Target Synonym: PIG;HER;Proto-oncogene c-ErbB;Receptortyrosine-protein kinase erbB;Receptor tyrosine-protein kinase erbB;NISBD;EGFR;ERBB;ERBB1;HER1;NISBD2;PIG61;mENA;ErbB-1;Receptortyrosine-protein kinase erbB-1;Epidermal growth factor receptor;Proto-oncogene c-ErbB-1;Receptor tyrosine-protein kinase erbB-1; NISBD2;epidermal growth factor receptor;ERBB;ERBB1;HER1;mENA;NISBD2;PIG61;Avian erythroblastic leukemia viral (v erb b) oncogene homolog;Cell growth inhibiting protein 40;Cell proliferation inducing protein 61;EGF R;Epidermal growth factor receptor (avian erythroblastic leukemia viral (v erb b) oncogene homolog);Epidermal growth factor receptor (erythroblastic leukemia viral (v erb b) oncogene homolog avian);ErbB1;ERBB;erb-b2 receptor tyrosine kinase 1;Errp;Oncogen ERBB;Receptor tyrosine protein kinase ErbB 1;SA7;Species antigen 7;Urogastrone;v-erb-b Avian erythroblastic leukemia viral oncogen homolog;wa2;Wa5
Background: The epidermal growth factor receptor (EGFR) subfamily of receptor tyrosine kinases comprises four members: EGFR (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER2), ErbB3 (HER3), and ErbB4 (HER4). All family members are type I transmembrane glycoproteins that have an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGFR gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGFR has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 alpha in the absence of a co-receptor. Ligand binding induces EGFR homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGFR signaling has also been shown to play a role in carcinogenesis.
Immunogen: A synthetic phosphopeptide corresponding to residues around Tyr845 of the Human Phospho-EGF Receptor
Buffer: 10 mM sodium HEPES, 150 mM NaCl, 100 μg/mL protein protectant, 50% glycerol, pH 7.5
Dilution: WB 1:1000-1:10000
Calculated MW: 134 kDa
Observed MW: 200 kDa
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