15410253). Cells were fixed with ice-cold methanol for 5 min and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labeled with the SMYD3 antibody (left) diluted 1:500 in blocking solution. The right panel shows costaining with Hoechst 33342.</small></p>
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against SMYD3</strong><br /> ChIP was performed on HepG2 cells with 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253). IgG (5 µg/IP) was used as negative IP control. QPCR was performed with primers for the 5’ flanking region of Nkx2.8. Figure 1 shows the fold enrichment over the IgG negative control.</small></p>
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<p><small><strong>Figure 2. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts from 293T cells (30 µg) transfected with a SMYD3 expression vector (lane 2, partial fragment) and untransfected control cells (lane 1) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1,000. 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 3. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts (30 µg) from 293T, A431, HeLa and HepG2 cells (lane 1, 2, 3 and 4, respectively) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1.000. 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 4. Immunoprecipitation using the Diagenode antibody directed against SMYD3</strong><br /> Immunoprecipitation was performed on whole cell extracts from 293T cells using 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253) (lane 2) or with an equal amount of rabbit IgG (lane 1). The immunoprecipitated SMYD3 protein was detected by western blot with the SMYD3 antibody diluted 1:1,000.</small></p>
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<p><small><strong>Figure 5. Immunofluorescence using the Diagenode antibody directed against SMYD33</strong><br /> HCT116 cells were stained with the Diagenode antibody against SMYD3 (Cat. No. C15410253). Cells were fixed with ice-cold methanol for 5 min and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labeled with the SMYD3 antibody (left) diluted 1:500 in blocking solution. The right panel shows costaining with Hoechst 33342.</small></p>
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'description' => '<p>In obesity, adipose tissue undergoes a remodeling process characterized by increased adipocyte size (hypertrophia) and number (hyperplasia). The individual ability to tip the balance toward the hyperplastic growth, with recruitment of new fat cells through adipogenesis, seems to be critical for a healthy adipose tissue expansion, as opposed to the development of inflammation and detrimental metabolic consequences. However, the molecular mechanisms underlying this fine-tuned regulation are far from being understood. Methods We analyzed by mass spectrometry-based proteomics visceral white adipose tissue (vWAT) samples collected from C57BL6 mice fed with a HFD for 8 weeks. A subset of these mice, called low inflammation (Low-INFL), showed a low susceptibility to the onset of adipose tissue inflammation, as opposed to those developing the expected inflammatory response (Hi-INFL). We identified the discriminants between Low-INFL and Hi-INFL vWAT samples and explored their function in Adipose Derived human Mesenchymal Stem Cells (AD-hMSCs) differentiated to adipocytes. Results We quantified 6051 proteins. Among the candidates that most differentiate Low-INFL from Hi-INFL vWAT, we found proteins involved in adipocyte function, including adiponectin and hormone sensitive lipase, suggesting that adipocyte differentiation is enhanced in Low-INFL, as compared to Hi-INFL. The chromatin modifier SET and MYND Domain Containing 3 (SMYD3), whose function in adipose tissue was so far unknown, was another top-scored hit. SMYD3 expression was significantly higher in Low-INFL vWAT, as confirmed by western blot analysis. In vitro, we found that SMYD3 mRNA and protein levels decrease rapidly along the differentiation process of AD-hMSCs. Moreover, SMYD3 knock-down at the beginning of adipocyte differentiation resulted in reduced cell proliferation and, at longer term, reduced lipid accumulation in adipocytes. Conclusions Our study describes an important role for SMYD3 as a newly discovered regulator of adipocyte proliferation during the early steps of adipogenesis.</p>',
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410253-CHIP.jpg" alt="SMYD3 Antibody ChIP Grade" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against SMYD3</strong><br /> ChIP was performed on HepG2 cells with 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253). IgG (5 µg/IP) was used as negative IP control. QPCR was performed with primers for the 5’ flanking region of Nkx2.8. Figure 1 shows the fold enrichment over the IgG negative control.</small></p>
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<p><small><strong>Figure 2. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts from 293T cells (30 µg) transfected with a SMYD3 expression vector (lane 2, partial fragment) and untransfected control cells (lane 1) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1,000. 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 3. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts (30 µg) from 293T, A431, HeLa and HepG2 cells (lane 1, 2, 3 and 4, respectively) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1.000. 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 4. Immunoprecipitation using the Diagenode antibody directed against SMYD3</strong><br /> Immunoprecipitation was performed on whole cell extracts from 293T cells using 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253) (lane 2) or with an equal amount of rabbit IgG (lane 1). The immunoprecipitated SMYD3 protein was detected by western blot with the SMYD3 antibody diluted 1:1,000.</small></p>
