Product Pathways - Tyrosine Kinase / Adaptors
FGF Receptor 3 (C51F2) Rabbit mAb #4574
|W IP IHC-P IF-IC||H||Endogenous||165, 145 and 125||Rabbit IgG|
Reactivity Key: H=Human
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
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 animals with a GST-FGFR-3 cytoplasmic domain fusion protein.
Western blot analysis of recombinant human FGFR-3 cytoplasmic fragment proteins (lane 1) and extracts from KMS-11 cells (lane 2) using FGF Receptor 3 (C51F2) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded KMS-11 cells, using FGF Receptor 3 (C51F2) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded small cell lung carcinoma, using FGF Receptor 3 (C51F2) Rabbit mAb.
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 (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.
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For Research Use Only. Not For Use In Diagnostic Procedures.