Epidermal growth factor receptor (EGFR, ErbB1) is a transmembrane protein that exerts tyrosine kinase activity upon ligand induced activation. EGFR can be activated by binding EGF or at least six other structurally related protein ligands, including transforming growth factor α (TGFα), heparin-binding EGF-like growth factor (HB-EGF), betacellulin (BTC), amphiregulin, epiregulin and epigen. The gene encoding it is localized on human chromosome 7p11.2.
Immunogen
The epitope recognized by PLA0101 maps to a region between residue 1150 and the C-terminus (residue 1210) of human Epidermal Growth Factor Receptor using the numbering given in Swiss-Prot entry P00533 (GeneID 1956).
Biochem/physiol Actions
Upon activation by ligands, epidermal growth factor receptor (EGFR, ErbB1) initiates a signaling cascade which includes dimerization and internalization, tyrosine phosphorylation, DNA synthesis of target genes, and, ultimately, cell proliferation. EGFR signaling plays a role in the growth and differentiation of normal cells, but elevated EGFR activity is correlated with the development and pathogenesis of certain cancers.
Physical form
Tris-citrate/phosphate buffer, pH 7 to 8 containing 0.09% Sodium Azide
Other Notes
The epidermal growth factor receptor (EGFR) is a membrane spanning tyrosine kinase receptor for epidermal growth factor (EGF) and other ligands of the EGF family such as TGF-alpha, amphiregulin, betacellulin, epiregulin and heparin-binding EGF-like growth factor. Upon ligand binding, the EGFR homodimerizes or heterodimerizes with other ErbB receptor family members and tranduces a downstream signal via the ras-raf-mitogen activated protein kinase pathway or the phosphatidylinositol 3-kinase (PI3K)/Akt pathway. Signals from the EGFR function to influence cell proliferation, differentiation, and development.
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