EGFR vIII Protein, Human (HEK293, His-Avi)

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 vIII Protein, Human (HEK293, His-Avi) is the recombinant human-derived EGFR vIII protein, expressed by HEK293 , with N-Avi, N-His 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

HEK293

N-Avi;N-8*His

NP_001333870 (L25-S378)

1956  [NCBI]

Partial

LEEKKGNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPS

Approximately 68-80 kDa,based on SDS-PAGE under reducing conditions,due to the glycosylation.

≥ 95%, as determined by Bis-Tris PAGE.

<1 EU/μg, determined by LAL method.