FGF-R2 Cellular Phosphorylation Assay (intracellular kinase activity assay) for compound screening and profiling in intact cells
Fibroblast growth factor receptor 2 (FGF-R2) is a member of the FGFR receptor tyrosine kinase family, which consists of 4 receptors and 23 ligands. Ligand binding leads to FGF-R2 dimerization, autophosphorylation and activation of signaling components including Akt and Erk kinases. FGF-R2 is amplified in 3-10% of primary gastric cancer, resulting in ligand independent receptor activity and cell transformation.
BEK, BFR-1, CD332, CEK3, CFD1, ECT1, JWS, KGFR, KSAM, K-SAM, TK14, TK25
In the human gastric carcinoma cell line Kato-III, DNA-amplification results in overexpression of FGF-R2 which is associated with constitutive, ligand-independent autophosphorylation of this receptor. FGF-R2 activity is potently inhibited in the presence of cognate FGF-R2 inhibitors such as Vargatef (BIBF1120) (see Fig. 1). Phospho-FGF-R2 levels are quantified by Sandwich-ELISA technique.
Substrate phosphorylation as a readout of intracellular kinase activity via ELISA
More information can be found on our website Cellular Phosphorylation Assay Services.
Reference compound IC50 for FGF-R2
Vargatef (BIBF1120) is a potent inhibitor of the phospho-FGF-R2 signal detected in Kato-III cells. Highly reproducible IC50 values were generated in the cellular FGF-R2. The graph shows representative results.