In proinsulin the insulin A and B chains are linked by C peptide. During the biosynthesis of insulin, the C peptide promotes proper protein folding and disulfide bond placement after which it is cleaved. The cleaved peptide may inhibit insulin aggregation and is stored and released from the β cells with insulin in a one-to-one molar ratio. C peptide is a marker for β cell function in vivo; levels are enhanced in insulin resistance or insuloma and reduced in insulin insufficiency (type I diabetes). C peptide may alleviate the vascular damage and neuropathy associated with insulin depletion.
Insulin Chain B Oxidized from bovine pancreas ≥80% (HPLC), powder
Insulin regulates the cellular uptake, utilization, and storage of glucose, amino acids, and fatty acids. It inhibits the breakdown of glycogen, protein, and fat. The β chain is a substrate for carboxypeptidase Y.
Insulin chain A oxidized ammonium salt from bovine pancreas ≥80% (HPLC), powder
Insulin regulates the cellular uptake, utilization, and storage of glucose, amino acids, and fatty acids. It inhibits the breakdown of glycogen, protein, and fat. The α chain contains an intrachain disulfide bond.
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