Full-length human recombinant PRMT5. PRMT5, a type II arginine methyltransferase, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (SAM) to an omega-nitrogen of the guanidino function of protein L-arginine residues (omega-monomethylation) and the transfer of a second methyl group to the other omega-nitrogen, yielding symmetric dimethylarginine (sDMA). PRMT5 catalytic activity with certain substrates (e.g. histones H2A, H4) can be weak when PRMT5 is not complexed with MEP50, which may be due to MEP50’s role in substrate binding. However, Reaction Biology has found that PRMT5 alone displays significant activity with GST-GAR (see data sheet). The GAR domain of this substrate (“glycine and arginine rich”) derives from the N-terminus of fibrillarin, a nucleolar protein and RNA methyltransferase that can form a protein complex whose components include PRMT5 and PRMT1. In complex with MEP50, PRMT5 is also a component of multiple macromolecular complexes (e.g. 20S Methylosome, Swi/Snf), 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. PRMT5’s pro-proliferative effects and their association with multiple cancers (e.g. lung, breast, ovarian, lymphoid) has led to increased interest in its possible targeting for anti-cancer therapy.
ACCESSION #: NM_006109
INCLUDES AMINO ACIDS: 2-637
TAG(S): N-terminal Flag tag
MW: 73.7 kDa
EXPRESSION SYSTEM: Insect cell/Baculovirus
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.
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