EGFR Protein, Human (C797S, T790M, L858R, sf9, GST)

The EGFR protein is a receptor tyrosine kinase that can bind to a variety of ligands, such as EGF, TGFA, AREG, epigen, BTC, epiregulin, and HBEGF, to initiate signaling cascades that mediate cellular responses. This involves receptor dimerization, autophosphorylation and recruitment of adapter proteins such as GRB2, activating downstream pathways such as RAS-RAF-MEK-ERK, PI3-kinase-AKT, PLCgamma-PKC and STAT. EGFR Protein, Human (C797S, T790M, L858R, sf9, GST) is the recombinant human-derived EGFR, expressed by Sf9 insect cells , with N-GST labeled tag. ,

The EGFR protein, a receptor tyrosine kinase, binds ligands of the EGF family, including EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG, and HBEGF/heparin-binding EGF. This interaction initiates cascades that convert extracellular signals into cellular responses, involving receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2, activating downstream signaling cascades, including RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC, and STATs modules. Additionally, EGFR may trigger the NF-kappa-B signaling cascade and directly phosphorylate proteins like RGS16, activating its GTPase activity, potentially linking EGF receptor signaling to G protein-coupled receptor signaling. Furthermore, EGFR phosphorylates MUC1, enhancing its interaction with SRC and CTNNB1/beta-catenin. It positively regulates cell migration through interaction with CCDC88A/GIV, retaining EGFR at the cell membrane post-ligand stimulation, thereby promoting EGFR signaling and triggering cell migration. Beyond its canonical functions, EGFR contributes to enhancing learning and memory performance and plays a role in mammalian pain signaling, with isoform 2 potentially acting as an antagonist to EGF action.

Human

Sf9 insect cells

N-GST

P00533-1 (M668-A1210, C797S, T790M, L858R)

1956

87.9 KDa

Greater than 85 % as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.