|Other Names||Protein arginine N-methyltransferase 7, 211-, Histone-arginine N-methyltransferase PRMT7, [Myelin basic protein]-arginine N-methyltransferase PRMT7, PRMT7, KIAA1933|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP1010c was selected from the C-term region of human PRMT7. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.|
|Cellular Location||Cytoplasm, cytosol. Nucleus|
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Provided below are standard protocols that you may find useful for product applications.
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, IL enhancer binding factor, nuclear factors, cell cycle proteins, signal transduction proteins, apoptosis proteins, and viral proteins. The mammalian PRMT family currently consists of 7 members that share two large domains of homology. Outside of these domains, epitopes were identified and antibodies against all 7 PRMT members have been developed.
Lee,J.H., et al. J. Biol. Chem. 280 (5), 3656-3664 (2005)Miranda,T.B., et al. J. Biol. Chem. 279 (22), 22902-22907 (2004)Frankel A., et al. J. Biol. Chem. 277:3537-3543(2002).Pal, S., et al., Mol. Cell. Biol. 23(21):7475-7487 (2003).Rho, J., et al., J. Biol. Chem. 276(14):11393-11401 (2001).Pollack, B.P., et al., J. Biol. Chem. 274(44):31531-31542 (1999).Gilbreth, M., et al., PNAS 95(25):14781-14786 (1998).
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