Cayman 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.^, 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.^,, Under unstimulated conditions, EGFR is an auto-inhibited monomer in the plasma membrane. 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). 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. Inhibition of EGFR reduces angiotensin II-induced cardiac hypertrophy in mice. 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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