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<p><small><strong>Figure 5. Immunofluorescence using the Diagenode antibody directed against SMYD33</strong><br /> HCT116 cells were stained with the Diagenode antibody against SMYD3 (Cat. No. C15410253). Cells were fixed with ice-cold methanol for 5 min and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labeled with the SMYD3 antibody (left) diluted 1:500 in blocking solution. The right panel shows costaining with Hoechst 33342.</small></p>
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<p>Polyclonal antibody raised in rabbit against <strong>SMYD3 (SET and MYND domain containing 3)</strong>, using a recombinant protein.</p>',
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410253-CHIP.jpg" alt="SMYD3 Antibody ChIP Grade" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against SMYD3</strong><br /> ChIP was performed on HepG2 cells with 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253). IgG (5 µg/IP) was used as negative IP control. QPCR was performed with primers for the 5’ flanking region of Nkx2.8. Figure 1 shows the fold enrichment over the IgG negative control.</small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410253-WB.jpg" alt="SMYD3 Antibody validated in Western Blot" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 2. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts from 293T cells (30 µg) transfected with a SMYD3 expression vector (lane 2, partial fragment) and untransfected control cells (lane 1) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1,000. 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><img src="https://www.diagenode.com/img/product/antibodies/c15410253-wb-2.jpg" alt="SMYD3 Antibody validated in Western Blot" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 3. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts (30 µg) from 293T, A431, HeLa and HepG2 cells (lane 1, 2, 3 and 4, respectively) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1.000. 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><img src="https://www.diagenode.com/img/product/antibodies/C15410253-IP.jpg" alt="SMYD3 Antibody validated in Immunoprecipitation" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 4. Immunoprecipitation using the Diagenode antibody directed against SMYD3</strong><br /> Immunoprecipitation was performed on whole cell extracts from 293T cells using 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253) (lane 2) or with an equal amount of rabbit IgG (lane 1). The immunoprecipitated SMYD3 protein was detected by western blot with the SMYD3 antibody diluted 1:1,000.</small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410253-IF.jpg" alt="SMYD3 Antibody validated in Immunofluorescence" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 5. Immunofluorescence using the Diagenode antibody directed against SMYD33</strong><br /> HCT116 cells were stained with the Diagenode antibody against SMYD3 (Cat. No. C15410253). Cells were fixed with ice-cold methanol for 5 min and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labeled with the SMYD3 antibody (left) diluted 1:500 in blocking solution. The right panel shows costaining with Hoechst 33342.</small></p>
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<p><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
<p><sup>HeLa cells transfected with a Cas9 expression vector (left) or untransfected cells (right) were fixed in methanol at -20°C, permeabilized with acetone at -20°C and blocked with PBS containing 2% BSA. The cells were stained with the Cas9 C-terminal antibody (Cat. No. C15200229) diluted 1:400, followed by incubation with an anti-mouse secondary antibody coupled to AF488. The bottom images show counter-staining of the nuclei with Hoechst 33342.</sup></p>
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<p>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><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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'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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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against SMYD3</strong><br /> ChIP was performed on HepG2 cells with 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253). IgG (5 µg/IP) was used as negative IP control. QPCR was performed with primers for the 5’ flanking region of Nkx2.8. Figure 1 shows the fold enrichment over the IgG negative control.</small></p>
