Technology employs a proprietary methodology from Cell Signaling Technology (CST) for peptide enrichment by immunoprecipitation using a specific bead-conjugated antibody in conjunction with liquid chromatography (LC) tandem mass spectrometry (MS/MS) for quantitative profiling of post-translational modification (PTM) sites in cellular proteins. These include phosphorylation (PhosphoScan®
), ubiquitination (UbiScan®
), acetylation (AcetylScan®
), and methylation (MethylScan®
), among others. PTMScan®
Technology enables researchers to isolate, identify, and quantitate large numbers of post-translationally modified cellular peptides with a high degree of specificity and sensitivity, providing a global overview of PTMs in cell and tissue samples without preconceived biases about where these modified sites occur. For more information on PTMScan®
Proteomics Services, please visit https://www.cellsignal.com/services/index.html.
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. Prominent kinases targeting consensus substrate motifs account for 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. Arg-directed or AGC-family kinases including PKA, PKG, PKC, Akt, p70 S6 kinase, AMPK, and RSK and are characterized by preference for basic amino acids (Lys or Arg) especially Arg at position -3 relative to the phosphorylated Ser or Thr (1,4). Akt, p70S6 kinase and RSK additionally share specificity for Lys or Arg at position -5 (5). CST™ has developed a Basophilic PTMScan®
kit comprising a pool of antibodies that recognize basophilic kinase substrate motifs as a powerful proteomics analysis tool for investigating the regulation of phosphorylation by Arg-directed kinases, as well as for high throughput kinase drug discovery.
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