Render Target: STATIC
Render Timestamp: 2024-12-06T11:07:40.060Z
Commit: 224419269841c11382c4555dbee545259bf6c379
XML generation date: 2024-10-17 15:55:08.101
Product last modified at: 2024-09-19T22:13:09.971Z
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PDP - Template Name: ELISA Kit
PDP - Template ID: *******bd382c2

PathScan® Total FGF Receptor 4 Sandwich ELISA Kit #15078

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  • ELISA

    Supporting Data

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

    Product Information

    Product Description

    The 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.

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

    Protocol

    Specificity / Sensitivity

    PathScan® Total FGF Receptor 4 Sandwich ELISA Kit detects endogenous levels of FGFR4 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.

    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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