Recombinant Chicken Insulin Like Growth Factor-I - rcIGF-I



Data Sheet
Home > cytokines > Recombinant Chicken Insulin Like Growth Factor-I - rcIGF-I

Recombinant Chicken Insulin Like Growth Factor-I - rcIGF-I

Description Recombinant Chicken IGF-I produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7738 Dalton. rcIGF-I is purified by proprietary chromatographic techniques.
Source Escherichia Coli.
Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation The protein was lyophilized after extensive dialysis against 100mM acetic acid.
Solubility It is recommended to reconstitute the lyophilized rcIGF-I in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Stability Lyophilized rcIGF-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution rcIGF-I 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.
Purity Greater than 95.0% as determined by: Analysis by RP-HPLC.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.
Biological Activity: ProSpec’s rcIGF-I is fully biologically active when compared to standards. The ED50, was calculated 2 methods: 1. Stimulation of protein synthesis in rat L6 myoblasts ED50 was found to be less then 30 ng/ml. 2. Type 1 IGF receptor binding assay ED50 was found to be less then 10 ng/ml.
Endotoxin: Less than 0.1 ng/µg (IEU/µg) of rcIGF-I.
Protein content: Protein quantitation was carried out by two independent methods: UV spectroscopy at 280 nm.nalysis by RP-HPLC, using a calibrated solution of chicken IGF-I as a Reference Standard.
Usage This material is offered for research, laboratory or further manufacturing purposes.
Refrences Upton F.Z. et al. (1992) J. Mol. Endocrinol. 9, 83-92. McMurtry J.P. et al. (1997) Dom. Animal Endocrinol. 14, 199-229.