PRMT5 (Protein Arginine Methyltransferase 5) is a key enzyme responsible for symmetric dimethylation of arginine residues (SDMA) on histones and non-histone proteins, playing a critical role in epigenetic regulation, RNA splicing, DNA repair, and cellular signaling. As a member of the PRMT family, it catalyzes the transfer of methyl groups from S-adenosylmethionine (SAM) to specific arginine residues, primarily targeting substrates like histone H4R3. H3R8. and non-histone proteins (e.g., spliceosome components). Dysregulation of PRMT5 is linked to cancer, cardiovascular diseases, and neurological disorders, with overexpression observed in multiple malignancies, making it a therapeutic target.
PRMT5 antibodies are essential tools for studying its expression, localization, and functional roles. These antibodies are widely used in techniques such as Western blotting, immunoprecipitation (IP), immunofluorescence (IF), and immunohistochemistry (IHC) to detect PRMT5 protein levels or assess methylation status of its substrates. Specificity varies depending on the epitope; some antibodies recognize total PRMT5. while others distinguish between methylated forms (e.g., anti-SDMA antibodies). Validated PRMT5 antibodies help elucidate its interaction networks, downstream pathways, and responses to inhibitors in preclinical models. Recent research focuses on developing selective PRMT5 inhibitors, and corresponding antibodies are critical for pharmacodynamic biomarker analysis in drug development. Challenges include cross-reactivity with other PRMTs, emphasizing the need for rigorous validation using knockout controls or peptide competition assays.