PTMScan Phospho-Ser-Pro-Pro Motif [pSPP] Kit

PTMScan^® Technology employs a proprietary methodology 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.

The MAPK and CDK families of serine/threonine protein kinases play important roles in cell signaling and cell cycle control. These kinases phosphorylate threonine or serine followed by a proline residue.

[1] Pearson, R.B. and Kemp, B.E. (1991) Methods Enzymol 200, 62-81.
[2] Seger, R. and Krebs, E.G. (1995) FASEB J 9, 726-35.
[3] Nurse, P. (2000) Cell 100, 71-8.
[4] Cross, T.G. et al. (2000) Exp Cell Res 256, 34-41.
[5] Yang, C.C. et al. (1998) J Protein Chem 17, 329-35.
[6] Reynolds, C.H. et al. (2000) J Neurochem 74, 1587-65.
[7] Shah, O.J. et al. (2003) J Biol Chem 278, 16433-42.
[8] Songyang, Z. et al. (1994) Curr Biol 4, 973-82.
[9] Gonzalez, F.A. et al. (1991) J Biol Chem 266, 22159-63.
[10] Yang, X. and Gabuzda, D. (1998) J Biol Chem 273, 29879-87.