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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 (NF-45, -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.
Our Abpromise guarantee covers the use of ab3763 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/100 - 1/500. Predicted molecular weight: 49 kDa.|
|IHC-P||1/50 - 1/100.|
|ChIP||Use 10µl for 106 cells.|
Sonicated Chromatin prepared from untreated or 17beta-estradiol (E2) treated MCF7 cells was subjected to the ChIP procedure with ab3763 to PRMT2 and the immunoprecipitated chromatin was analysed in the proximal region of the estrogen-responsive pS2 promoter (as shown above) and quantified by real-time PCR (values are % of inputs). The primers are designed to follow the nucleosome E (including the Estrogen Responsive Element ERE). 10
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