Human recombinant PRMT5 in complex with human recombinant MEP50, produced by co-expression in an insect cell/baculovirus expression system. PRMT5, a type II 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 other w-nitrogen, yielding symmetric dimethylarginine (sDMA). Structural studies show the PRMT5/MEP50 complex to consist of four heterodimers. PRMT5 catalytic activity is weak when not complexed with MEP50, which may be due to MEP50’s role in substrate binding. A component of multiple macromolecular complexes (e.g. 20S Methylosome, Swi/Snf), PRMT5/MEP50 is located in both the nucleus and cytoplasm, modifies a variety of substrates and plays roles in chromatin remodeling, RNA processing, and regulation of gene expression, cell growth and differentiation. Its pro-proliferative effects and their association with multiple cancers (lung, breast, ovarian, lymphoid) has led to increasing interest in PRMT5 as a target for anti-cancer therapy.

SUPPLIED AS: Solution of purified recombinant protein in 50 mM Tris/HCl, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 3 mM TCEP, 20% (v/v) glycerol.

STORAGE: -80°C, aliquot and snap-freeze after first use.