PRMT6 antibody Polyclonal Antibodies Primary antibodies
- Known as:
- PRMT6 (anti-) Polyclonal Antibodies Primary antibodies
- Catalog number:
- orb100707
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- PRMT6 antibody Polyclonal Antibodies Primary antibodies
Related genes to: PRMT6 antibody Polyclonal Antibodies Primary antibodies
- Gene:
- PRMT6 NIH gene
- Name:
- protein arginine methyltransferase 6
- Previous symbol:
- HRMT1L6
- Synonyms:
- FLJ10559
- Chromosome:
- 1p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-06-22
- Date modifiied:
- 2016-10-05
Related products to: PRMT6 antibody Polyclonal Antibodies Primary antibodies
Related articles to: PRMT6 antibody Polyclonal Antibodies Primary antibodies
- Enhancer of zeste homologue 2 (EZH2), as a key histone methyltransferase, is elevated in multiple malignant tumours, which leads to poor prognosis. However, the underlying mechanisms for mediation of EZH2 enzyme activity remain elusive. Here, we report that PRMT6 asymmetrically dimethylates EZH2 at R509 to promote the bindings between EZH2 and other core component of the polycomb repressive complex 2 (PRC2), which enhances PRC2 induced methylation of histone H3 at K27. EZH2 R509 methylation blocks the expression of PRC2 target genes, leading to breast tumorigenesis in vitro and in vivo. Combination of PRMT6 inhibitor EPZ020411, and EZH2 inhibitor GSK126 effectively suppresses breast tumour growth in the mouse xenografts. Furthermore, immunohistochemical analyses demonstrate there is a positive correlation between PRMT6 and meR509-EZH2 expression in the breast cancer tissues. Consistently, PRMT6 mediated EZH2 R509 methylation is also confirmed in PRMT6-knockout mice. Our findings reveal that PRMT6 inhibitors might be promising combination therapy for EZH2-targeting cancer. - Source: PubMed
Publication date: 2026/04/19
Han XueZhang MaoxiangLu ChaoXu HuiDu ShiyuYue ChenjingYu Zhenhai - Neonatal mice achieve scar-free healing after spinal cord injury (SCI) by restoring microglial homeostasis, unlike adults, where persistent microglial dyshomeostasis drives scar expansion through mechanisms that remain elusive. Using RNA sequencing, we identified protein arginine methyltransferase 6 (PRMT6) as a key regulator of this disparity, upregulated in activated microglia at adult SCI lesions but maintained at low levels in neonatal microglia after injury. In adult mice, Prmt6 deficiency restored microglial homeostasis, evidenced by increased P2Y12/TMEM119 and reduced CD68, while reducing scar formation and enhancing axonal regrowth and motor recovery. Microglia-specific Prmt6 knockdown or PRMT6 inhibitor administration recapitulated these effects. Mechanistically, PRMT6 deposits H3R2me2a at the Ppargc1a promoter to repress peroxisome proliferator-activated receptor-γ coactivator-1α（PGC-1α）, thereby inhibiting fatty acid oxidation (FAO) and disrupting microglial homeostasis. Loss of Prmt6 alleviates this epigenetic repression, restoring FAO and microglial homeostasis. These findings establish PRMT6 as a novel epigenetic regulator linking microglial dyshomeostasis and metabolic dysfunction to maladaptive scar formation in adult SCI, highlighting PRMT6 inhibition as a promising therapeutic strategy to reprogram microglial metabolism and promote neural repair. - Source: PubMed
Publication date: 2026/04/17
Peng WeilinWu ZhengqiangXiong YuGao ZhongyaLiu YishanWang ZiyiWang HaibinHan ChaofengChu WenxiangLu Xuhua - Protein arginine methyltransferases (PRMTs) catalyze the methylation of arginine residues on both histone and non-histone substrates, orchestrating cellular processes such as transcriptional regulation, RNA splicing, signal transduction, and DNA damage response. Because dysregulated methylation reprograms epigenetic and post-transcriptional landscapes to promote malignant transformation, aberrant PRMT activity is closely associated with tumorigenesis and cancer progression. Major family members, containing PRMT1, CARM1, PRMT5, and PRMT6, regulate gene expression through site-specific histone methylation, thereby contributing to the transcriptional activation or repression. PRMTs also methylate a wide range of non-histone proteins, including transcription factors, splicing regulators, and signaling intermediates, to coordinate cell cycle progression, DNA repair, and RNA metabolism. Collectively, PRMT-mediated methylation contributes to higher-order cancer phenotypes, including metabolic reprogramming-through modulation of glycolytic flux, lipid biosynthesis, and redox homeostasis-and immune evasion via altered immune signaling and checkpoint pathways within the tumor microenvironment. Recent advances in chemical biology have led to the development of selective PRMT inhibitors, several of which are currently under clinical evaluation. In this review, we provide a comprehensive and integrative overview of PRMT biology, systematically organizing current knowledge from multilayered regulatory mechanisms to downstream oncogenic effects and emerging therapeutic opportunities. - Source: PubMed
