EGF receptor Recombinant Protein

EGF Receptor (EGFR, ErbB1) is a transmembrane protein that exerts tyrosine kinase activity upon ligand induced activation. EGFR can be activated by binding EGF or at least six other structurally related protein ligands, including TGF, HB-EGF, Betacellulin (BTC), Amphiregulin, Epiregulin, and Epigen. Upon activation, EGFR initiates a signaling cascade which includes dimerization and internalization, tyrosine phosphorylation, DNA synthesis of target genes, and, ultimately, cell proliferation. EGFR signaling plays a role in the growth and differentiation of normal cells, but elevated EGFR activity is correlated with the development and pathogenesis of certain cancers. Recombinant soluble human EGFR is a 621 amino acid glycoprotein comprising the extracellular domain of EGFR, and migrates at an apparent MW of 97.5 kDa by SDS-PAGE analysis under reducing conditions.

The lyophilized EGF receptor recombinant protein is stable for at least 2 years from date of receipt at -20˚ C. Reconstituted EGF receptor is stable for at least 3 months when stored in working aliquots with a carrier protein at -20˚ C. As with any protein, exposing EGF receptor recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.