Recombinant full-length human protein was used as the immunogen for the PRMT7 antibody.
Arginine methylation is an irreversible protein modification catalyzed by Arginine methyltransferases, such as PRMT7, which uses S-adenosylmethionine (AdoMet) as the methyl donor. Arginine methylation is implicated in signal transduction, RNA transport and RNA splicing. PRMT7 has two methyltransferase domains, each containing a putative AdoMet-binding motif. The N-terminal methyltransferase domain closely resembles the catalytic core of PRMT5, and the C-terminal domain is most similar to that of PRMT1. Three PRMT7 splice variants have been identified by database analysis. PRMT7 is localized to the nucleus and cytoplasm and moderate expression is observed in adult brain and lung tissues.
