|Other Names||Histone-arginine methyltransferase CARM1, 211-, Coactivator-associated arginine methyltransferase 1, Protein arginine N-methyltransferase 4, CARM1, PRMT4|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI 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.
Protein arginine N-methyltransferases, such as CARM1,catalyze the transfer of a methyl group fromS-adenosyl-L-methionine to the side chain nitrogens of arginineresidues within proteins to form methylated arginine derivativesand S-adenosyl-L-homocysteine. Protein arginine methylation hasbeen implicated in signal transduction, metabolism of nascentpre-RNA, and transcriptional activation (Frankel et al., 2002[PubMed 11724789]).
Gao, X., et al. J. Cell. Biochem. 110(1):162-170(2010)Carascossa, S., et al. Genes Dev. 24(7):708-719(2010)Kim, Y.R., et al. BMC Cancer 10, 197 (2010) :Ito, T., et al. BMC Dev. Biol. 9, 47 (2009) :Haiman, C.A., et al. BMC Cancer 9, 43 (2009) :
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