| 货号 | 26101S |
| 供应商 | CST |
| 背景 | Lysine is subject to a wide array of regulatory post-translational modifications due to its positively charged ε-amino group side chain. The most prevalent of these are ubiquitination and acetylation, which are highly conserved among prokaryotes and eukaryotes (1,2). Acyl group transfer from the metabolic intermediates acetyl-, succinyl-, malonyl-, glutaryl-, butyryl-, propionyl-, and crotonyl-CoA all neutralize lysine’s positive charge and confer structural alterations affecting substrate protein function. Lysine acetylation is catalyzed by histone acetyltransferases, HATs, using acetyl-CoA as a cofactor (3,4). Deacylation is mediated by histone deacetylases, HDACs 1-11, and NAD-dependent Sirtuins 1-7. Some sirtuins have little to no deacetylase activity, suggesting that they are better suited for other acyl lysine substrates (5). |
| 存放说明 | -20C |
| 参考文献 | Liu, Z. et al. (2014) Nucleic Acids Res 42, D531-6. Lee, S. (2013) Toxicol Res 29, 81-6. Lin, H. et al. (2012) ACS Chem Biol 7, 947-60. Zhang, Z. et al. (2011) Nat Chem Biol 7, 58-63. Du, J. et al. (2011) Science 334, 806-9. Hirschey, M.D. and Zhao, Y. (2015) Mol Cell Proteomics [Epub ahead of print] Tan, M. et al. (2014) Cell Metab 19, 605-17. |
The chart shows the relative category distribution of proteins with glutarylated lysine residues derived from peptides identified in a PTMScan® LC-MS/MS experiment of mouse liver tissue using PTMScan® Glutaryl-Lysine [Glut-K] Immunoaffinity Beads. | |
The Motif Logo was generated from a PTMScan® LC-MS/MS experiment using 190 nonredundant tryptic peptides derived from mouse liver tissue immunoprecipitated with PTMScan® Glutaryl-Lysine [Glut-K] Immunaffinity Beads. The logo represents the relative frequency of amino acids in each position surrounding the central glutarylated residue within this data set. |
