|Other Names||Protein arginine N-methyltransferase 2, 211-, Histone-arginine N-methyltransferase PRMT2, PRMT2, HMT1, HRMT1L1|
|Target/Specificity||The synthetic peptide sequence is selected from aa 37~53 of human PRMT2.|
|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 methylates the guanidino nitrogens of arginyl residues in proteins such as STAT3, FBL, histone H4. Acts as a coactivator (with NCOA2) of the androgen receptor (AR)-mediated transactivation. Acts as a coactivator (with estrogen) of estrogen receptor (ER)-mediated transactivation. Enhances PGR, PPARG, RARA-mediated transactivation. May inhibit NF-kappa-B transcription and promote apoptosis. Represses E2F1 transcriptional activity (in a RB1- dependent manner). May be involved in growth regulation.|
|Cellular Location||Isoform 1: Cytoplasm. Nucleus. Note=Translocates from the cytoplasm to the nucleus, after hormone exposure. Excluded from nucleolus Isoform PRMT2Beta: Cytoplasm. Nucleus. Nucleus, nucleolus Isoform PRMT2L2: Cytoplasm. Nucleus. Note=Predominantly cytoplasmic|
|Tissue Location||Widely expressed. Highly expressed in androgen target organs such as heart, prostate, skeletal muscle, ovary and spinal cord.|
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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.
Wada K, et al. Biochim Biophys Acta. 2002. 1591:1.Cimato TR, et al. J Neurosci Res. 2002. 67:435.Frankel A, et al. J Biol Chem. 2002. 277:3537.Brahms H, et al. RNA. 2001. 7:1531.Pelletier M, et al. Mol Biochem Parasitol. 2001. 118:49.Belyanskaya LL, et al. J Biol Chem. 2001. 276:18681.Rho J, et al. J Biol Chem. 2001. 276:11393.Scorilas A, et al. Biochem Biophys Res Commun. 2000. 278:349.Frankel A, et al. J Biol Chem. 2000. 275:32974.Zhang X, et al. EMBO J. 19:3509.Tang J, et al. J Biol Chem. 1998. 273:16935.
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