Anti-EGFR [Matuzumab], Mouse IgG1

This antibody binds the extracellular domain III of the human EGFR and does not cross react with murine EGFR. It was also reported that residues S460/G461 in EGFR domain III are essential components of the epitope. This antibody binds at a site distinct from the EGF binding site, preventing conformational re-arrangement required for dimerization, a process essential for high-affinitiy ligand binding (Schmiedel, 2008). This antibody can only recognize the active form of EGFR. The antibody binds to both glyco- and aglyco receptor forms. EGFR is a transmembrane mitogenic glycoprotein with a cytoplasmically facing tyrosine kinase site which is activated by binding of the epidermal growth factor in the external domain. It also binds transforming growth factor alpha (TGFa). EGFR a member of the epidermal growth factor family and is closely related to receptor tyrosine kinases. This receptor tyrosine kinase binds ligands of the EGF family and activates signallying cascades to convert extracellular cues into appropriate cellular responses. Mutations that lead to EGFR overexpression (known as upregulation) or overactivity have been associated with a number of cancers, including lung cancer, anal cancers and glioblastoma multiforme as well as inflammatory diseases.

[epidermal growth factor receptor isoform a; Epidermal growth factor receptor; epidermal growth factor receptor; proto-oncogene c-ErbB-1; cell growth inhibiting protein 40; cell proliferation-inducing protein 61; receptor tyrosine-protein kinase erbB-1; avian erythroblastic leukemia viral (v-erb-b) oncogene homolog; epidermal growth factor receptor; Proto-oncogene c-ErbB-1; Receptor tyrosine-protein kinase erbB-1]