Epidermal Growth Factor
human, recombinant, Pichia pastoris
For in vitro use only!
Shipping: shipped at ambient temperature
Storage Conditions: store at -20 °C
avoid freeze/thaw cycles
Shelf Life: 12 months
Molecular Weight: 6 kDa
Accession number: Q6QBS2
Accession number: Q6QBS2
Purity: > 95 % (SDS-PAGE, RP-HPLC)
Form: lyophilised (Solution contained 0.15 M NaCl and 0.025 M sodium bicarbonate pH 7.5)
Solubility: It is recommended to reconstitute the lyophilised EGF in sterile bidest H2O not less than 100 μg/ml, which can then be further diluted to other aqueous solutions. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Activity: EC50: 0.1 ng/ml corresponding to a specific activity of 1 x 107 Units/mg, calculated by the dosedependent proliferation of murine BALB/c 3T3 cells (measured by 3H-thymidine uptake).
Epidermal Growth Factor (EGF) is a 6 kDa polypeptide growth factor initially discovered in mouse submaxillary glands. Human epidermal growth factor was originally isolated from urine based on its ability to inhibit gastric secretion and called urogastrone. EGF exerts a wide variety of biological effects including the promotion of proliferation and differentiation of mesenchymal and epithelial cells. Recombinant human Epidermal Growth Factor produced in Pichia pastoris is a single, glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 6.2 kDa. Recombinant EGF is purified by proprietary chromatographic techniques.
Amino Acid Sequence: The sequence of the first five N-terminal amino acids was determined and was found to be Asn-Ser-Asp-Ser-Glu, which agrees with the sequence of native EGF human. N-terminal methionine has been completely removed enzymatically.
Jahanshahi et al. (2004) Alterations in antioxidant power and levels of epidermal growth factor and nitric oxide in saliva of patients with inflammatory bowel diseases. Dig. Dis. Sci. 49:1752.
Zanuttin et al. (2004) Folding of epidermal growth factor-like repeats from human tenascin studied through a sequence frame-shift approach. Eur. J. Biochem. 271:4229.
Leahy (2004) Structure and function of the epidermal growth factor (EGF/ErbB) family of receptors. Adv. Protein Chem. 68:1.
Chlenski et al. (2004) Neuroblastoma angiogenesis is inhibited with a folded synthetic molecule corresponding to the epidermal growth factor-like module of the follistatin domain of SPARC. Cancer Res. 64:7420.
Smith et al. (2004) Epidermal growth factor stimulates urokinasetype plasminogen activator expression in human gingival fibroblasts. Possible modulation by genistein and curcumin. J. Periodontal Res. 39:380.