Amino Acid Sequence Arg-Arg-Glu-Ala-Glu-Asp-Leu-Gln-Val-Gly-Gln-Val-Glu-Leu-Gly-Gly-Gly-Pro-Gly-Ala-Gly-Ser-Leu-Gln-Pro-Leu-Ala-Leu-Glu-Gly-Ser-Leu-Gln-Lys-Arg Other Notes Human proinsulin, the single-chain peptide precursor of insulin, consists of the insulin A and B chains connected by the 31 amino acid C-peptide. Cleavage of proinsulin by proteolytic enzymes produces insulin and free C-peptide. The product here is the 35-mer peptide (Arg-Arg-C-Peptide-Lys-Arg) observed to separate the insulin A and B chains.1 Biochem/physiol Actions 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. |
Amino Acid Sequence Arg-Arg-Glu-Ala-Glu-Asp-Leu-Gln-Val-Gly-Gln-Val-Glu-Leu-Gly-Gly-Gly-Pro-Gly-Ala-Gly-Ser-Leu-Gln-Pro-Leu-Ala-Leu-Glu-Gly-Ser-Leu-Gln-Lys-Arg Other Notes Human proinsulin, the single-chain peptide precursor of insulin, consists of the insulin A and B chains connected by the 31 amino acid C-peptide. Cleavage of proinsulin by proteolytic enzymes produces insulin and free C-peptide. The product here is the 35-mer peptide (Arg-Arg-C-Peptide-Lys-Arg) observed to separate the insulin A and B chains.1 Biochem/physiol Actions 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. |