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<p><small><strong>Figure 2. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts from 293T cells (30 µg) transfected with a SMYD3 expression vector (lane 2, partial fragment) and untransfected control cells (lane 1) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1,000. 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 3. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts (30 µg) from 293T, A431, HeLa and HepG2 cells (lane 1, 2, 3 and 4, respectively) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1.000. 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 4. Immunoprecipitation using the Diagenode antibody directed against SMYD3</strong><br /> Immunoprecipitation was performed on whole cell extracts from 293T cells using 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253) (lane 2) or with an equal amount of rabbit IgG (lane 1). The immunoprecipitated SMYD3 protein was detected by western blot with the SMYD3 antibody diluted 1:1,000.</small></p>
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<p><small><strong>Figure 5. Immunofluorescence using the Diagenode antibody directed against SMYD33</strong><br /> HCT116 cells were stained with the Diagenode antibody against SMYD3 (Cat. No. C15410253). Cells were fixed with ice-cold methanol for 5 min and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labeled with the SMYD3 antibody (left) diluted 1:500 in blocking solution. The right panel shows costaining with Hoechst 33342.</small></p>
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against SMYD3</strong><br /> ChIP was performed on HepG2 cells with 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253). IgG (5 µg/IP) was used as negative IP control. QPCR was performed with primers for the 5’ flanking region of Nkx2.8. Figure 1 shows the fold enrichment over the IgG negative control.</small></p>
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<p><small><strong>Figure 3. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts (30 µg) from 293T, A431, HeLa and HepG2 cells (lane 1, 2, 3 and 4, respectively) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1.000. 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 4. Immunoprecipitation using the Diagenode antibody directed against SMYD3</strong><br /> Immunoprecipitation was performed on whole cell extracts from 293T cells using 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253) (lane 2) or with an equal amount of rabbit IgG (lane 1). The immunoprecipitated SMYD3 protein was detected by western blot with the SMYD3 antibody diluted 1:1,000.</small></p>
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<p><small><strong>Figure 5. Immunofluorescence using the Diagenode antibody directed against SMYD33</strong><br /> HCT116 cells were stained with the Diagenode antibody against SMYD3 (Cat. No. C15410253). Cells were fixed with ice-cold methanol for 5 min and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labeled with the SMYD3 antibody (left) diluted 1:500 in blocking solution. The right panel shows costaining with Hoechst 33342.</small></p>
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'description' => '<p>In obesity, adipose tissue undergoes a remodeling process characterized by increased adipocyte size (hypertrophia) and number (hyperplasia). The individual ability to tip the balance toward the hyperplastic growth, with recruitment of new fat cells through adipogenesis, seems to be critical for a healthy adipose tissue expansion, as opposed to the development of inflammation and detrimental metabolic consequences. However, the molecular mechanisms underlying this fine-tuned regulation are far from being understood. Methods We analyzed by mass spectrometry-based proteomics visceral white adipose tissue (vWAT) samples collected from C57BL6 mice fed with a HFD for 8 weeks. A subset of these mice, called low inflammation (Low-INFL), showed a low susceptibility to the onset of adipose tissue inflammation, as opposed to those developing the expected inflammatory response (Hi-INFL). We identified the discriminants between Low-INFL and Hi-INFL vWAT samples and explored their function in Adipose Derived human Mesenchymal Stem Cells (AD-hMSCs) differentiated to adipocytes. Results We quantified 6051 proteins. Among the candidates that most differentiate Low-INFL from Hi-INFL vWAT, we found proteins involved in adipocyte function, including adiponectin and hormone sensitive lipase, suggesting that adipocyte differentiation is enhanced in Low-INFL, as compared to Hi-INFL. The chromatin modifier SET and MYND Domain Containing 3 (SMYD3), whose function in adipose tissue was so far unknown, was another top-scored hit. SMYD3 expression was significantly higher in Low-INFL vWAT, as confirmed by western blot analysis. In vitro, we found that SMYD3 mRNA and protein levels decrease rapidly along the differentiation process of AD-hMSCs. Moreover, SMYD3 knock-down at the beginning of adipocyte differentiation resulted in reduced cell proliferation and, at longer term, reduced lipid accumulation in adipocytes. Conclusions Our study describes an important role for SMYD3 as a newly discovered regulator of adipocyte proliferation during the early steps of adipogenesis.</p>',
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against SMYD3</strong><br /> ChIP was performed on HepG2 cells with 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253). IgG (5 µg/IP) was used as negative IP control. QPCR was performed with primers for the 5’ flanking region of Nkx2.8. Figure 1 shows the fold enrichment over the IgG negative control.</small></p>
