货号 | 25081S |
供应商 | CST |
背景 | As an integral part of the machinery of cellular function, proteins undergo regulation by a variety of post-translational modifications. One of the most prevalent and widely studied PTMs is Serine/Threonine phosphorylation. A few prominent kinases targeting a handful of substrate consensus motifs account for a majority of the tens of thousands of known and predicted sites on more than 13,000 human proteins (1-3). Cell Signaling Technology has developed phospho-Ser/Thr motif antibodies for proteomic profiling of kinase substrates. These include, among others, substrates of Akt, AMPK, MAPK, CDK, PKA, PKC, and CKII. |
存放说明 | -20C |
参考文献 | 1 . Rao, R.S. and Møller, I.M. (2012) Biochim Biophys Acta 1824, 405-12. 2 . Goel, R. et al. (2012) Mol Biosyst 8, 453-63. 3 . Pearson, R.B. and Kemp, B.E. (1991) Methods Enzymol 200, 62-81. |
The Motif Logo was generated from a PhosphoScan® LC-MS/MS experiment using 581 nonredundant Lys-C/tryptic peptides generated from 293T cells treated with Calyculin A #9902 (10 nM, 30 min) and immunoprecipitated using PTMScan® Phospho-Ser/Thr Motif [pS/T] Immunoaffinity Beads. The Motif Logo demonstrates the relative abundance of amino acids in a given position within this data set. | |
The chart shows the underlying distribution of phospho-peptide motifs in a PhosphoScan® LC-MS/MS experiment using 581 nonredundant Lys-C/tryptic peptides generated from 293T cells treated with Calyculin A #9902 (10 nM, 30 min) and immunoprecipitated with PTMScan® Phospho-Ser/Thr Motif [pS/T] Immunoaffinity Beads. |