|Products||Mouse Anti-PRMT5 Monoclonal Antibody, Unconjugated, Clone PRMT5-21 from GeneTex|
|Item||Mouse Anti-PRMT5 Monoclonal Antibody, Unconjugated, Clone PRMT5-21|
|Description|| Mouse monoclonal [PRMT5-21] to PRMT5|
Arginine methylation is an irreversible post translational modification which has only recently been linked to protein activity. At least three types of PRMT enzymes have been identified in mammalian cells. These enzymes have been shown to have essential regulatory functions by methylation of key proteins in several fundamental areas. These protein include nuclear proteins (Histone 2A, 3, 4), IL enhancer binding factor, nuclear factors (NF45, 90, ILF3, Nucleolin, STAT1, Poly(A) binding protein II), cell cycle proteins (phosphoprotein phosphatase 2A), signal transduction proteins (FGF2, Fibrillarin, FN, INFAR1, Jak, MBP, Src-adaptor Sam68), apoptosis proteins (FADD, ICE-like protease), and viral proteins (Hepatitis C NS3 RNA Helicase, HIV TAR). The mammalian PRMT family currently consists of 5 members that share two large domains of homology. Outside of these domains, epitopes were identified and antibodies against all five PRMT members have been developed. These antibodies can be utilized to explore arginine methylation and its regulatory functions.
Immunogen: Antibody was produced by the fusion of mouse myeloma cells and splenocytes from mice immunized with PRMT5 containing the C-terminal region of the Human PRMT5 (amino acids 315-637).
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