Recombinant human soluble EGF-R 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. Recombinant soluble human EGF-R is a 621 amino acid glycoprotein comprising the extracellular domain of EGF-R, and migrates at an apparent MW of 97.5 kDa by SDS-PAGE analysis under reducing conditions.
Human EGFR expressed in CHO cells
CAT# CSC-CTK0129-10 (10 μg); CAT# CSC-CTK0129-50 (50 μg)
Greater than 95% as determined by SDS-PAGE and RP-HPLC analysis.
Less than 1 EU/μg.
Sterile-filtered through a 0.2 micron filter and lyophilized from 10 mM sodium phosphate buffer (pH 7.5).
Please centrifuge product briefly before opening vial. The lyophilized rHu EGF-R should be reconstituted in sterile, ultra-pure water 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.
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