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Render Timestamp: 2024-12-02T11:56:44.689Z
Commit: cd2fae6ca3f811b1ddb1df24ac291ed56d5d501b
XML generation date: 2024-10-29 16:01:07.690
Product last modified at: 2024-11-14T13:00:39.400Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

EGF Receptor (D38B1) XP® Rabbit mAb (Biotinylated) #6627

Filter:
  • WB

    Supporting Data

    REACTIVITY H M Mk
    SENSITIVITY Endogenous
    MW (kDa) 175
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • Mk-Monkey 

    Product Information

    Product Description

    This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as unconjugated EGF Receptor (D38B1) XP® Rabbit mAb #4267.
    MW (kDa) 175

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 136 mM NaCl, 2.6 mM KCI, 12 mM sodium phosphate (pH 7.4) dibasic, 2 mg/ml BSA, and 50% glycerol. Store at –20°C. Do not aliquot the antibodies.

    Protocol

    Specificity / Sensitivity

    EGF Receptor (D38B1) XP® Rabbit mAb (Biotinylated) detects endogenous levels of total EGF receptor protein. The antibody does not cross-react with other proteins of the ErbB family.

    Species Reactivity:

    Human, Mouse, Monkey

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a fusion protein containing the cytoplasmic domain of human EGF receptor protein.

    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.
    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
    XP is a registered trademark of Cell Signaling Technology, Inc.
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