Clone RE688 recognizes the human epidermal growth factor receptor (EGFR) antigen. EGFR is a single-pass type I membrane protein which is also known as receptor tyrosine-protein kinase ErbB-1 or HER1. It is a critical regulator of many normal cellular processes, including cell growth, differentiation, survival, and migration. The EGFR also is implicated in pathological processes of cellular transformation and oncogenesis due to its overexpression in many types of cancers and its ability to induce morphological transformation of cultured cells and tumor formation in nude mice. Many different signaling pathways have been discovered to mediate the effects of EGF, the most notable being Ras-mitogen-activated protein kinase (MAPK) and the phosphatidylinositol 3-kinase pathways. In these pathways EGF binds to the EGFR to induce dimerization, catalytic activation, and autophosphorylation of tyrosines in the C-terminal tail of the EGFR. These phosphorylated tyrosines provide docking sites for adapter proteins such as Grb2, Shc, and Gab2 to link the receptor to the Ras-MAPK, as well as phosphatidylinositol 3-kinase pathways.
Additional information: Clone REA688 displays negligible binding to Fc receptors.