EGFR Protein, Human (621a.a, HEK293, Llama Fc)

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 (621a.a, HEK293, Llama Fc) is the recombinant human-derived EGFR protein, expressed by HEK293, with C-Llama Fc 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.

This product does not contain protein kinase domain.

Human

HEK293

C-Llama Fc

P00533-1 (L25-S645)

1956

Extracellular Domain

LEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPS

115-150 kDa

≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from 0.22 μm filtered solution of 50 mM Tris, 100 mM Glycine, 25 mM Arginine, 150 mM NaCl, pH7.5 with trehalose as protectant.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.