Anti-EGFR Antibody Picoband® Fluoro488 Conjugated

The epidermal growth factor receptor (EGFR; ErbB-1; HER1 in humans) is the cell-surface receptor for members of the epidermal growth factor family (EGF-family) of extracellular protein ligands. It is a member of the ErbB family of receptors, a subfamily of four closely related receptor tyrosine kinases: EGFR (ErbB-1), HER2/c-neu (ErbB-2), Her 3 (ErbB-3) and Her 4 (ErbB-4) . EGFR exists on the cell surface and is activated by binding of its specific ligands, including epidermal growth factor and transforming growth factor α (TGFα) . EGFR and its ligands are cell signaling molecules involved in diverse cellular functions, including cell proliferation, differentiation, motility, and survival, and in tissue development. Mutations that lead to EGFR overexpression (known as upregulation) or overactivity have been associated with a number of cancers, including lung cancer and glioblastoma multiforme. In this latter case a more or less specific mutation of EGFR, called EGFRvIII is often observed.

Cancer, Growth Factors/Hormones, Oncoproteins, Oncoproteins/Suppressors, Protein Phosphorylation, Receptor Tyrosine Kinases, Signal Transduction, Tumor Biomarkers, Tyrosine Kinases

Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, amphiregulin, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS- RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also ly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin. .

1. Herbst RS (2004) . Review of epidermal growth factor receptor biology. Int. J. Radiat. Oncol. Biol. Phys. 59 (2 Suppl) : 21–6. 2. Kuan CT, Wikstrand CJ, Bigner DD (June 2001) . EGF mutant receptor vIII as a molecular target in cancer therapy. Endocr. Relat. Cancer 8 (2) : 83–96. 3. Wang, K.; Yamamoto, H.; Chin, J. R.; Werb, Z.; Vu, T. H.: Epidermal growth factor receptor-deficient mice have delayed primary endochondral ossification because of defective osteoclast recruitment. J. Biol. Chem. 279: 53848-53856, 2004.

Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane ; Single-pass type I membrane protein . Golgi apparatus membrane ; Single-pass type I membrane protein . Nucleus membrane ; Single-pass type I membrane protein . Endosome. Endosome membrane. Nucleus . In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) (By similarity) . .