- Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. Recombinant human Insulin produced in Yeast consists of two glycosylated polypeptide chains with 51 amino acids, having a molecular mass of 5807 Dalton. Zinc content was found to be 0.4%. The recombinant Insulin has been purified using proprietary chromatographic techniques.
- Product Overview
- Human INS expressed in Saccharomyces cerevisiae
- CAT# CSC-CTK0133-10 (10 mg); CAT# CSC-CTK0133-50 (50 mg)
- Expression System
- Saccharomyces cerevisiae
- Greater than 98% as determined by SDS-PAGE and RP-HPLC analysis.
- 27 units/mg. Insulin has been evaluated in cell culture (Human Foreskin Fibroblasts). The effective concentration range for use in defined media is 1-5 μg/ml. However, the optimum concentration range for a particular application has to be determined by the investigator.
- Sterile-filtered, white, lyophilized (freeze-dried)powder. The protein was lyophilized from a protein solution in 50 mM sodium chloride.
- Please centrifuge product briefly before opening vial. The lyophilized protein should be reconstituted in sterile PBS to a concentration of 0.1 - 1.0 mg/ml. This solution can then be diluted into other aqueous buffers and stored at -20°C for future use.
- Storage & Stability
- The lyophilized protein, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted protein should be used immediately or stored long-term in undiluted working aliquots at -20°C. Avoid repeated freeze-thaw cycles.
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