anti prmt5 antibody (Proteintech)
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Structured Review
Proteintech
anti prmt5 antibody
Anti Prmt5 Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 41 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/prmt5+knockdown+cells/pmc12229037-109-31-62?v=Proteintech
Average 93 stars, based on 41 article reviews
Anti Prmt5 Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 41 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/prmt5+knockdown+cells/pmc12229037-109-31-62?v=Proteintech
Average 93 stars, based on 41 article reviews
anti prmt5 antibody - by Bioz Stars,
2026-08
93/100 stars
Images
1) Product Images from "Cardiac-specific overexpression of PRMT5 exacerbates pressure overload-induced hypertrophy and heart failure"
Article Title: Cardiac-specific overexpression of PRMT5 exacerbates pressure overload-induced hypertrophy and heart failure
Journal: Journal of Biomedical Science
doi: 10.1186/s12929-025-01162-6
Figure Legend Snippet: Cardiac-specific overexpression of PRMT5 accelerates pressure overload-induced cardiac systolic dysfunction. a A schematic diagram of the transgene to create mice with cardiac-specific Prmt5 overexpression (PRMT5-TG). b Images of WT and PRMT5-TG mice littermates at 10 weeks of age. Scale bar: 20 µm. c Cardiac PRMT5 overexpression confirmed using Western blotting. d Echocardiographic analysis images of PRMT5-TG mice performed 4 weeks after TAC surgery. e , f Fractional shorting ( e ) and ejection fraction ( f ) calculated from M-mode echocardiography. Values are presented as mean ± SD (n = 6–8 mice/group). Data are analyzed using two-way ANOVA, followed by Tukey’s multiple comparison test. A p < 0.05 is considered statistically significant. *** p < 0.001
Techniques Used: Over Expression, Western Blot, Comparison
Figure Legend Snippet: Cardiac overexpression of PRMT5 promotes pressure overload-induced cardiac hypertrophy. a Representative photos of the hearts extracted from the mice. b Histological analysis of the heart tissues. Scale bars: 2 mm. c Heart weight/body weight comparisons at 4 weeks after TAC surgery. Values are presented as mean ± SD (n = 6–8 mice/group) d Cardiac overexpression of PRMT5 promotes the increases in lung weight after TAC surgery. e , f Histological analysis results of PRMT5-TG mice at 4 weeks after TAC surgery. Representative images of HE-stained sections of the mice hearts. Cross-sectional myocardial cell diameter measurement ( e ). Representative images of MT-stained perivascular and interstitial fibrosis area of the LV myocardium of the mice. Perivascular and interstitial fibrotic area measurements ( f ). Values are presented as mean ± SD (n = 5 mice/group). Scale bars: 20 µm ( e ), 50 µm (Perivascular) and 100 µm (interstitial) ( f ). g Hypertrophic gene expression is increased by cardiac overexpression of PRMT5. Values are expressed as mean ± SD (n = 7–8 mice/group). Data are analyzed using two-way ANOVA, followed by Tukey’s multiple comparison test. A p < 0.05 is considered statistically significant. * p < 0.05, ** p < 0.01, *** p < 0.001
Techniques Used: Over Expression, Staining, Gene Expression, Comparison
Figure Legend Snippet: Pharmacological inhibition and knockdown of PRMT5 suppresses phenylephrine (PE)-induced hypertrophic responses in cultured cardiomyocytes. a Immunostaining images for α-actinin to determine the cell surface area of cardiomyocytes, quantified using ImageJ software. Scale bars: 20 µm. b Hypertrophic gene expression levels of Nppa and Nppb , quantified by qRT-PCR. c Primary cultured cardiomyocytes were transfected with siRNA (siControl or siPrmt5) and then stimulated with or without PE (30 µM). Prmt5 knockdown is confirmed by qRT-PCR and WB. The cell surface area was quantified using ImageJ software. Scale bars: 20 µm. d PE-induced Nppa and Nppb gene expression as quantified by qRT-PCR and Western blotting. Values are presented as mean ± SD (n = 4–5). Data are analyzed using one-way ANOVA, followed by Dunnett’s multiple comparison tests versus the PE-treated group. * p < 0.05, ** p < 0.01, *** p < 0.001
Techniques Used: Inhibition, Knockdown, Cell Culture, Immunostaining, Software, Gene Expression, Quantitative RT-PCR, Transfection, Western Blot, Comparison
Figure Legend Snippet: PRMT5 modifies histone methylation and acetylation in hearts and cultured cardiomyocytes. a Acid extracts from mouse hearts of WT and PRMT5 transgenic (PRMT5-TG) mice were applied to Western blotting analysis. Western blotting was performed using the indicated antibodies. b WT and PRMT5-TG mice were subjected to the TAC surgery. The samples prepared from these hearts were used for Western blotting. c Western blotting was performed using acid extracts from mouse hearts of sham and TAC mice treated with or without the PRMT5 inhibitor EPZ015666. Values are presented as mean ± SD (n = 4 mice). d Cultured cardiomyocytes were treated with EPZ015666 in the presence or absence of PE. Values are presented as mean ± SD (n = 3). e HAT activity in hearts was measured using a fluorescent-based method. A p300 HAT inhibitor, C646, was added to the protein extracts from the hearts of PRMT5-TG mice. Values are presented as mean ± SD (n = 10 mice/group). f Immunostaining images for α-actinin to determine the cell surface area of cardiomyocytes, quantified using ImageJ software. Scale bars: 20 µm. Values are presented as mean ± SD (n = 4). Data are analyzed using one-way ANOVA, followed by Tukey’s multiple comparison ( c , e , f ) or Dunnett’s multiple comparison tests versus the PE-treated group ( d ). * p < 0.05, ** p < 0.01, *** p < 0.001
