Product Pathways - Motif Antibodies
PTMScan® Phospho-PDK1 Docking Motif (F/YS*/T*F/Y) Immunoaffinity Beads
| Consenus Site | Cell or Tissue Type | Study No. | Modified Peptides Identified |
|---|---|---|---|
| (F/K)XX(F/Y)(S*/T*)(F/Y) | Mouse brain | 3121 | 424 |
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-PDK1 Docking Motif (F/YS*/T*F/Y) Immunoaffinity Beads detect and capture endogenous levels of peptide derived from protease digested cellular proteins containing phosphorylated Ser or Thr that is surrounded by Tyr or phenylalanine at the -1 and +1 positions. (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 Jurkat cells, untreated or treated with calyculin A, using Phospho-(Ser/Thr) PDK1 Docking Motif (18A2) Mouse mAb, the unconjugated antibody corresponding to PTMScan® Phospho-PDK1 Docking Motif (F/YS*/T*F/Y) Immunoaffinity Beads.
Background
Many critical protein kinases can be regulated by phosphorylation at a specific serine or threonine in a hydrophobic motif (1). For example, Akt, an important kinase that regulates cell survival, is activated by phosphorylation at Ser473, a site preceded by phenylalanine at -4 and -1 and followed by tyrosine at +1 (2). RSK2, p70 S6 K and certain PKC isoforms also contain a similar consensus phosphorylation motif. Phosphorylation of these motifs is required for binding to 3-phosphoinositide-dependent kinase 1 (PDK1) (3-5). This antibody is a powerful new tool for the characterization of phosphorylated PDK1 docking motifs and the identification of new proteins with PDK1 docking motifs.
- Vanhaesebroeck, B. and Alessi, D.R. (2000) Biochem. J. 346, 561-576.
- Alessi, D. R. et al. (1996) EMBO J. 15, 6541-6551.
- Frodin, M. et al. (2000) EMBO J. 19, 2924-2934.
- Balendran, A. et al. (1999) J. Biol. Chem. 274, 37400-37406.
- Balendran, A. et al. (2000) J. Biol. Chem. 275, 20806-20813.
Application References
Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!
For Research Use Only. Not For Use In Diagnostic Procedures.
