Full-length, human recombinant PRMT7 expressed in a baculovirus system. PRMT7, type III arginine methyltransferase, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (SAM) to an ?-nitrogen of the guanidino function of protein L-arginine residues forming ?-NG-monomethylarginine, but is apparently not capable of forming asymmetric (type I activity) or symmetric (type II activity) dimethylarginine. Recombinant PRMT7 can methylate various proteins in vitro including histones H2A, H3 and H4. RBC's PRMT7 (His) is particularly active with fibrillarin, GST-GAR (GST fusion with N-terminal region of fibrillarin) and in scintillation proximity assay, a peptide derived from histone H2B. PRMT7 interacts with PRMT5 in vivo and both enzymes are implicated and may cooperate in the methylation of histone H3 Arg-2 and the Sm ribonucleoproteins. PRMT7 expression is elevated in highly metastatic breast cancer lines and in breast carcinomas generally. PRMT7 overexpression promotes epithelial-mesenchymal transition, cell migration and invasiveness and a reduction of E-cadherin expression. Conversely, knockdown of PRMT7 in MDA-MB-231 cells inhibited these processes, suggesting PRMT7 as a therapeutic target for metastatic breast cancer.

SUPPLIED AS: Solution of purified recombinant protein in 50mM Tris, pH 7.5, 500mM NaCl, 10% (w/v) glycerol, 1 mM TCEP

STORAGE: -70°C, aliquot and snap-freeze after first use.