Render Target: STATIC
Render Timestamp: 2024-12-13T10:49:53.802Z
Commit: 611277b6de3cd1bb065350b6ef8d63df412b7185
XML generation date: 2024-09-20 06:14:10.644
Product last modified at: 2024-06-27T13:36:07.927Z
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PDP - Template Name: Blocking Peptide
PDP - Template ID: *******6db2f4c

Phospho-EGF Receptor (Tyr1068) Blocking Peptide #1110

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Important Ordering Details

Custom Ordering Details: This product is assembled upon order. Please allow two-four weeks for your product to be processed.

    Product Information

    Product Usage Information

    Use as a blocking reagent to evaluate the specificity of antibody reactivity in dot blot protocols.

    Storage

    Supplied in 20 mM potassium phosphate (pH 7.0), 50 mM NaCl, 0.1 mM EDTA, 1 mg/ml BSA, 5% glycerol and 1% DMSO. Store at –20°C.

    Product Description

    This peptide is used to block Phospho-EGF Receptor (Tyr1068) Antibody #2234 reactivity.

    Quality Control

    The quality of the peptide was evaluated by reversed-phase HPLC and by mass spectrometry. The peptide reacts with Phospho-EGF Receptor (Tyr1068) Antibody #2234 in dot blot.

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