|Other Names||Histone-arginine methyltransferase CARM1, 211-, Coactivator-associated arginine methyltransferase 1, Protein arginine N-methyltransferase 4, CARM1, PRMT4|
|Target/Specificity||The synthetic peptide sequence is selected from aa 341~357 of human PRMT4.|
|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||Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activate transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg- 2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA- stabilizing properties and the half-life of their target mRNAs.|
|Cellular Location||Nucleus. Cytoplasm. Note=Mainly nuclear during the G1, S and G2 phases of the cell cycle. Cytoplasmic during mitosis, after breakup of the nuclear membrane|
|Tissue Location||Overexpressed in prostate adenocarcinomas and high-grade prostatic intraepithelial neoplasia|
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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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