PathScanTotalFGFReceptor 4Sandwich ELISA Kit

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Company Name: Cell Signaling Technology Inc  
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PathScanTotalFGFReceptor 4Sandwich ELISA Kit Basic information
Description Reactivity Background References
Product Name:PathScanTotalFGFReceptor 4Sandwich ELISA Kit
Synonyms:PathScanTotalFGFReceptor 4Sandwich ELISA Kit
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PathScanTotalFGFReceptor 4Sandwich ELISA Kit Structure
PathScanTotalFGFReceptor 4Sandwich ELISA Kit Chemical Properties
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PathScanTotalFGFReceptor 4Sandwich ELISA Kit Usage And Synthesis
DescriptionThe PathScan® Total FGF Receptor 4 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of FGFR4 protein. An FGFR4 rabbit mAb has been coated onto the microwells. After incubation with cell lysates, both phospho- and nonphospho-FGFR4 proteins are captured by the coated antibody. Following extensive washing, an FGFR4 mouse detection mAb is added to detect captured FGFR4 proteins. Anti-mouse IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of absorbance for the developed color is proportional to the quantity of FGFR4 protein.
ReactivityHuman
BackgroundFibroblast growth factors 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, FGFR2, FGFR3, and FGFR4. Each receptor contains an extracellular ligand-binding domain, a transmembrane domain, and a cytoplasmic kinase domain. Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues. 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. The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components, such as Crk and PLCγ.
References[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.
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