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Human EGFR / HER1 / ErbB1 Protein (His Tag)

ERBB,ERBB1,HER1,mENA,NISBD2,PIG61

Catalog Number P10001-H08H
Organism Species Human
Host Human Cells
Synonyms ERBB,ERBB1,HER1,mENA,NISBD2,PIG61
Molecular Weight The recombinant human EGF receptor consists of 630 amino acids and has a calculated molecular mass of 69.8 kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 110 kDa protein in SDS-PAGE under reducing conditions.
predicted N Leu 25
SDS-PAGE
Purity > 95 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the extracellular domain (Met 1-Ser 645) of human EGFR (NP_005219) was expressed with a C-terminal polyhistidine tag.
Bio-activity Measured by its ability to bind human EGF in a functional ELISA.
Research Area Signaling |Signal Transduction |Protein Phosphorylation |Tyrosine Kinase |Receptor Tyrosine Kinases
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background As a member of the epidermal growth factor receptor (EGFR) family, EGFR protein is type I transmembrane glycoprotein that binds a subset of EGF family ligands including EGF, amphiregulin, TGF-α, betacellulin, etc. EGFR protein plays a crucial role in signaling pathway in the regulation of cell proliferation, survival and differentiation. Binding of a ligand induces EGFR protein homo- or heterodimerization, the subsequent tyrosine autophosphorylation and initiates various down stream pathways (MAPK, PI3K/PKB and STAT). In addition, EGFR signaling also has been shown to exert action on carcinogenesis and disease progression, and thus EGFR protein is proposed as a target for cancer therapy currently.
Reference
  • Schlessinger, J. (2000) Cell signaling by receptor tyrosine kinases. Cell 103(2): 211-25.
  • Giaccone, G. (2005) HER1/EGFR-targeted agents: predicting the future for patients with unpredictable outcomes to therapy. Ann. Oncol. 16(4): 538-48.
  • Yarden, Y., et al. (2001) Untangling the ErbB signalling network. Nat. Rev. Mol. Cell. Biol. 2(2): 127-37.