PathScan® Phospho-FGF Receptor 3 (panTyr) Chemiluminescent Sandwich ELISA Kit #64740
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Supporting Data
| REACTIVITY | H |
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Description
*Antibodies in this kit are custom formulations specific to kit.
Protocol
Specificity / Sensitivity
PathScan® Phospho-FGF Receptor 3 (panTyr) Chemiluminescent Sandwich ELISA Kit #64740 detects endogenous levels of tyrosine-phosphorylated FGFR3 in human cells. This kit detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species.
Species Reactivity:
Human
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: FGFR1 (flg), FGFR2 (bek, KGFR), FGFR3, and FGFR4. 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 FGFR1 can be phosphorylated: Tyr463, 583, 585, 653, 654, 730, and 766. Tyr653 and Tyr654 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 (FGFR3) are responsible for human skeletal dysplasias including achondroplasia and the neonatal lethal syndromes thanatophoric dysplasia types I and II (6,7). Several of these same FGFR3 mutations as well as overexpression of FGFR3 proteins have also been identified somatically in human cancers, including multiple myeloma, bladder carcinoma and cervical cancer (8). Thus, FGFR3 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.
- Yamashita, A. et al. (2014) Nature 513, 507-11.
- Miyake, M. et al. (2007) Biochem Biophys Res Commun 362, 865-71.
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