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<p><small><strong>Figure 2. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts from 293T cells (30 µg) transfected with a SMYD3 expression vector (lane 2, partial fragment) and untransfected control cells (lane 1) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1,000. 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 3. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts (30 µg) from 293T, A431, HeLa and HepG2 cells (lane 1, 2, 3 and 4, respectively) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1.000. 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 4. Immunoprecipitation using the Diagenode antibody directed against SMYD3</strong><br /> Immunoprecipitation was performed on whole cell extracts from 293T cells using 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253) (lane 2) or with an equal amount of rabbit IgG (lane 1). The immunoprecipitated SMYD3 protein was detected by western blot with the SMYD3 antibody diluted 1:1,000.</small></p>
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<p><small><strong>Figure 5. Immunofluorescence using the Diagenode antibody directed against SMYD33</strong><br /> HCT116 cells were stained with the Diagenode antibody against SMYD3 (Cat. No. C15410253). Cells were fixed with ice-cold methanol for 5 min and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labeled with the SMYD3 antibody (left) diluted 1:500 in blocking solution. The right panel shows costaining with Hoechst 33342.</small></p>
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<p><small><strong>Figure 2. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts from 293T cells (30 µg) transfected with a SMYD3 expression vector (lane 2, partial fragment) and untransfected control cells (lane 1) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1,000. 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 3. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts (30 µg) from 293T, A431, HeLa and HepG2 cells (lane 1, 2, 3 and 4, respectively) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1.000. 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 4. Immunoprecipitation using the Diagenode antibody directed against SMYD3</strong><br /> Immunoprecipitation was performed on whole cell extracts from 293T cells using 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253) (lane 2) or with an equal amount of rabbit IgG (lane 1). The immunoprecipitated SMYD3 protein was detected by western blot with the SMYD3 antibody diluted 1:1,000.</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><br />Chromatin immunoprecipitation (<b>ChIP</b>) is a technique to study the associations of proteins with the specific genomic regions in intact cells. One of the most important steps of this protocol is the immunoprecipitation of targeted protein using the antibody specifically recognizing it. The quality of antibodies used in ChIP is essential for the success of the experiment. Diagenode offers extensively validated ChIP-grade antibodies, confirmed for their specificity, and high level of performance in ChIP. Each batch is validated, and batch-specific data are available on the website.</p>
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<p><strong>ChIP results</strong> obtained with the antibody directed against H3K4me3 (Cat. No. <a href="../p/h3k4me3-polyclonal-antibody-premium-50-ug-50-ul">C15410003</a>). </p>
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<p><small><strong>Figure 4. Immunoprecipitation using the Diagenode antibody directed against SMYD3</strong><br /> Immunoprecipitation was performed on whole cell extracts from 293T cells using 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253) (lane 2) or with an equal amount of rabbit IgG (lane 1). The immunoprecipitated SMYD3 protein was detected by western blot with the SMYD3 antibody diluted 1:1,000.</small></p>
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<p><small><strong>Figure 5. Immunofluorescence using the Diagenode antibody directed against SMYD33</strong><br /> HCT116 cells were stained with the Diagenode antibody against SMYD3 (Cat. No. C15410253). Cells were fixed with ice-cold methanol for 5 min and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labeled with the SMYD3 antibody (left) diluted 1:500 in blocking solution. The right panel shows costaining with Hoechst 33342.</small></p>
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'description' => '<p>In obesity, adipose tissue undergoes a remodeling process characterized by increased adipocyte size (hypertrophia) and number (hyperplasia). The individual ability to tip the balance toward the hyperplastic growth, with recruitment of new fat cells through adipogenesis, seems to be critical for a healthy adipose tissue expansion, as opposed to the development of inflammation and detrimental metabolic consequences. However, the molecular mechanisms underlying this fine-tuned regulation are far from being understood. Methods We analyzed by mass spectrometry-based proteomics visceral white adipose tissue (vWAT) samples collected from C57BL6 mice fed with a HFD for 8 weeks. A subset of these mice, called low inflammation (Low-INFL), showed a low susceptibility to the onset of adipose tissue inflammation, as opposed to those developing the expected inflammatory response (Hi-INFL). We identified the discriminants between Low-INFL and