ED50 <0.6 ng/mL, measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblasts in serum-free medium and CellTiter-Glo cell viability assay, corresponding to a specific activity of >1.7 x 10^6 units/mg. AA 971-1023, expressed with an N-terminal Met
EGF
Origine: Humain
Hôte: Escherichia coli (E. coli)
> 95 % as determined by (a) Analysis by SEC-HPLC (b) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel
Active
EGF
Origine: Souris
Hôte: HEK-293 Cells
Recombinant
>95 % as determined by SDS-PAGE.
Active
Restrictions
For Research Use only
Format
Lyophilized
Reconstitution
Reconstituted in ddH2O at 100 μg/mL.
Buffer
Lyophilized after extensive dialysis against 10 mM PB, pH 7.0.
Stock
-80 °C
Stockage commentaire
Lyophilized recombinant human Epidermal Growth Factor (rhEGF) remains stable up to 12 months at -80 °C from date of receipt. Upon reconstitution, rhEGF should be stable up to 4 weeks at 4 °C or up to 6 months at -20 °C.
Epidermal Growth Factor (EGF) is a potent growth factor that stimulates the proliferation of various epidermal and epithelial cells. Additionally, EGF has been shown to inhibit gastric secretion, and to be involved in wound healing. EGF signals through a receptor known as c-erbB, which is a class I tyrosine kinase receptor. This receptor also binds with TGF-a and VGF (vaccinia virus growth factor). Recombinant human EGF is a 6.2 kDa globular protein containing 53 amino acid residues including 3 intramolecular disulfide-bonds. Recombinant human Epidermal Growth Factor (rhEGF) produced in E. coli is a non-glycosylated polypeptide chain of 54 amino acids. A fully biologically active molecule, rhEGF has a molecular mass of 6.2 kDa analyzed by reducing SDS-PAGE. Synonyms: Urogastrone, URG