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EGF Receptor (1F4) Mouse mAb

EGF Receptor (1F4) Mouse mAb #2239

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Supporting Data

REACTIVITY	H
SENSITIVITY	Endogenous
MW (kDa)	175
Source/Isotype	Mouse IgG1

Application Key:

WB-Western Blotting

Species Cross-Reactivity Key:

H-Human

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, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

Protocol

Specificity / Sensitivity

EGF Receptor(1F4) Mouse mAb detects endogenous levels of EGF receptors. It does not cross-react with other Erb family members.

Species Reactivity:

Human

Source / Purification

Monoclonal antibody is produced by immunizing animals with a recombinant protein corresponding to the C-terminal sequence of human EGF receptor.

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

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

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