Cell Signaling Technology

Product Pathways - Tyrosine Kinase / Adaptors

Phospho-FRS2-α (Tyr436) Antibody #3861

Applications Reactivity Sensitivity MW (kDa) Source
W IP H M (R) Endogenous 80 to 85 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
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-FRS2-alpha (Tyr436) Antibody detects endogenous levels of FRS2-alpha only when phosphorylated at tyrosine 436. The antibody does not cross-react with unrelated tyrosine-phosphorylated proteins.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr436 of human FRS2-alpha. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from COS cells cotransfected with human FRS2-alpha and rat TrkA, untreated or NGF-stimulated, using Phospho-FRS2-alpha (Tyr436) Antibody. (Cell lysates provided by Dr. Susan Meakin, Robarts Research Institute, London, Ontario.)

Background

Fibroblast growth factor receptor substrate 2 (FRS2, also called Suc-associated neurotrophic factor-induced tyrosine-phosphorylated target or SNT) participates in the transmission of extracellular signals from the fibroblast growth factor receptor (FGFR). Activation of the FGFR leads to tyrosine phosphorylation of FRS2 (1). Two FRS2 family members have been identified, FRS2-alpha (SNT1) and FRS2-beta (SNT2) (2), which are phosphorylated by these RTKs. Once they are phosphorylated, they recruit SH2 domain-containing proteins including Grb2 and SHP-2 (3,4), mediating downstream signaling. Tyr436 is required for efficient SHP-2 recruitment (5), whereas Tyr196 functions as a docking site for Grb2-Sos complexes (6).

  1. Kouhara, H. et al. (1997) Cell 89, 693-702.
  2. Ong, S. H. et al. (2000) Mol. Cell. Biol. 20, 979-989.
  3. Kontaridis, M. I. et al. (2002) Mol. Cell. Biol. 22, 3875-3891.
  4. Xu, H. and Goldfarb, M. (2001) J. Biol. Chem. 276, 13049-13056.
  5. Hadari, Y. R. et al. (1998) Mol. Cell. Biol. 18, 3966-3973.
  6. Kouhara, M. et al. (1997) Cell 89, 693-702.

Application References

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