Phospho-FRS2-α (Tyr436) Antibody #3861
- WB
Supporting Data
| REACTIVITY | H M |
| SENSITIVITY | Endogenous |
| MW (kDa) | 80 to 85 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
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.
Species Reactivity:
Human, Mouse
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Rat
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.
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). FGFR activation leads to tyrosine phosphorylation of FRS2 (1). Two FRS2 family members have been identified, FRS2-α (SNT1) and FRS2-β (SNT2) (2), which are phosphorylated by these receptor tyrosine kinases (RTKs). Once 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).
- Kouhara, H. et al. (1997) Cell 89, 693-702.
- Ong, S. H. et al. (2000) Mol. Cell. Biol. 20, 979-989.
- Kontaridis, M. I. et al. (2002) Mol. Cell. Biol. 22, 3875-3891.
- Xu, H. and Goldfarb, M. (2001) J. Biol. Chem. 276, 13049-13056.
- Hadari, Y. R. et al. (1998) Mol. Cell. Biol. 18, 3966-3973.
- Kouhara, M. et al. (1997) Cell 89, 693-702.
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