C-peptide Detection
C-peptide Detection - Related Videos
08:07
Personalized Peptide Arrays for Detection of HLA Alloantibodies in Organ Transplantation
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Cited by 2 •
2017
Mismatches in human leukocyte antigen (HLA) sequences between organ donor and recipient pairs are the major cause of antibody-mediated rejection in organ transplantation. Here we present the use of custom antigen arrays that are based on individual donors' HLA sequences to probe anti-donor HLA alloantibodies in organ recipients.
06:15
Biotinylated Cell-Penetrating Peptide Probe to Detect Protein-Protein Interactions
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2025
This video demonstrates a technique that uses biotinylated cell-penetrating peptides to detect intracellular protein-protein interactions. The cell-penetrating peptides facilitate the conjugated peptide to enter a cell and specifically bind to its interacting proteins. The biotin, after binding to avidin, allows purification of the interacting proteins’ complex from a cell lysate.
05:15
Target Peptide Detection and Measurement Using a Capacitive Immunoprobe Biosensor
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2025
This video demonstrates a method for detecting and quantifying peptide transmitters using a capacitive immunoprobe biosensor. The functionalized electrode, coated with antibodies, interacts with peptides of interest, leading to a signal change that allows precise measurement and detection of peptides.
08:37
Sampling Human Indigenous Saliva Peptidome Using a Lollipop-Like Ultrafiltration Probe: Simplify and Enhance Peptide Detection for Clinical Mass Spectrometry
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Cited by 2 •
2012
Considering saliva sampling for future clinical application, a lollipop-like ultrafiltration (LLUF) probe was fabricated to fit in the human oral cavity. Direct analysis of undigested saliva by NanoLC-LTQ mass spectrometry demonstrated the ability of LLUF probes to remove large proteins and high abundance proteins, and make low-abundant peptides more detectable.
03:15
A Peptide Array-Based Detection of Anti-donor HLA Alloantibodies in Organ Recipients
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2025
This video demonstrates an assay to detect anti-donor HLA alloantibodies in organ recipients. A peptide array is synthesized to represent potential epitopes for antibody-mediated organ rejection. The array is incubated with the recipient's serum, containing alloantibodies that bind to their target epitopes. Antibody binding is detected using chemiluminescence to identify donor-specific HLA epitopes that incite alloantibody reactivity.
FAQs
The distinction depends on how the two insulin sources are made. Pancreatic beta cells release C-peptide when they process proinsulin, whereas pharmaceutical insulin does not contain this connecting peptide. Consequently, a measured C-peptide signal indicates insulin production by the patient’s own beta cells, even when injected insulin is also present in the circulation.
Because proinsulin cleavage produces insulin and C-peptide in approximately equal amounts, C-peptide concentration serves as an indicator of insulin secretion rather than a measurement of administered insulin. Interpreting the result therefore centers on whether the pancreas is producing insulin and how much residual beta-cell activity may remain, rather than on total insulin exposure from all sources.
C-peptide is generated at the same biosynthetic step that produces pancreatic insulin, so its detection provides information about the activity of insulin-producing beta cells. Measuring it can reveal whether endogenous secretion persists and can help clinicians assess insulin production over time. This makes the marker useful when direct insulin results could include both pancreatic and pharmaceutical sources.
Laboratories measure C-peptide in blood or urine using immunoassays, which use targeted detection of the peptide to produce a laboratory result. The choice of specimen allows assessment of endogenous insulin secretion through more than one sample type. Results must then be considered in the clinical context, particularly when evaluating insulin production or unexplained low blood glucose.
During evaluation of unexplained hypoglycemia, C-peptide detection helps determine whether insulin secretion from the pancreas is contributing to the low-glucose state. A result can be interpreted alongside the possibility of injected insulin, because pharmaceutical insulin lacks C-peptide. This distinction supports a more focused assessment of the source of insulin activity involved in the presentation.
C-peptide results provide evidence about how much endogenous insulin production remains, which can contribute to classifying diabetes according to pancreatic beta-cell function. Repeated assessment can also show changes in insulin production over time. This information adds functional context to clinical evaluation by indicating whether endogenous secretion is preserved, reduced, or changing.