EGFR Extracellular Domain (human, recombinant)

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. EGFR inhibits autophagy under nutrient-rich growth conditions and, conversely, induces autophagy under serum-starved conditions by interacting with the autophagy inhibitor Rubicon to induce its dissociation from Beclin-1. Overexpression of EGFR is found in multiple solid tumors, including renal, breast, ovarian, and head and neck cancer, as well as non-small cell lung cancer (NSCLC).² EGFR^L858R is associated with increased susceptibility to tyrosine kinase inhibition and cell death, while EGFR^T790M is associated with kinase inhibitor resistance in NSCLC.⁴ Inhibition of EGFR reduces angiotensin II-induced cardiac hypertrophy in mice.⁵ Cayman’s EGFR Extracellular Domain (human, recombinant) protein can be used for ELISA. This protein is a disulfide-linked homodimer. The reduced monomer, comprised of the EGFR extracellular domain (amino acids 25-645) fused to human IgG1 Fc at its C-terminus, consists of 860 amino acids and has a calculated molecular weight of 95 kDa, and a predicted N-terminus of Leu25 after signal peptide cleavage. As a result of glycosylation, the monomer migrates at approximately 130 to 140 kDa by SDS-PAGE under reducing conditions.

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1. Sigismund, S., Avanzato, D., and Lanzetti, L. Emerging functions of the EGFR in cancer. Mol. Oncol. 12(1), 3-20 (2018).

2. Herbst, R.S. Review of epidermal growth factor receptor biology. Int. J. Radiat. Oncol. Biol. Phys. 59(2 Suppl), 21-26 (2004).

3. Yano, S., Kondo, K., Yamaguchi, M., et al. Distribution and function of EGFR in human tissue and the effect of EGFR tyrosine kinase inhibition. Anticancer Res. 23(5A), 3639-3650 (2003).

4. Jia, Y., Yun, C.H., Park, E., et al. Overcoming EGFR(T790M) and EGFR(C797S) resistance with mutant-selective allosteric inhibitors. Nature 534(7605), 129-132 (2016).

5. Peng, K., Tian, X., Qian, Y., et al. Novel EGFR inhibitors attenuate cardiac hypertrophy induced by angiotensin II. J. Cell. Mol. Med. 20(3), 482-494 (2016).