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Product last modified at: 2025-01-01T09:08:14.147Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-EGF Receptor (Ser1046/1047) Antibody #2238

Filter:
  • WB
Western Blotting Image 1: Phospho-EGF Receptor (Ser1046/1047) Antibody
Western blot analysis of extracts from A431 cells, untreated or stimulated with EGF (100 ng/ml, 10 min), using Phospho-EGF Receptor (Ser1046/1047) Antibody (upper) or EGF Antibody #2232 (lower). Calf intestinal phosphatase (CIP) treatment abolished the immunoreactivity of Phospho-EGF Receptor (Ser1046/1047) Antibody with EGF-stimulated A431 cell lysates (middle).

To Purchase # 2238

Cat. # Size Qty. Price
2238S 100 µl
$357

Supporting Data

REACTIVITY H M R
SENSITIVITY Endogenous
MW (kDa) 175
SOURCE Rabbit
Application Key:
  • WB-Western Blotting 
Species Cross-Reactivity Key:
  • H-Human 
  • M-Mouse 
  • R-Rat 
  • Related Products

Product Information

Product Usage Information

Application Dilution
Western Blotting 1:1000

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

Protocol

Specificity / Sensitivity

Phospho-EGF Receptor (Ser1046/1047) Antibody detects endogenous levels of EGF receptors only when phosphorylated at Ser1046/1047. This antibody may cross-react with other activated EGF receptor family members (e.g. ErbB2).

Species Reactivity:

Human, Mouse, Rat

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser1046/1047 of human EGF receptor. Antibodies are purified by protein A and peptide affinity chromatography.

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).

Pathways

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