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 (TGF-α), 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.
Peptide sequence around aa. 691-695 (P-L-T-P-S), according to the protein EGFR.
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.
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Receptor for EGF, but also for other members of the EGF family, as TGF-alpha, amphiregulin, betacellulin, heparin-binding EGF-like growth factor, GP30 and vaccinia virus growth factor. Is involved in the control of cell growth and differentiation.
Solution in phosphate-buffered saline containing 0.02% sodium azide and 50% glycerol