Techniques Used: Methylation, Cell Culture, Transgenic Assay, Western Blot, Activity Assay, Immunostaining, Software, Comparison
![PRMT5 methylates p300 at R200. a The plasmids of WT PRMT5 and the deletion mutant lacking enzymatic activity of PRMT5 (ΔPRMT5) were transfected into HEK293T cells. Immunoprecipitation of p300 and Western blotting was performed. b GST pull-down assay was performed with GST-fusioned aa1-450, aa1514-1922, and aa1817-2160 of p300 mutants extracted from E. coli . [ 35 S]radiolabeled PRMT5 was obtained using an in vitro translation system. The arrows show GST fusion proteins. c PRMT5 and aa1-450, aa1514-1922, and aa1817-2160 of p300 mutants were mixed in reaction solution with [ 14 C]radiolabeled S-adenosyl methionine (SAM). The proteins were analyzed using SDS-PAGE and scanned using BAS2000. d PRMT5 and R200K, R202K, and R237K of p300 aa1-450 point mutants were mixed in reaction solution with [ 14 C]radiolabeled SAM, and an in vitro methylation assay was performed](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_9037/pmc12229037/pmc12229037__12929_2025_1162_Fig5_HTML.jpg "PRMT5 methylates p300 at R200. a The plasmids of ...")
Figure Legend Snippet: PRMT5 methylates p300 at R200. a The plasmids of WT PRMT5 and the deletion mutant lacking enzymatic activity of PRMT5 (ΔPRMT5) were transfected into HEK293T cells. Immunoprecipitation of p300 and Western blotting was performed. b GST pull-down assay was performed with GST-fusioned aa1-450, aa1514-1922, and aa1817-2160 of p300 mutants extracted from E. coli . [ 35 S]radiolabeled PRMT5 was obtained using an in vitro translation system. The arrows show GST fusion proteins. c PRMT5 and aa1-450, aa1514-1922, and aa1817-2160 of p300 mutants were mixed in reaction solution with [ 14 C]radiolabeled S-adenosyl methionine (SAM). The proteins were analyzed using SDS-PAGE and scanned using BAS2000. d PRMT5 and R200K, R202K, and R237K of p300 aa1-450 point mutants were mixed in reaction solution with [ 14 C]radiolabeled SAM, and an in vitro methylation assay was performed
Techniques Used: Mutagenesis, Activity Assay, Transfection, Immunoprecipitation, Western Blot, Pull Down Assay, In Vitro, SDS Page, Methylation
![PRMT5-mediated p300 arginine methylation of R200 is required for p300 histone acetyltransferase activity. a The plasmids encoding p300 WT or p300 R200K point mutant and PRMT5 were transfected to HEK293T cells. Immunoprecipitation by anti-HA antibody followed by Western blotting was performed. The band density was measured using ImageJ software. Values are presented as mean ± SD (n = 3). b p300 WT and p300 R200K point mutant were purified using anti-HA-tag agarose beads from HEK293T cells co-transfected with or without PRMT5. Purified p300 was incubated with recombinant histone H3 peptide and [ 3 H]-labeled acetyl-CoA. The histone H3 peptides were isolated, and radioactivity was measured using a liquid scintillation counter. Values are presented as mean ± SD (n = 6). Data are analyzed using two-way ANOVA, followed by Tukey’s multiple comparison test. p < 0.05 was considered statistically significant. * p < 0.05, *** p < 0.001](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_9037/pmc12229037/pmc12229037__12929_2025_1162_Fig6_HTML.jpg "PRMT5-mediated p300 arginine methylation of R200 is required for ...")
Figure Legend Snippet: PRMT5-mediated p300 arginine methylation of R200 is required for p300 histone acetyltransferase activity. a The plasmids encoding p300 WT or p300 R200K point mutant and PRMT5 were transfected to HEK293T cells. Immunoprecipitation by anti-HA antibody followed by Western blotting was performed. The band density was measured using ImageJ software. Values are presented as mean ± SD (n = 3). b p300 WT and p300 R200K point mutant were purified using anti-HA-tag agarose beads from HEK293T cells co-transfected with or without PRMT5. Purified p300 was incubated with recombinant histone H3 peptide and [ 3 H]-labeled acetyl-CoA. The histone H3 peptides were isolated, and radioactivity was measured using a liquid scintillation counter. Values are presented as mean ± SD (n = 6). Data are analyzed using two-way ANOVA, followed by Tukey’s multiple comparison test. p < 0.05 was considered statistically significant. * p < 0.05, *** p < 0.001
Techniques Used: Methylation, Activity Assay, Mutagenesis, Transfection, Immunoprecipitation, Western Blot, Software, Purification, Incubation, Recombinant, Labeling, Isolation, Radioactivity, Comparison
Figure Legend Snippet: Graphical abstract. The gain-of-function of PRMT5 accelerates pressure overload-induced cardiomyocyte hypertrophy and heart failure. PRMT5 methylates p300 at R200 and regulates p300 HAT activity, which is essential for histone acetylation during the development of cardiomyocyte hypertrophy
Techniques Used: Activity Assay