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. Recombinant soluble human EGFR is a 621 amino acid glycoprotein comprising the extracellular domain of EGFR, and migrates at an apparent MW of 97.5kDa by SDS-PAGE analysis under reducing conditions. Anti-EGFR Antibody detects endogenous levels of total EGFR protein.
The antiserum was produced against synthesized peptide derived from human EGFR.
Immunogen Range: 651-700
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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Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
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