Anti-EGFRvIII mutation Antibody, clone L8A4 clone L8A4, from mouse

Epidermal growth factor receptor (UniProt: P00533; also known as EC:2.7.10.1, Proto-oncogene c-ErbB-1, Receptor tyrosine-protein kinase erbB-1) is encoded by the EGFR (also known as ERBB, ERBB1, HER1) gene (Gene ID: 1956) in human. EGFR is a single-pass type 1 membrane protein that is ubiquitously expressed. It is synthesized with a 24 amino acids signal peptide that is subsequently cleaved. It contains an extracellular domain (aa 25-645) a transmembrane domain (aa 646-668), and a cytoplasmic domain (aa 669-1210). Upon binding of EGF, the receptor is phosphorylated and recruits adapter proteins to turn on downstream signaling cascades. EGFR is commonly overexpressed and is mutated in many human malignancies and is often associated with aggressive phenotypes. The most common truncated EGFR is the variant III EGFR deletion mutant (EGFRvIII), containing an inframe deletion of exons 2 7 (801 bp) from the extracellular domain. EGFRvIII mutation is reported in about 5% of human lung squamous cell carcinoma (SCC). It has also been suggested that EGFRvIII potentially plays an essential role in the human NSCLC tumor initiation and maintenance. Drugs such as Gefitinib, erlotnib, and HKI-272 are shown to inhibit the growth of EGFRvIII transformed cells and tumor growth. This monoclonal antibody binds specifically to the epidermal growth factor receptor variant III (EGFRvIII), which is present on gliomas, but not normal tissues, and is internalized rapidly after receptor binding. (Ref.: Ji, H., et al. (2006). Proc. Natl. Acad. Sci. USA 103(20); 7817-7822; Hens, M., et al. (2010). Nucl. Med. Biol. 37(7); 741-750).