WB-Western Blot IP-Immunoprecipitation IHC-Immunohistochemistry IF-Immunofluorescence ICC-Immunocytochemistry FC-Flow Cytometry

PRMT7 also known as ANM7 is a member of the protein arginine N-methyltransferase family of proteins. PRMT7 plays a crucial role in arginine methylation, an irreversible post-translational modification essential for various cellular functions, including signal transduction, RNA transport, and RNA splicing. This modification is catalyzed by arginine methyltransferases like PRMT7, which utilizes S-adenosylmethionine as the methyl donor. PRMT7 contains two methyltransferase domains, each featuring a putative S-adenosylmethionine-binding motif, with the N-terminal domain closely resembling the catalytic core of PRMT5 and the C-terminal domain showing similarity to PRMT1. Three splice variants of PRMT7 have been identified, indicating a potential for diverse functional roles.