Product Pathways - Tyrosine Kinase / Adaptors
Phospho-FGF Receptor (Tyr653/654) (55H2) Mouse mAb #3476
PhosphoSitePlus® protein, site, and accession data: FGFR1
| Applications | Reactivity | Sensitivity | MW (kDa) | Isotype |
|---|---|---|---|---|
| W | H (M) (R) | Transfected Only | 120 to 145 | Mouse IgG2b |
Applications Key:
W=Western Blotting
Reactivity Key:
H=Human
M=Mouse
R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Protocols
- 3476:
- Western Blotting
Specificity / Sensitivity
Phospho-FGF Receptor (Tyr653/654) (55H2) Mouse mAb detects transfected levels of FGF receptors only when phosphorylated at tyrosines 653/654. The antibody cross-reacts slightly with activated PDGF and insulin/IGF-I receptors.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr653/654 of human FGF receptor-1. The corresponding sequence is identical in FGF receptor-2, -3 and -4.
Western Blotting
Western blot analysis of extracts from COS cells overexpressing human FGF receptor-1, untreated or calf intestine phosphatase (CIP)-treated, using Phospho-FGF Receptor (Tyr653/654) (55H2) Mouse mAb. Overexpression of human FGF receptor-1 results in constitutive activation of the receptors (courtesy of Dr. Pamela Maher, Scripps Research Institute, California, personal communication). CIP treatment abolishes the reactivity of this antibody to FGF receptor-1.
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, 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).
- 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.
Application References
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This product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.