Product Pathways - Motif Antibodies
PTMScan® Phospho-PDK1 Docking Motif (F/YS*/T*F/Y) Immunoaffinity Beads #1992
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
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For Research Use Only. Not For Use In Diagnostic Procedures.