Metabolic research

C-Peptide

Late stage

Endogenous proinsulin peptide fragment

Research material. Not for human or animal consumption.

Research overview

C-peptide is the 31-amino-acid 'connecting peptide' that links the A and B chains of insulin inside proinsulin. When proinsulin is processed, C-peptide is released into the blood in equal amounts to insulin. Because the liver clears little of it and it is unaffected by injected insulin, it is the standard measure of how much insulin a person's pancreas still makes. It is used to distinguish type 1 from type 2 diabetes and as an endpoint in trials aiming to preserve beta cells. Trials of C-peptide replacement for nerve damage did not show benefit.

EVIDENCE LEVEL Late stage

Substantial controlled clinical research or late stage development has been identified; this is not a product authorisation claim.

Molecule classEndogenous proinsulin peptide fragment
Batch documentationAsk for the batch COA
Research fieldMetabolic Research
EnquiriesContact the team

Questions about C-Peptide

PRODUCT QUESTIONS
What is C-Peptide?

C Peptide is a 31 residue peptide cut from proinsulin when insulin is formed. It has no disulfide bonds and its sequence varies more between species than insulin's does.

What research has been published on C-Peptide?

Human research centres on measurement: fasting and stimulated levels for diabetes classification, monogenic diabetes testing and beta cell function in new onset type 1 diabetes trials. Earlier studies tested C peptide replacement for diabetic nerve and kidney complications.

What batch documentation should accompany C-Peptide?

C-Peptide: Ask for the COA and analytical reports for the batch being quoted. For use as an assay standard, ask for species, mass spectrometry, HPLC purity, accurately stated peptide content and traceability to a recognised reference material.

How should C-Peptide storage conditions be assessed?

Store C Peptide lyophilised at −20°C. For calibration work, divide solutions into single use portions and freeze them, avoiding repeated thawing.