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Insulin Peptides

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C9781 Tyr-C-Peptide human ≥95% (HPLC) Tyr-C-Peptide is derived from genetically modified Arg32Tyr human pro-insulin mutants by trypsin and carboxypeptidase B codigestion.
C8662 C-Peptide Fragment 3-33 human ≥85% (HPLC)  
I1633 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.
I6383 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.
C4999 Proinsulin C-Peptide (55-89) human bioactive peptide hormone C-Peptide Fragment (55-89) is a fragment derived from the proinsulin C-peptide. C-peptide has cell signaling activity that involves calcium-dependent intracellular signaling. C-Peptide Fragment 55-89 may be used to help researchers understand the role of specific sequences within the C-peptide in binding, conformation and function of C-peptide.
C-Peptide was initially thought to have no intrinsic biological activity. More recent research has identified multiple biological effects of C-peptide, including binding to cell membranes, activation of signaling pathways, and stimulation of Na+,K+-ATPase and endothelial nitric oxide synthetase. However, the exact function of C-peptide is unclear due to conflicting physiological effects.