PRMT2 (Protein Arginine Methyltransferase 2) is a member of the PRMT family, which catalyzes the post-translational methylation of arginine residues in proteins, influencing chromatin remodeling, transcriptional regulation, and cellular signaling. As a type I PRMT, it mediates asymmetric dimethylation of arginine, primarily targeting histones (e.g., H3R8. H4R3) and non-histone substrates like EGFR, ERα, and NF-κB. PRMT2 contains a conserved S-adenosylmethionine (SAM)-binding domain but lacks a canonical catalytic domain, suggesting it may act as a regulatory co-factor or collaborate with other PRMTs for enzymatic activity.
PRMT2 antibodies are essential tools for studying its expression, localization, and interactions in cellular processes. They are widely used in techniques such as Western blotting, immunoprecipitation, and immunohistochemistry to detect PRMT2 in tissues or cell lines. Specific antibodies help identify PRMT2 isoforms (e.g., the shorter variant lacking the N-terminal region) and assess its role in diseases. Research links PRMT2 to cancer progression (e.g., breast cancer via ERα modulation), inflammatory responses, and metabolic disorders, highlighting its potential as a therapeutic target. Validated antibodies are critical for elucidating PRMT2's context-dependent functions and its interplay with signaling pathways, advancing studies in epigenetics and disease mechanisms.