Hi-INFL vWAT samples and explored their function in Adipose Derived human Mesenchymal Stem Cells (AD-hMSCs) differentiated to adipocytes. Results We quantified 6051 proteins. Among the candidates that most differentiate Low-INFL from Hi-INFL vWAT, we found proteins involved in adipocyte function, including adiponectin and hormone sensitive lipase, suggesting that adipocyte differentiation is enhanced in Low-INFL, as compared to Hi-INFL. The chromatin modifier SET and MYND Domain Containing 3 (SMYD3), whose function in adipose tissue was so far unknown, was another top-scored hit. SMYD3 expression was significantly higher in Low-INFL vWAT, as confirmed by western blot analysis. In vitro, we found that SMYD3 mRNA and protein levels decrease rapidly along the differentiation process of AD-hMSCs. Moreover, SMYD3 knock-down at the beginning of adipocyte differentiation resulted in reduced cell proliferation and, at longer term, reduced lipid accumulation in adipocytes. Conclusions Our study describes an important role for SMYD3 as a newly discovered regulator of adipocyte proliferation during the early steps of adipogenesis.</p>',
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against SMYD3</strong><br /> ChIP was performed on HepG2 cells with 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253). IgG (5 µg/IP) was used as negative IP control. QPCR was performed with primers for the 5’ flanking region of Nkx2.8. Figure 1 shows the fold enrichment over the IgG negative control.</small></p>
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<p><small><strong>Figure 3. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts (30 µg) from 293T, A431, HeLa and HepG2 cells (lane 1, 2, 3 and 4, respectively) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1.000. 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 4. Immunoprecipitation using the Diagenode antibody directed against SMYD3</strong><br /> Immunoprecipitation was performed on whole cell extracts from 293T cells using 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253) (lane 2) or with an equal amount of rabbit IgG (lane 1). The immunoprecipitated SMYD3 protein was detected by western blot with the SMYD3 antibody diluted 1:1,000.</small></p>
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<p><small><strong>Figure 5. Immunofluorescence using the Diagenode antibody directed against SMYD33</strong><br /> HCT116 cells were stained with the Diagenode antibody against SMYD3 (Cat. No. C15410253). Cells were fixed with ice-cold methanol for 5 min and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labeled with the SMYD3 antibody (left) diluted 1:500 in blocking solution. The right panel shows costaining with Hoechst 33342.</small></p>
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<p><small><strong>Figure 2. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts from 293T cells (30 µg) transfected with a SMYD3 expression vector (lane 2, partial fragment) and untransfected control cells (lane 1) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1,000. 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 3. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts (30 µg) from 293T, A431, HeLa and HepG2 cells (lane 1, 2, 3 and 4, respectively) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1.000. 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 4. Immunoprecipitation using the Diagenode antibody directed against SMYD3</strong><br /> Immunoprecipitation was performed on whole cell extracts from 293T cells using 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253) (lane 2) or with an equal amount of rabbit IgG (lane 1). The immunoprecipitated SMYD3 protein was detected by western blot with the SMYD3 antibody diluted 1:1,000.</small></p>
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<p><small><strong>Figure 5. Immunofluorescence using the Diagenode antibody directed against SMYD33</strong><br /> HCT116 cells were stained with the Diagenode antibody against SMYD3 (Cat. No. C15410253). Cells were fixed with ice-cold methanol for 5 min and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labeled with the SMYD3 antibody (left) diluted 1:500 in blocking solution. The right panel shows costaining with Hoechst 33342.</small></p>
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<p><sup><strong>Immunofluorescence using the Diagenode monoclonal antibody directed against CRISPR/Cas9</strong></sup></p>
<p><sup>HeLa cells transfected with a Cas9 expression vector (left) or untransfected cells (right) were fixed in methanol at -20°C, permeabilized with acetone at -20°C and blocked with PBS containing 2% BSA. The cells were stained with the Cas9 C-terminal antibody (Cat. No. C15200229) diluted 1:400, followed by incubation with an anti-mouse secondary antibody coupled to AF488. The bottom images show counter-staining of the nuclei with Hoechst 33342.</sup></p>
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<p>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><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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<div class="small-2 columns"><img src="https://www.diagenode.com/emailing/images/epi-success-guaranteed-icon.png" alt="Epigenetic success guaranteed" /></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>
