Proinsulin C-peptide (human) is a 31-amino-acid peptide that links the A and B chains of proinsulin, ensuring its correct folding, which is biologically active and modulates cellular function .
CAT No: R1632
CAS No:33017-11-7
Synonyms/Alias:C-Peptide;33017-11-7;Human proinsulin C-peptide;Proinsulin C-peptide (human);C-Peptide, Proinsulin;Human c-peptide;Proinsulin C-peptide human;Nmij-crm 6901a;Insulin c-peptide;CBX 129801;CBX129801;DTXSID00186651;C-Peptide (human) acetate salt;Connecting Peptide;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;PROINSULIN CONNECTING PEPTIDE (HUMAN), 1-DE-L-ARGININE-2-DE-L-ARGININE-34-DE-L-LYSINE-35-DE-L-ARGININE-;Proinsulin C Peptide;C Peptide, Proinsulin;c-Peptide(human);GTPL6145;CHEMBL4594409;DTXCID40109142;GLXC-26476;DA-52113;L-Glutamine, L-alpha-glutamyl-L-alanyl-L-alpha-glutamyl-L-alpha-aspartyl-L-leucyl-L-glutaminyl-L-valylglycyl-L-glutaminyl-L-valyl-L-alpha-glutamyl-L-leucylglycylglycylglycyl-L-prolylglycyl-L-alanylglycyl-L-seryl-L-leucyl-L-glutaminyl-L-prolyl-L-leucyl-L-alanyl-L-leucyl-L-alpha-glutamylglycyl-L-seryl-L-leucyl-;
Proinsulin C-peptide human is a synthetic peptide corresponding to the connecting peptide region of human proinsulin, a critical intermediate in insulin biosynthesis. As a 31-amino acid sequence that links the A and B chains of proinsulin, C-peptide is enzymatically cleaved during the maturation of insulin within pancreatic β-cells. Its unique structure and physiological role in insulin processing make it a valuable tool in studies of peptide hormone biochemistry, pancreatic function, and metabolic regulation. Researchers and industry professionals utilize this biomolecule to elucidate the mechanistic underpinnings of insulin biosynthesis, secretion, and associated metabolic pathways, as well as to develop and refine analytical methods relevant to endocrinology and metabolism.
Peptide hormone research: The synthetic human C-peptide serves as an essential research tool for investigating peptide hormone processing and secretion in mammalian systems. By mimicking the native connecting peptide, it enables detailed study of the enzymatic cleavage events that generate mature insulin and C-peptide from proinsulin precursors. Its use in in vitro and ex vivo systems provides insight into the regulation of insulin biosynthesis, the fidelity of post-translational modifications, and the activity of prohormone convertases. Researchers leverage this molecule to dissect the molecular mechanisms governing peptide hormone maturation and to clarify the roles of intermediate peptides in endocrine physiology.
Metabolic pathway elucidation: C-peptide is integral to metabolic research focused on glucose homeostasis and pancreatic β-cell function. Its measurement and manipulation in cell culture and biochemical assays facilitate the exploration of insulin secretion dynamics and the interplay between proinsulin processing and metabolic signaling pathways. By incorporating synthetic C-peptide into experimental models, scientists can probe the regulatory networks that control insulin release, assess β-cell viability, and investigate metabolic adaptations under various physiological and pathological conditions.
Immunoassay development: The availability of highly characterized human C-peptide supports the development and validation of quantitative immunoassays for peptide hormones. It acts as a standard or calibrator in enzyme-linked immunosorbent assays (ELISA), radioimmunoassays, and other immunodetection platforms designed to measure C-peptide levels in biological samples. This application is crucial for ensuring assay specificity, reproducibility, and sensitivity, thereby enabling the accurate quantification of endogenous peptide concentrations in research settings.
Peptide structure-function analysis: Synthetic C-peptide provides a reliable substrate for studies aimed at understanding peptide conformation, receptor interactions, and post-translational modifications. Structural and biophysical investigations using this peptide help delineate the three-dimensional arrangement of the connecting region in proinsulin, as well as its influence on the folding and stability of the hormone precursor. Such research supports the rational design of peptide analogs and the identification of critical residues required for biological activity or molecular recognition.
Analytical method calibration: In biochemical and analytical laboratories, human C-peptide serves as a reference compound for method development, calibration, and performance verification. Its defined sequence and physicochemical properties make it suitable for mass spectrometry, chromatography, and electrophoretic techniques aimed at detecting and quantifying peptide hormones. Employing this standard ensures the validity and comparability of analytical results across diverse experimental systems, facilitating robust data interpretation in peptide research and metabolic studies.
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