The members of epidermal growth factor receptor (EGF R) or the ErbB receptor family have been identified as useful biomarkers and targets for cancer therapy. The EGFR family includes four receptor tyrosine kinases, EGF R (ErbB1), ErbB2 (neu), ErbB3, and ErbB4. EGF R binds EGF and induces tyrosine phosphorylation leading to proliferation of cells. EGF R is present on many cell types of epithelial and mesenchymal lineages. EGF R is capable of binding transforming growth factor-α and heparin-binding EGF in addition to EGF. There are numerous effector molecule activated by EGF R that result in a variety of biological processes such as morphogenesis, cell motility, apoptosis, differentiation and organ repair and maintenance. Deregulation of EGF R signaling is implicated in progression of a wide variety of tumors, invasion and metastasis. Phosphorylation of EGF R at Tyr1148 is required for the binding of protein tyrosine phosphatase, SHP-1, which results in dephosphorylation of EFG R
Anti-phospho-EGFR [pTyr1173] specifically recognizes human EGFR phosphorylated at tyrosine 1173. Cross reactivity may be observed with mouse and rat.

synthetic phosphopeptide derived from the region of EGFR that contains tyrosine 1173.

Anti-phospho-EGFR [pTyr1173] antibody may be used at a working dilution of 1:1000 for immunoblotting using A431 cells.

Solution in Dulbecco′s phosphate buffered saline (without Mg²⁺ and Ca²⁺), pH 7.3, with 50% glycerol, 1.0 mg/ml BSA (IgG, protease free) and 0.05% sodium azide.

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