Recombinant Human EGFR (C-6His)

SKU: EPT097

Size:10ug

Description:Recombinant Human Epidermal Growth Factor Receptor is produced by our Mammalian expression system and the target gene encoding Leu25-Ser645 is expressed with a 6His tag at the C-terminus.

Accession:P00533

Molecular weight:69.6 KDa

Apparent molecular weight:90-120 KDa, reducing conditions

Other names:Epidermal growth factor receptor; Proto-oncogene c-ErbB-1; Receptor tyrosine-protein kinase erbB-1; EGFR;ERBB; ERBB1; HER1

Storage condition:Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.

Purity:Greater than 95% as determined by reducing SDS-PAGE.

Endotoxin:Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.

Biological activity:

Redissolve:Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

Storage:Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.

Delivery condition:The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.

Background:The EGFR subfamily of receptor tyrosine kinases is composed of EGFR, ErbB2, ErbB3 and ErbB4. The EGFR shares 43% - 44% aa sequence identity with the ECD of human EGFR subfamily. All these family members are type I transmembrane glycoproteins with an extracellular ligand binding domain. The extracellular ligand binding domain is containing two cysteine-rich domains separated by a spacer region and a cytoplasmic domain containing a membrane-proximal tyrosine kinase domain. Ligand binding could induce EGFR homodimerization and heterodimerization with ErbB2, resulting in cell signaling, heterodimerization tyrosine phosphorylation and kinase activation. It can bind EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, HB-EGF, epigen, and so on. Its signaling regulates multiple biological functions including cell proliferation, differentiation, motility, and apoptosis. EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR is overexpressed in different tumors. Several anti-cancer drugs use EGFR as target.