| Description/Background | EGFR is a 170 kD transmembrane glycoprotein that is part of the ErbB family of receptors within the protein kinase superfamily. EGFR is one 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 is essential for various processes including controlling cell growth and differentiation and ductal development of the mammary glands. Ligand binding induces dimerization and autophosphorylation. It consists of a glycosylated extracellular domain which binds to EGF and an intracellular domain with tyrosine-kinase activity necessary for signal transduction. TGFα, vaccinia virus growth factor, and related growth factors can also bind to and signal through EGFR. Abnormal EGFR signaling has been implicated in inflammatory diseases such as psoriasis, eczema and atherosclerosis. Alzheimer's disease is linked with poor signaling of the EGFR and other receptor tyrosine kinases. Furthermore, over-expression of the EGFR is linked with the growth of various tumors. EGFR has been identified as an oncogene, a gene which in certain circumstances can transform a cell into a tumor cell, which has led to the therapeutic development of anticancer EGFR inhibitors. EGFR is a well-established target for both mAbs and specific tyrosine kinase inhibitors. Anti-Human EGFR (Cetuximab) utilizes the same variable regions from the therapeutic antibody Cetuximab making it ideal for research projects. |
|---|
