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Insulin-like Growth Factor-I (IGF-I) is a polypeptide growth factor that stimulates the proliferation of a range of cell types including muscle, bone, and cartilage tissue. Human IGF-I is a 7.6 kDa protein containing 70 amino acid residues. The source is E.coli. Formulation is sterile filtered and then the protein was lyophilized with no additives. The lyophilized IGF-I, though stable at room temperature, is best stored desiccated below 0°C. Reconstituted IGF-I should be stored in working aliquots at -20°C. Purity is greater than 97% by SDS-PAGE and HPLC analyses. Endotoxin level is less than 0.1 ng per µg (1EU/ug) of IGF-I.

The lyophilized IGF-I is soluble in water and most aqueous buffers. The lyophilized protein can be reconstituted in 10 mM acetic acid to a concentration of 1 mg/ml. This solution can be diluted into other buffered solutions or stored at -20°C for future use. For most in vitro applications, IGF-I exerts its biological activity in the concentration range of 0.2 to 20.0 ng/ml.

The human IGF-I is fully biologically active when compared to standards. The ED₅₀ as determined by the dose-dependent stimulation of thymidine uptake by BALB/c 3T3 cells is < 1.0 ng/ml, corresponding to a specific activity of > 1 x 10⁶ units/mg. Usage is for research use only, not for diagnostic or therapeutic procedures.

PeproTech, Inc., Princeton Business Park, 5 Crescent Ave., G2 Rocky Hill, NJ 08553. Tel: 609-497-0253; Fax: 609-492-0321.

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