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'description' => '<p>In obesity, adipose tissue undergoes a remodeling process characterized by increased adipocyte size (hypertrophia) and number (hyperplasia). The individual ability to tip the balance toward the hyperplastic growth, with recruitment of new fat cells through adipogenesis, seems to be critical for a healthy adipose tissue expansion, as opposed to the development of inflammation and detrimental metabolic consequences. However, the molecular mechanisms underlying this fine-tuned regulation are far from being understood. Methods We analyzed by mass spectrometry-based proteomics visceral white adipose tissue (vWAT) samples collected from C57BL6 mice fed with a HFD for 8 weeks. A subset of these mice, called low inflammation (Low-INFL), showed a low susceptibility to the onset of adipose tissue inflammation, as opposed to those developing the expected inflammatory response (Hi-INFL). We identified the discriminants between Low-INFL and Hi-INFL vWAT samples and explored their function in Adipose Derived human Mesenchymal Stem Cells (AD-hMSCs) differentiated to adipocytes. Results We quantified 6051 proteins. Among the candidates that most differentiate Low-INFL from Hi-INFL vWAT, we found proteins involved in adipocyte function, including adiponectin and hormone sensitive lipase, suggesting that adipocyte differentiation is enhanced in Low-INFL, as compared to Hi-INFL. The chromatin modifier SET and MYND Domain Containing 3 (SMYD3), whose function in adipose tissue was so far unknown, was another top-scored hit. SMYD3 expression was significantly higher in Low-INFL vWAT, as confirmed by western blot analysis. In vitro, we found that SMYD3 mRNA and protein levels decrease rapidly along the differentiation process of AD-hMSCs. Moreover, SMYD3 knock-down at the beginning of adipocyte differentiation resulted in reduced cell proliferation and, at longer term, reduced lipid accumulation in adipocytes. Conclusions Our study describes an important role for SMYD3 as a newly discovered regulator of adipocyte proliferation during the early steps of adipogenesis.</p>',
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'name' => 'SMYD3 Antibody',
'description' => '<p><strong>Other names:</strong> ZMYND1, ZNFN3A1, KMT3E, BA74P14.1</p>
<p>Polyclonal antibody raised in rabbit against <strong>SMYD3 (SET and MYND domain containing 3)</strong>, using a recombinant protein.</p>',
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<div class="small-5 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410253-CHIP.jpg" alt="SMYD3 Antibody ChIP Grade" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against SMYD3</strong><br /> ChIP was performed on HepG2 cells with 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253). IgG (5 µg/IP) was used as negative IP control. QPCR was performed with primers for the 5’ flanking region of Nkx2.8. Figure 1 shows the fold enrichment over the IgG negative control.</small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410253-WB.jpg" alt="SMYD3 Antibody validated in Western Blot" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 2. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts from 293T cells (30 µg) transfected with a SMYD3 expression vector (lane 2, partial fragment) and untransfected control cells (lane 1) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1,000. 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><img src="https://www.diagenode.com/img/product/antibodies/c15410253-wb-2.jpg" alt="SMYD3 Antibody validated in Western Blot" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 3. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts (30 µg) from 293T, A431, HeLa and HepG2 cells (lane 1, 2, 3 and 4, respectively) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1.000. 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><img src="https://www.diagenode.com/img/product/antibodies/C15410253-IP.jpg" alt="SMYD3 Antibody validated in Immunoprecipitation" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 4. Immunoprecipitation using the Diagenode antibody directed against SMYD3</strong><br /> Immunoprecipitation was performed on whole cell extracts from 293T cells using 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253) (lane 2) or with an equal amount of rabbit IgG (lane 1). The immunoprecipitated SMYD3 protein was detected by western blot with the SMYD3 antibody diluted 1:1,000.</small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410253-IF.jpg" alt="SMYD3 Antibody validated in Immunofluorescence" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<div class="small-7 columns">
<p><small><strong>Figure 5. Immunofluorescence using the Diagenode antibody directed against SMYD33</strong><br /> HCT116 cells were stained with the Diagenode antibody against SMYD3 (Cat. No. C15410253). Cells were fixed with ice-cold methanol for 5 min and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labeled with the SMYD3 antibody (left) diluted 1:500 in blocking solution. The right panel shows costaining with Hoechst 33342.</small></p>
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'description' => '<p><strong>Other names:</strong> ZMYND1, ZNFN3A1, KMT3E, BA74P14.1</p>
<p>Polyclonal antibody raised in rabbit against <strong>SMYD3 (SET and MYND domain containing 3)</strong>, using a recombinant protein.</p>',
