Figure 1. FGF receptor 3 protein is detected at varying levels from multiple cell lines using the PathScan® Total FGF Receptor 3 Sandwich ELISA Kit #15077. The absorbance readings at 450 nm are shown in the top figure, while corresponding western blots using FGF Receptor 3 (C51F2) Rabbit mAb #4574 are shown in the bottom figure.
Figure 2. The relationship between protein concentration of lysates from KMS-11 cells and the absorbance at 450 nm as detected by the PathScan® Total FGF Receptor 3 Sandwich ELISA Kit #15077 is shown. KMS-11 cells (0.5-1.0 x 106 cells/ml) were harvested and then lysed.
The PathScan® Total FGF Receptor 3 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of FGF receptor 3 (FGFR3) protein. An FGFR3 mouse antibody has been coated onto the microwells. After incubation with cell lysates, both phospho- and nonphospho-FGFR3 proteins are captured by the coated antibody. Following extensive washing, an FGFR3 rabbit antibody is added to detect captured FGFR3 proteins. An anti-rabbit IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added for colorimetric detection. The magnitude of absorbance for the developed color is proportional to the quantity of FGFR3 protein.
Antibodies in the kit are custom formulations specific to the kit.
PathScan® Total FGF Receptor 3 Sandwich ELISA Kit detects endogenous levels of FGFR3 protein in human cells, as shown in Figure 1. The kit sensitivity is shown in Figure 2. This kit detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species.
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 (6,8). 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 (7). Thus, FGFR3 may represent a potential target for therapy.
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