Publication date: 2026/04/02
Jeong YoonaeCho YenaKim Yong Kee - Protein arginine methyltransferases are key epigenetic regulators and promising targets for cancer therapy. PRMT4 plays an important role in transcriptional regulation and tumor progression, yet selective inhibition remains challenging because type I PRMTs share highly conserved catalytic sites. The success of allosteric inhibitors targeting PRMT3 and PRMT6 suggests that selective modulation through regulatory sites outside the catalytic pocket may also be feasible for PRMT4. Motivated by this rationale, we investigated whether PRMT4 undergoes conformational transitions between active and inactive states and whether it contains allosterically targetable pockets capable of regulating its enzymatic activity. Using an integrated computational strategy, we characterized the conformational dynamics and allosteric regulation mechanisms of PRMT4. Structural analysis identified a molecular switch involving order and disorder transitions of the N terminal helices that governs the active inactive transition. Free energy landscape analysis supported that this transition is thermodynamically accessible. We identified a PRMT3 like allosteric pocket, Cavity 1, whose targeting is predicted to disrupt inter chain communication and impair cofactor binding and active site organization. Dynamic residue network analysis further supported Cavity 1 as a functional allosteric site. We also identified a PRMT4 specific pocket, Cavity 2, with a distinct selectivity profile. These findings validate the active inactive switch and identify two druggable allosteric sites. Although experimental validation is required, this work provides a computational framework for the rational design of PRMT4 selective allosteric inhibitors. - Source: PubMed
Publication date: 2026/03/26
Abbas AmrMiao ZhanpengJin JiaYe Fei - Heterotopic ossification (HO) is a debilitating disorder marked by ectopic bone formation in soft tissues, frequently triggered by inflammation after trauma. While macrophage-driven inflammation plays a critical role in HO pathogenesis, the molecular mechanisms governing its initiation, amplification and resolution remain elusive. Using a trauma/burn injury (TBI)-induced mouse model of HO, we identified rapid and sustained macrophage accumulation at the injury site during the early inflammatory phase, and macrophage depletion markedly suppressed HO formation. Transcriptomic profiling identified a pronounced upregulation of protein arginine methyltransferase 6 (PRMT6) in macrophages following injury. Genetic deletion or macrophage-targeted knockdown of Prmt6 reduced macrophage accumulation and significantly attenuated HO, without impairing tendon repair. Consistently, pharmacological inhibition of PRMT6 suppressed HO only when administered during the early inflammatory phase, indicating a restricted therapeutic window. Mechanistically, PRMT6 amplified macrophage chemotactic signaling by transcriptionally and epigenetically upregulating CCL2. Genetic disruption of macrophage-derived CCL2 phenocopied Prmt6 deficiency, whereas CCL2 supplementation rescued macrophage recruitment and partially restored HO in Prmt6-deficient mice. At the molecular level, PRMT6 formed a coactivation complex with NF-κB and catalyzed H3R17 asymmetric dimethylation at the Ccl2 promoter, thereby promoting sustained chemokine expression. Collectively, our findings identify PRMT6 as a central epigenetic amplifier of macrophage-driven inflammation that links early injury responses to ectopic bone formation. Targeting PRMT6 during the early inflammatory phase represents a promising strategy to prevent HO while preserving physiological tissue repair. - Source: PubMed
Publication date: 2026/03/10
Chu WenxiangPeng WeilinWu ZhengqiangXiong YuGao ZhongyaLi YangZhang BangkeWang LiangWang HaibinHan ChaofengLu Xuhua