Product Pathways - Tyrosine Kinase/ Adaptors
FGF Receptor 3 (C51F2) Rabbit mAb #4574
| Applications | Reactivity | MW (kDa) | Source | Isotype |
|---|---|---|---|---|
| W IP | H | 165, 145 and 125 | Rabbit | IgG |
Applications Key:
W=Western Blotting
IP=Immunoprecipitation
Reactivity Key:
H=Human
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.
Specificity / Sensitivity
FGF Receptor 3 (C51F2) Rabbit mAb detects endogenous levels of FGF Receptor 3 protein. This antibody does not cross-react with other related family members.
Source / Purification
Monoclonal antibody is produced by immunizing rabbits with a GST-FGFR-3 cytoplasmic domain fusion protein.
Background
Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through cell surface receptor tyrosine kinases. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane domain and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosines 653 and 654 are important for catalytic activity of activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCγ (4,5).
Activating mutations within fibroblast growth factor receptor 3 (FGFR-3) are responsible for human skeletal dysplasias including achondroplasia and the neonatal lethal syndromes thanatophoric dysplasia types I and II (6). Several of these same FGFR-3 mutations as well as overexpression of FGFR-3 proteins have also been identified somatically in human cancers, including multiple myeloma, bladder carcinoma and cervical cancer (7). Thus, FGFR-3 may represent a potential target for therapy.
- Powers, C.J. et al. (2000) Endocr Relat Cancer 7, 165-97.
- Reilly, J.F. et al. (2000) J Biol Chem 275, 7771-8.
- Mohammadi, M. et al. (1996) Mol Cell Biol 16, 977-89.
- Mohammadi, M. et al. (1991) Mol Cell Biol 11, 5068-78.
- Larsson, H. et al. (1999) J Biol Chem 274, 25726-34.
- Wilkie, A.O. et al. (2002) Am J Med Genet 112, 266-78.
- Miyake, M. et al. (2007) Biochem Biophys Res Commun 362, 865-71.
Application References
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