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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
Western Blotting Image 1: EGF Receptor (D38B1) XP® Rabbit mAb (Biotinylated)
Western blot analysis of extracts from HeLa and A-431 cells using EGF Receptor (D38B1) XP® Rabbit mAb (Biotinylated) and developed using Streptavidin-HRP #3999.

To Purchase # 6627

Cat. # Size Qty. Price Ships
6627S 100 µl
$450

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).

Pathways

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