PTMScan® Mono-Methyl Lysine Motif (mme-K) Kit #16892
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This product is intended for peptide enrichment and mass spectrometry analysis. To learn more about our Proteomics Kits and Services please answer a few questions for our Proteomics group.
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Background
Most PKMT substrates are histone proteins and transcription factors, emphasizing the importance of lysine methylation in regulating chromatin structure and gene expression. Lys9 of histone H3 is mono- or di-methylated by G9A/GLP and tri-methylated by SETDB1 to activate transcription. JHDM3A-mediated demethylation of the same residue creates mono-methyl Lys9 and inhibits gene transcription (5). Tumor suppressor p53 is regulated by methylation of at least four sites. p53-mediated transcription is repressed following mono-methylation of p53 at Lys370 by SMYD2. Mono-methylation at Lys382 by SET8 suppresses p53 transcriptional activity, while SET7/9 mono-methylation at Lys372 inhibits SMYD2 methylation at Lys370 and stabilizes the p53 protein (1,6). Overexpression of PKMTs is associated with multiple forms of human cancer, which has generated tremendous interest in targeting protein lysine methyltransferases in drug discovery research.
- Lanouette, S. et al. (2014) Mol Syst Biol 10, 724.
- Clarke, S.G. (2013) Trends Biochem Sci 38, 243-52.
- Herold, J.M. et al. (2011) Curr Chem Genomics 5, 51-61.
- Thinnes, C.C. et al. (2014) Biochim Biophys Acta 1839, 1416-32.
- Klose, R.J. et al. (2006) Nature 442, 312-6.
- Yost, J.M. et al. (2011) Curr Chem Genomics 5, 72-84.
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