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XML generation date: 2024-09-20 06:21:38.951
Product last modified at: 2024-09-19T22:12:41.218Z
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PDP - Template Name: FastScan ELISA Kit
PDP - Template ID: *******a26362b
  1. Products /
  2. ELISA Kits /
  3. FastScan™ Phospho-EGF Receptor (Tyr1068) ELISA Kit

FastScan™ Phospho-EGF Receptor (Tyr1068) ELISA Kit #89897

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  • ELISA

    Supporting Data

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

    Product Information

    Product Description

    The FastScan™ Phospho-EGF Receptor (Tyr1068) ELISA Kit is a sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of EGF receptor when phosphorylated at Tyr1068. To perform the assay, sample is incubated with a capture antibody conjugated with a proprietary tag and a second detection antibody linked to HRP, forming a sandwich with phospho-EGF receptor (Tyr1068) in solution. This entire complex is immobilized to the plate via an anti-tag antibody. The wells are then washed to remove unbound material. TMB is then added. The magnitude of observed signal is proportional to the quantity of phospho-EGF receptor (Tyr1068).

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

    Protocol

    Specificity / Sensitivity

    The FastScan™ Phospho-EGF Receptor (Tyr1068) ELISA Kit detects endogenous levels of EGF receptor when phosphorylated at Tyr1068 as shown in Figure 1. 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, Monkey

    Background

    The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation (1,2). Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the active state enzyme, and providing a binding surface for substrate proteins (3,4). c-Src is involved in phosphorylation of EGFR at Tyr845 (5). The SH2 domain of PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling (6). Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide a docking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation (2). Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation (10).

    Database Links

    UniProt ID: P00533


    Entrez-Gene Id: 1956


    Limited Uses

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    For Research Use Only. Not For Use In Diagnostic Procedures.
    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
    FastScan™ ELISA is a registered trademark of Cell Signaling Technology, Inc.
    U.S. Patents 9,086,407, 9,261,500, and 9,476,874, foreign equivalents, and child patents deriving therefrom.
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