Recombinant Human EGF produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 53 amino acids and having a molecular mass of 6222 Dalton. The rHuEGF 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 human EGF. N-terminal methionine has been completely removed enzymatically.
Greater than 98.0% as determined by: - (a) Analysis by RP-HPLC. - (b) Anion-exchange FPLC. - © Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel. Dimers and aggregates: Less than 1% as determined by silver-stained SDS-PAGE gel analysis.
BioVendor´s recombinant human EGF is fully biologically active when compared to standards. The ED50, calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml corresponding to a specific activity of 1×107 Units/mg.
Less than 0.1 ng/µg (IEU/µg) of rHuEGF.
The protein was lyophilized from a concentrated (1mg/mL) solution with no additives.
It is recommended to reconstitute the lyophilized rHuEGF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
At ambient temperature. Upon receipt, store the product at the temperature recommended below.
Lyophilized rHuEGF although stable at room temperature for 3 weeks, should be stored desiccated below –18°C. Upon reconstitution rHuEGF should be stored at 4°C between 2–7 days and for future use below –18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Sterile filtered white lyophilized (freeze-dried) powder.