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<div class="small-5 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410253-CHIP.jpg" alt="SMYD3 Antibody ChIP Grade" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 1. ChIP results obtained with the Diagenode antibody directed against SMYD3</strong><br /> ChIP was performed on HepG2 cells with 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253). IgG (5 µg/IP) was used as negative IP control. QPCR was performed with primers for the 5’ flanking region of Nkx2.8. Figure 1 shows the fold enrichment over the IgG negative control.</small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410253-WB.jpg" alt="SMYD3 Antibody validated in Western Blot" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 2. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts from 293T cells (30 µg) transfected with a SMYD3 expression vector (lane 2, partial fragment) and untransfected control cells (lane 1) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1,000. 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 3. Western blot analysis using the Diagenode antibody directed against SMYD3</strong><br /> Whole cell extracts (30 µg) from 293T, A431, HeLa and HepG2 cells (lane 1, 2, 3 and 4, respectively) were analysed by western blot using the Diagenode antibody against SMYD3 (Cat. No. C15410253) diluted 1:1.000. 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><img src="https://www.diagenode.com/img/product/antibodies/C15410253-IP.jpg" alt="SMYD3 Antibody validated in Immunoprecipitation" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 4. Immunoprecipitation using the Diagenode antibody directed against SMYD3</strong><br /> Immunoprecipitation was performed on whole cell extracts from 293T cells using 5 µg of the Diagenode antibody against SMYD3 (Cat. No. C15410253) (lane 2) or with an equal amount of rabbit IgG (lane 1). The immunoprecipitated SMYD3 protein was detected by western blot with the SMYD3 antibody diluted 1:1,000.</small></p>
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<div class="small-5 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410253-IF.jpg" alt="SMYD3 Antibody validated in Immunofluorescence" style="display: block; margin-left: auto; margin-right: auto;" /></p>
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<p><small><strong>Figure 5. Immunofluorescence using the Diagenode antibody directed against SMYD33</strong><br /> HCT116 cells were stained with the Diagenode antibody against SMYD3 (Cat. No. C15410253). Cells were fixed with ice-cold methanol for 5 min and blocked with PBS/TX-100 containing 5% normal goat serum and 1% BSA. The cells were immunofluorescently labeled with the SMYD3 antibody (left) diluted 1:500 in blocking solution. The right panel shows costaining with Hoechst 33342.</small></p>
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'name' => 'SMYD3: a new regulator of the early steps of adipocyte differentiation',
'authors' => 'Gilardi F. et al.',
'description' => '<p>In obesity, adipose tissue undergoes a remodeling process characterized by increased adipocyte size (hypertrophia) and number (hyperplasia). The individual ability to tip the balance toward the hyperplastic growth, with recruitment of new fat cells through adipogenesis, seems to be critical for a healthy adipose tissue expansion, as opposed to the development of inflammation and detrimental metabolic consequences. However, the molecular mechanisms underlying this fine-tuned regulation are far from being understood. Methods We analyzed by mass spectrometry-based proteomics visceral white adipose tissue (vWAT) samples collected from C57BL6 mice fed with a HFD for 8 weeks. A subset of these mice, called low inflammation (Low-INFL), showed a low susceptibility to the onset of adipose tissue inflammation, as opposed to those developing the expected inflammatory response (Hi-INFL). We identified the discriminants between Low-INFL and Hi-INFL vWAT samples and explored their function in Adipose Derived human Mesenchymal Stem Cells (AD-hMSCs) differentiated to adipocytes. Results We quantified 6051 proteins. Among the candidates that most differentiate Low-INFL from Hi-INFL vWAT, we found proteins involved in adipocyte function, including adiponectin and hormone sensitive lipase, suggesting that adipocyte differentiation is enhanced in Low-INFL, as compared to Hi-INFL. The chromatin modifier SET and MYND Domain Containing 3 (SMYD3), whose function in adipose tissue was so far unknown, was another top-scored hit. SMYD3 expression was significantly higher in Low-INFL vWAT, as confirmed by western blot analysis. In vitro, we found that SMYD3 mRNA and protein levels decrease rapidly along the differentiation process of AD-hMSCs. Moreover, SMYD3 knock-down at the beginning of adipocyte differentiation resulted in reduced cell proliferation and, at longer term, reduced lipid accumulation in adipocytes. Conclusions Our study describes an important role for SMYD3 as a newly discovered regulator of adipocyte proliferation during the early steps of adipogenesis.</p>',
'date' => '2023-06-01',
'pmid' => 'https://doi.org/10.21203%2Frs.3.rs-3126142%2Fv1',
'doi' => '10.21203/rs.3.rs-3126142/v1',
'modified' => '2023-08-01 14:00:06',
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