Product Pathways - Motif Antibodies
PTMScan® Phospho-Thr-Pro Motif (T*P) Immunoaffinity Beads
| Consenus Site | Cell or Tissue Type | Study No. | Modified Peptides Identified |
|---|---|---|---|
| T*P, T*PP | HeLa (human epithelial carcinoma) | 10686, 10689 | 578 PDF XLS |
Services Information
This product is not for individual sale. It is only available as a component of the PTMScan® Proteomics System. PTMScan® Proteomics System orders must be priced out individually. Please email us at ptmscan@cellsignal.com to receive the most accurate pricing.
Description
PTMScan® Immunoaffinity Beads are custom preparations of motif antibodies coupled to protein A beads. They are intended only for use for PTMScan® and are available as components of the PTMScan® Proteomics System.
Specificity / Sensitivity
PTMScan® Phospho-Thr-Pro Motif (T*P) Immunoaffinity Beads detect and capture endogenous levels of peptide derived from protease digested cellular proteins containing phospho-Thr only when followed by Pro. Some preference of Pro at +2 position is observed (e.g., phospho-Elk-1). (U.S. Patent No's.: 6,441,140; 6,982,318; 7,259,022; 7,344,714; U.S.S.N. 11,484,485; and all foreign equivalents.)
Western Blotting
Western blot analysis of extracts from HeLa cells, untreated or nocodazole-treated, using Phospho-Thr-Pro Motif Antibody, the unconjugated antibody corresponding to PTMScan® Phospho-Thr-Pro Motif (T*P) Immunoaffinity Beads.
Background
Proline-directed protein kinases phosphorylate Ser and Thr residues prior to Pro residues. MAP kinases and cyclin dependent kinases (CDKs) belong to this family of kinases. Proline-directed phosphorylation is one of the major regulatory phosphorylation events in many cellular processes such as cell proliferation and differentiation (1-6). More than a quarter of the sites identified in global phosphorylation studies are phosphorylated at pSer-Pro or pThr-Pro sites (7), suggesting proline-directed protein kinases regulate a large number of proteins. Cell Signaling Technology’s pThr-Pro Antibody provides a useful tool to study the substrates of proline-directed kinases.
- Pearson, R.B. and Kemp, B.E. (1991) Methods Enzymol 200, 62-81.
- Seger, R. and Krebs, E.G. (1995) FASEB J 9, 726-35.
- Nurse, P. (2000) Cell 100, 71-8.
- Cross, T.G. et al. (2000) Exp Cell Res 256, 34-41.
- Yang, C.C. et al. (1998) J Protein Chem 17, 329-35.
- Reynolds, C.H. et al. (2000) J Neurochem 74, 1587-95.
- Ubersax, J.A. and Ferrell, J.E. (2007) Nat Rev Mol Cell Biol 8, 530-41.
Application References
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For Research Use Only. Not For Use In Diagnostic Procedures.
