Cell Signaling Technology

Product Pathways - Tyrosine Kinase/ Adaptors

FGF Receptor 3 Antibody #3160

Applications Reactivity MW (kDa) Source
W H M 145 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse
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 Antibody detects endogenous levels of total FGF receptor 3 protein. This antibody does not cross-react with other FGF receptor family members.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to the sequence surrounding His111 of human FGF receptor 3. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from Kms-11 and BaF3 cells using FGF Receptor 3 Antibody.

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).

FGFR-3 participates in a diverse array of biological processes, including cell growth, differentiation, and migration. Activating mutations in FGFR-3 are associated with multiple myeloma, cervical carcinoma, and bladder cancer and it represents a potential target for therapy (6).

  1. Powers, C.J. et al. (2000) Endocr Relat Cancer 7, 165-97.
  2. Reilly, J.F. et al. (2000) J Biol Chem 275, 7771-8.
  3. Mohammadi, M. et al. (1996) Mol Cell Biol 16, 977-89.
  4. Mohammadi, M. et al. (1991) Mol Cell Biol 11, 5068-78.
  5. Larsson, H. et al. (1999) J Biol Chem 274, 25726-34.
  6. Knowles, M.A. (2008) Future Oncol 4, 71-83.

Application References

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