Rabbit Anti-Human PRMT10 Antibodies
- Known as:
- Rabbit Antibody toHuman PRMT10 Antibodies
- Catalog number:
- RB-15-0003-200
- Product Quantity:
- 200
- Category:
- -
- Supplier:
- Ray Biotech
- Gene target:
- Rabbit Anti-Human PRMT10 Antibodies
Related genes to: Rabbit Anti-Human PRMT10 Antibodies
- Gene:
- PRMT9 NIH gene
- Name:
- protein arginine methyltransferase 9
- Previous symbol:
- PRMT10
- Synonyms:
- FLJ46629
- Chromosome:
- 4q31.23
- Locus Type:
- gene with protein product
- Date approved:
- 2009-05-15
- Date modifiied:
- 2015-09-07
Related products to: Rabbit Anti-Human PRMT10 Antibodies
Related articles to: Rabbit Anti-Human PRMT10 Antibodies
- Multicopy transgene arrays remain widely used in research. It is usually assumed that they behave neutrally, not impacting the phenotype under investigation. Here, we reveal that a previously reported heterochronic extra-molt phenotype associated with depends on the presence of the integrated molting reporter . Nanopore long-read sequencing shows that is a massive 8.8-Mb insertion - around 50% of the size of its host chromosome - which disrupts the gene. Both and another array, , cause dysregulation of the transcriptome and accumulation of reads mapping to the promoter sequences used as components of the array. We identify additional arrays exceeding 4 Mb and show that variable molting defects occur across different transgenic lines when combined with , implicating array size or composition in the synthetic phenotype. Our results underscore the necessity of replacing multicopy reporters in developmental studies with single-copy insertions or endogenous tagging whenever possible. - Source: PubMed
Publication date: 2026/05/05
Katic IskraPapasaikas PanagiotisGaidatzis DimosGroßhans Helge - Arginine methylation catalyzed by protein arginine methyltransferases (PRMTs) is required for cancer cell proliferation, but whether PRMTs mediate resistance to therapy remains elusive. Here, we have performed loss-of-function screens in venetoclax-resistant (VEN-R) AML patient-derived xenograft (PDX) cells and found that PRMT9 plays a critical role in promoting VEN resistance. Specifically, VEN-R AML samples exhibited high levels of PRMT9, and PRMT9 inhibition re-sensitized the AML cells to VEN treatment. In preclinical resistant models, genetic ablation of PRMT9 synergized with VEN to eradicate AML cells. Consistently, pharmacologic inhibition of PRMT9 combined with VEN yielded similar effects in VEN-R AML mouse models. Mechanistically, PRMT9 ablation disrupted RNA splicing by inducing exon-skipping of mRNA encoding ALG13, an UDP-N-Acetylglucosaminyltransferase subunit, downregulating expression of a VEN-efflux transporter encoded by the adenosine triphosphate binding cassette subfamily C member 1 (ABCC1) gene. PRMT9 inhibition also suppressed protein synthesis, downregulating short-lived oncoproteins, such as MCL1. These findings establish a connection between PRMT9-mediated arginine methylation and poor VEN responsiveness, also demonstrate that targeting PRMT9 may represent a viable strategy to overcome VEN resistance. - Source: PubMed
Publication date: 2026/05/12
Li YangHe XinZhang LeiDong HaojieWang XinChe YuanYadav Umesh PrasadLiu MengZhang LianjunGe ShuaishuaiWu GuohuaFu Yu-HsuanChen WeiKuo Ya-HueiChen LiangMarcucci GuidoWang ShaoyuanLi Ling - During myocardial infarction (MI), M1-like macrophages exacerbate myocardial injury by excessively secreting inflammatory cytokines. Therefore, modulating the activity of M1-like macrophages may represent a novel therapeutic strategy for MI. PRMTs (protein arginine methyltransferases) primarily regulate protein function via asymmetric dimethylation, but PRMT9 does so through symmetric dimethylation. However, its role in cardiovascular diseases has yet to be established. In this study, we investigated the role of PRMT9 in macrophage polarization in the context of MI and explored its therapeutic effect for MI. - Source: PubMed
Publication date: 2026/02/11
Bai XuemeiRen RuiqingYuan JiahuaYu LiwenDong NaCao NanZhou MinZhang JiaJiaLi XiaoxiaoHe ZiyeLiu BingyuZhang MengGao Chengjiang - Protein arginine methyltransferase 9 (PRMT9) is dysregulated in various malignancies, particularly in lung adenocarcinoma (LUAD). This study aims to systematically investigate the expression patterns, biological functions, and underlying molecular mechanisms of PRMT9 in LUAD pathogenesis. - Source: PubMed
Publication date: 2025/12/10
Chen JinghuaYang JiahaoChen ZihaoChu Xiangpeng - Protein arginine methyltransferase 9 (PRMT9) is part of the PRMT family, and it is suspected to function in pathways relevant to neurodevelopment. It is thought to participate in alternative splicing through interactions with the splicing factor SF3B2 (SAP145). In this study, we report 26 families (35 individuals) with bi-allelic loss-of-function variants in PRMT9, implicating PRMT9 in an autosomal-recessive human disease. Individuals primarily present with a neurodevelopmental disorder characterized by global developmental delay, learning disabilities, mild to severe intellectual disability, autism spectrum disorder, epilepsy, and hypotonia. The mutation spectrum includes 26 different variants such as frameshifting indels, nonsense variants, missense variants, and two copy-number variants. Mapping of the disease-causing missense variants onto the crystal structure of PRMT9 revealed that several of the variants reside within the catalytically active module of PRMT9, likely impairing its methyltransferase activity and resulting in a loss of function. In skin fibroblasts derived from affected individuals, we observed reduced expression at the RNA and/or protein level and subsequent aberrant methylation activity. Moreover, transcriptomic analysis of fibroblasts from affected individuals indicated differential expression of genes related to intellectual disability, autism, and cilia, suggesting a role of PRMT9 during ciliogenesis. Under ciliogenesis conditions, the skin-derived fibroblasts exhibited anomalies in the length of primary cilia but normal amounts of cilia. In addition, a prmt9 knockout zebrafish model displayed abnormal social preference in adult animals. Altogether, our findings implicate bi-allelic PRMT9 loss-of-function variants as causal for neurodevelopmental disorders. - Source: PubMed
Publication date: 2025/11/18
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