Human EGFR, soluble

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Size25 µg
Price370 €
SourceInsect cells
Purity Confirmation~ 90% by SDS-PAGE
Length [aa]629
Molecular Weight~ 85.0 kDa
Biological ActivityMeasured by its ability to bind to immobilized recombinant human EGF in a functional ELISA.
Species ReactivityHuman
ReconstitutionThe lyophilized sEGFR is soluble in water and most aqueous buffers. The lyophilized sEGFR should be reconstituted in water or PBS to a concentration of not lower than 50µg/ml.
Stability and StorageLyophilized samples are stable for greater than six months at -20°C to -70°C. Reconstituted sEGFR should be stored in working aliquots at -20°C. Avoid repeated freeze-thaw cycles!
SynonymsEGF receptor; EGFR; ERBB; HER1; mENA; ERBB1; PIG61
DescriptionRecombinant human soluble EGFR is produced as a glycosylated monomeric protein with a mass of approximately 70 kDa in insect cells. The epidermal growth factor receptor (EGFR) subfamily of receptor tyrosine kinases comprises four members: EGFR (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGFR gene encodes a 1210 amino acid (aa) residue precursor with a 24aa putative signal peptide, a 621aa extracellular domain, a 23aa transmembrane domain, and a 542aa cytoplasmic domain. EGFR has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGFR homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGFR signaling has also been shown to play a role in carcinogenesis.
Uniprot IDP00533
Protein RefSeqNP_005219
mRNA RefSeqNM_005228


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