Epidermal Growth Factor Receptor Receptor (EGFR) Antibody – Mouse Monoclonal

The protein encoded by this gene is a transmembrane glycoprotein that is a member of the protein kinase superfamily. This protein is a receptor for members of the epidermal growth factor family. EGFR is a cell surface protein that binds to epidermal growth factor. Binding of the protein to a ligand induces receptor dimerization and tyrosine autophosphorylation and leads to cell proliferation. Mutations in this gene are associated with lung cancer. Multiple alternatively spliced transcript variants that encode different protein isoforms have been found for this gene. [provided by RefSeq]

EGFR: a receptor tyrosine kinase. This is a receptor for epidermal growth factor (EGF) and related growth factors including TGF-alpha, amphiregulin, betacellulin, heparin-binding EGF-like growth factor, GP30, and vaccinia virus growth factor. EGFR is involved in the control of cell growth and differentiation. It is a single-pass transmembrane tyrosine kinase. Ligand binding to this receptor results in receptor dimerization, autophosphorylation (in trans), activation of various downstream signaling molecules and lysosomal degradation. It can be phosphorylated and activated by Src. Activated EGFR binds the SH2 domain of phospholipase C-gamma (PLC-gamma), activating PLC-gamma-mediated downstream signaling. Phosphorylated EGFR binds Cbl, leading to its ubiquitination and degradation. Grb2 and SHC bind to phospho-EGFR and are involved in the activation of MAP kinase signaling pathways. Phosphorylation on Ser and Thr residues is thought to represent a mechanism for attenuation of EGFR kinase activity. EGFR is overexpressed in breast, head and neck cancers, correlating with poor survival. Activating somatic mutations are seen in lung cancer, corresponding to the minority of patients with strong responses to the EGFR inhibitor Iressa (gefitinib). Mutations and amplifications are also seen in glioblastoma, and upregulation is seen in colon cancer and neoplasms. In xenografts, inhibitors synergize with cytotoxic drugs in the inhibition of many tumor types. Inhibitors include: Iressa/ZD1839, Erbitux, Tarceva, and lapatinib. Four alternatively spliced isoforms have been described.

Protein type: Kinase, protein; EC 2.7.10.1; Tumor suppressor; Protein kinase, tyrosine (receptor); Protein kinase, TK; Membrane protein, integral; TK group; EGFR family

Chromosomal Location of Human Ortholog: 7p12

Cellular Component: extracellular space; endoplasmic reticulum membrane; nuclear membrane; focal adhesion; cell surface; basolateral plasma membrane; integral to membrane; lipid raft; Golgi membrane; membrane; perinuclear region of cytoplasm; apical plasma membrane; cytoplasm; plasma membrane; AP-2 adaptor complex; endosome membrane; nucleus; receptor complex; endosome

Molecular Function: identical protein binding; epidermal growth factor receptor activity; epidermal growth factor binding; nitric-oxide synthase regulator activity; receptor signaling protein tyrosine kinase activity; transmembrane receptor protein tyrosine kinase activity; protein phosphatase binding; protein kinase binding; integrin binding; actin filament binding; protein binding; transmembrane receptor activity; enzyme binding; MAP kinase kinase kinase activity; protein heterodimerization activity; protein-tyrosine kinase activity; ubiquitin protein ligase binding; double-stranded DNA binding; chromatin binding; glycoprotein binding; ATP binding

Biological Process: circadian rhythm; diterpenoid metabolic process; positive regulation of nitric oxide biosynthetic process; activation of MAPKK activity; nerve growth factor receptor signaling pathway; alkanesulfonate metabolic process; protein insertion into membrane; positive regulation of vasodilation; G1/S-specific positive regulation of cyclin-dependent protein kinase activity; positive regulation of MAP kinase activity; cell-cell adhesion; positive regulation of fibroblast proliferation; ovulation cycle; cell surface receptor linked signal transduction; hair follicle development; positive regulation of superoxide release; negative regulation of mitotic cell cycle; positive regulation of DNA repair; fibroblast growth factor receptor signaling pathway; digestive tract morphogenesis; response to osmotic stress; phospholipase C activation; hydrogen peroxide metabolic process; response to hydroxyisoflavone; positive regulation of transcription from RNA polymerase II promoter; response to oxidative stress; regulation of nitric-oxide synthase activity; negative regulation of protein catabolic process; response to calcium ion; positive regulation of epithelial cell proliferation; negative regulation of apoptosis; negative regulation of epidermal growth factor receptor signaling pathway; tongue development; axon guidance; embryonic placenta development; peptidyl-tyrosine phosphorylation; translation; positive regulation of smooth muscle cell proliferation; protein amino acid autophosphorylation; signal transduction; positive regulation of synaptic transmission, glutamatergic; learning and/or memory; positive regulation of cell proliferation; salivary gland morphogenesis; response to stress; regulation of peptidyl-tyrosine phosphorylation; epidermal growth factor receptor signaling pathway; ossification; phosphoinositide-mediated signaling; MAPKKK cascade; liver development; positive regulation of protein kinase B signaling cascade; cell proliferation; cerebral cortex cell migration; positive regulation of vasoconstriction; calcium-dependent phospholipase A2 activation; innate immune response; positive regulation of protein amino acid phosphorylation; astrocyte activation; response to cobalamin; positive regulation of DNA replication; positive regulation of phosphorylation; lung development; positive regulation of inflammatory response; positive regulation of cell migration

Disease: Lung Cancer