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PDP - Template Name: ELISA Kit
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PathScan® Phospho-FGFR2 (panTyr) Sandwich ELISA Kit #7954

Important Ordering Details

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    Supporting Data

    REACTIVITY H
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Description

    The PathScan® Phospho-FGFR2 (panTyr) Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of tyrosine-phosphorylated FGFR2 protein. An FGFR2 rabbit antibody has been coated on the microwells. After incubation with cell lysates, FGFR2 protein (phospho and nonphospho) is captured by the coated antibody. Following extensive washing, a phospho-tyrosine mouse detection antibody is added to detect captured tyrosine-phosphorylated FGFR2 protein. 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 the absorbance for this developed color is proportional to the quantity of tyrosine-phosphorylated FGFR2 protein.

    *Antibodies in this kit are custom formulations specific to kit.

    Protocol

    Specificity / Sensitivity

    PathScan® Phospho-FGFR2 (panTyr) Sandwich ELISA Kit #7954 detects endogenous levels of FGFR2 protein phosphorylated at Tyr residues 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.


    Species Reactivity:

    Human

    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: 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).

    For Research Use Only. Not For Use In Diagnostic Procedures.
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