Description
Recombinant full-length human PRMT5 was expressed by baculovirus in Sf9 insect cells using an N-terminal GST tag.
Scientific Background: PRMT5 is a protein arginine methyltransferase and part of a 20S methyltransferase complex that modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins (1). This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles. MEP50 associates with PRMT5 in the 20S arginine methyltransferase complex in HeLa cells (2). Antibodies directed against MEP50 can reduce the arginine methyltransferase activity of the immunopurified complex toward Sm substrates. PRMT5-mediated transcriptional repression of reporter gene is dependent on MEP50