C Peptide protein (30-AC96)
Purified recombinant Human C Peptide protein
Overview
Overview
| Synonyms | Proinsulin connecting peptide, C-Peptide protein |
|---|---|
| Species | Human |
| Protein Type | Synthetic |
| Applications | User optimized |
Specifications
| Residues | Region of C Peptide protein corresponding to amino acids 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. |
|---|---|
| Source | Human (full length synthetic C-peptide) Tyr-C-Peptide |
| Grade & Purity | > 95% pure |
| Molecular Weight | 3616.99 kDa |
| Form & Buffer | Supplied as a lyophilized powder purified by HPLC, tyrosine residue. |
Storage & Safety
| Storage | Aliquot and store at -20 deg C. Avoid repeated freeze/thaw cycles |
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General Information
| Biological Significance | Proinsulin C-peptide was first described in 1967 in connection with the discovery of the insulin biosynthesis. It serves as an important linker between the A- and the B- chains of insulin and facilitates the efficient assembly, folding, and processing of insulin in the endoplasmic reticulum. Equimolar amounts of C-peptide and insulin are then stored in secretory granules of the pancreatic beta cells and both are eventually released to the portal circulation. Initially, the sole interest in C-peptide was as a marker of insulin secretion and has as such been of great value in furthering the understanding of the pathophysiology of type 1 and type 2 diabetes. The first documented use of the C-peptide test was in 1972. During the past decade, however, C-peptide has been found to be a bioactive peptide in its own right, with effects on microvascular blood flow and tissue health. |
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