PRMT8, a type I arginine methyltransferase, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (SAM) to an w-nitrogen of the guanidino function of protein L-arginine residues (w-monomethylation) and the transfer of a second methyl group to the same nitrogen, yielding asymmetric dimethylarginine (aDMA). Although highly homologous (>80% identity) to the major arginine methyltransferase PRMT1, distinctive characteristics of PRMT8 include a unique, regulatory 76 residue N-terminal domain and its brain-specific expression, especially enhanced in the cortex. Although transfected GFP-PRMT8 can be myristoylated and localized to the plasma membrane, other evidence suggests that the endogenous, central nervous system PRMT8 is a nuclear protein. Removal of the N-terminal 60 amino acids of PRMT8 has been shown to dramatically enhance PRMT8 catalytic activity. RBC’s PRMT8 is deleted for residues 1-60 and is highly active with the substrate GST-GAR.
ACCESSION #: NM_019854
INCLUDES AMINO ACIDS: 61-394
TAG(S): N- & C-terminal His-tags
MW: 43.2 kDa
EXPRESSION SYSTEM: E. coli
SUPPLIED AS: Solution of purified recombinant protein in 50 mM Tris/HCl, pH 7.5, 125 mM NaCl, 1 mM TCEP, 10% (v/v) glycerol
STORAGE: -80°C, aliquot and snap-freeze after first use.
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