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Epidermal growth factor receptor (EGFR), also known as HER1 and ErbB1, is a cell surface receptor and member of the EGF family of receptor tyrosine kinases with roles in cell proliferation, differentiation, and survival.1,2 It is a 170 kDa transmembrane receptor composed of an intracellular tyrosine kinase domain, a transmembrane lipophilic segment, and an extracellular domain that is expressed in epithelial, mesenchymal, and neuronal tissues.1,2,3 Under unstimulated conditions, EGFR is an auto-inhibited monomer in the plasma membrane.1 Upon canonical ligand binding, EGFR undergoes homodimerization or heterodimerization with HER2, HER3, or HER4, which induces a conformational change in the cytoplasmic domain that facilitates autophosphorylation and intracellular signaling. The exon 19 in-frame deletion mutant EGFRL858R is found, often in conjunction with additional EGFR mutations, in non-small cell lung cancers (NSCLC) and is associated with increased susceptibility to tyrosine kinase inhibition and cell death.4,5 Cayman’s EGFRL858R Rabbit Monoclonal Antibody (RM380) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.
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1. Emerging functions of the EGFR in cancer. Mol. Oncol. 12(1), 3-20 (2018).
2. Review of epidermal growth factor receptor biology. Int. J. Radiat. Oncol. Biol. Phys. 59(2 Suppl), 21-26 (2004).
3. Distribution and function of EGFR in human tissue and the effect of EGFR tyrosine kinase inhibition. Anticancer Res. 23(5A), 3639-3650 (2003).
4. Overcoming EGFR(T790M) and EGFR(C797S) resistance with mutant-
5. Compound EGFR mutations and response to EGFR tyrosine kinase inhibitors. J. Thorac. Oncol. 8(1), 45-51 (2013).