Cell Signaling Technology

Product Pathways - Tyrosine Kinase / Adaptors

Phospho-Gab2 (Ser159) Antibody #3884

Applications Reactivity Sensitivity MW (kDa) Source
W H M R Endogenous 98 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Phospho-Gab2 (Ser159) Antibody detects endogenous levels of Gab2 only when phosphorylated at serine 159. This antibody does not cross-react with Gab1 or Gab3.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser159 of human Gab2. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from H-4-II-E cells, untreated, HGF-treated, insulin-treated or treated with lambda phosphatase after lysis, using Phospho-GAB2 (Ser159) Antibody.

Background

The Grb-associated binder (Gab) family is a family of adaptor proteins recruited by a wide variety of receptor tyrosine kinases (RTKs) such as EGFR, HGFR, insulin receptor, cytokine receptor and B cell antigen receptors. Upon stimulation of RTKs by their cognate ligand, Gab is recruited to the plasma membrane where it is phosphorylated and functions as a scaffold (1-4). Multiple tyrosine phosphorylation sites of Gab1 protein have been identified (5). Phosphorylation of Tyr472 regulates its binding to p85 PI3 kinase (6,7). Phosphorylation of Gab1 at Tyr307, Tyr373 and Tyr407 modulates its association to PLCγ (8). Phosphorylation of Tyr627 and Tyr659 is required for Gab1 binding to and activation of the protein tyrosine phosphatase SHP2 (6,9).

Akt phosphorylates Gab2 at Ser159. This phosphorylation inhibits Gab2 tyrosine phosphorylation and downstream signal amplification (10).

  1. Holgado-Madruga, M. et al. (1996) Nature 379, 560-564.
  2. Weidner, K.M. et al. (1996) Nature 384, 173-176.
  3. Takahashi-Tezuka, M. et al. (1998) Mol. Cell. Biol. 18, 4109-4117.
  4. Ingham, R.J. et al. (2001) J Biol Chem 276, 12257-65.
  5. Lehr, S. et al. (1999) Biochemistry 38, 151-159.
  6. Rocchi, S. et al. (1998) Mol. Endocrinol. 12, 914-923.
  7. Yu, C.F. et al. (2001) J Biol Chem 276, 32552-8.
  8. Gual, P. et al. (2000) Oncogene 19, 1509-18.
  9. Cunnick, J.M. et al. (2001) J Biol Chem 276, 24380-7.
  10. Lynch, D.K. and Daly, R.J. (2002) EMBO J 21, 72-82.

Application References

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