Recombinant 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 (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (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 EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-á , betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a coreceptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.
Human EGFR expressed in E.coli
CAT# CSC-CTK0128-25 (25 μg); CAT# CSC-CTK0128-125 (125 μg)
Greater than 90% as determined by SDS-PAGE analysis.
Recombinant human EGF is fully biologically active when compared to standards. The ED50, as calculated by the dose-dependent proliferation of murine BALB/c 3T3 cells (measured by 3H- thymidine uptake), is ≤ 0.1 ng/ml corresponding to a specific activity of Greater than 1 x 10^7 units/mg.
Less than 1 EU/μg.
Sterile filtered and lyophilized protein from a protein solution in PBS buffer (pH 7.4).
Please centrifuge product briefly before opening vial. The lyophilized rHu EGF-R should be reconstituted in sterile, ultra-pure water or PBS to a concentration of 0.1-1.0 mg/ml. This solution can then be diluted into other aqueous buffers and stored at -20°C for future use.
Storage & Stability
The lyophilized powder, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted rHu EGF-R should be stored long-term in undiluted working aliquots at -20°C. For long-term storage, it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze / thaw cycles.
If you use this products in your scientific publication, it should be cited in the publication as: Creative Bioarray cat no. If your paper has been published, please click here to submit the Pub Med ID of your paper to get a coupon.