Proinsulin C-Peptide (55-89), human is a peptide fragment of the cleavage product of proinsulin.
CAT No: R1631
CAS No:11097-48-6
Synonyms/Alias:11097-48-6;Proinsulin C-Peptide (55-89) human;Proinsulin C-Peptide (55-89), human;MFCD00076294;Proinsulin C-Peptide (55-89) (human);DTXSID00745469;PUBCHEM_71308369;C-Peptide human, >=95% (HPLC);DA-66889;FP108538;G12215;Proinsulin C-Peptide (55-89) (human) (H-L-Arg-L-Arg-L-Glu-L-Ala-L-Glu-L-Asp-L-Leu-L-Gln-L-Val-Gly-L-Gln-L-Val-L-Glu-L-Leu-Gly-Gly-Gly-L-Pro-Gly-L-Ala-Gly-L-Ser-L-Leu-L-Gln-L-Pro-L-Leu-L-Ala-L-Leu-L-Glu-Gly-L-Ser-L-Leu-L-Gln-L-Lys-L-Arg-OH);
Proinsulin C-Peptide (55-89), human, is a synthetic peptide corresponding to the C-terminal segment of human proinsulin, comprising amino acids 55 through 89. This peptide represents a crucial connecting region between the A and B chains of proinsulin, which is cleaved during the maturation of insulin in pancreatic beta cells. As a well-characterized peptide fragment, it serves as a valuable tool for investigating insulin biosynthesis, secretion pathways, and the physiological role of C-peptide itself. Its defined sequence and human origin make it particularly relevant for studies requiring precise molecular mimicry of endogenous human proinsulin processing.
Peptide biochemistry research: The human C-Peptide (55-89) is widely utilized in peptide biochemistry for elucidating the structural and functional properties of proinsulin and its cleavage products. Researchers employ this fragment to study the mechanisms underlying proinsulin folding, disulfide bond formation, and the enzymatic processes responsible for generating mature insulin and C-peptide. Its use enables detailed characterization of the molecular events involved in insulin maturation, providing insight into both normal physiology and the molecular basis of beta cell dysfunction.
Immunoassay development: The synthetic C-Peptide (55-89) is an essential calibrator and antigen standard in the development and validation of immunoassays designed to quantify C-peptide levels in biological samples. Its sequence fidelity and immunogenic properties facilitate the production of highly specific antibodies and allow for the establishment of robust, reproducible assay systems. These immunoassays are critical tools in research focused on pancreatic beta cell activity, insulin secretion dynamics, and metabolic regulation.
Receptor interaction studies: Emerging evidence indicates that C-peptide may possess biological activity through interaction with cell surface receptors and intracellular signaling pathways. The defined human peptide fragment is employed in vitro to investigate these potential receptor-mediated effects, enabling researchers to dissect the molecular mechanisms by which C-peptide influences cellular function, gene expression, or metabolic responses. Such studies help clarify the non-insulin-related actions of proinsulin cleavage products.
Cell signaling investigations: Proinsulin C-Peptide (55-89), human, serves as a functional probe in the exploration of intracellular signaling cascades modulated by C-peptide. By introducing the peptide into cultured cells or biochemical systems, investigators can assess its impact on pathways such as MAPK, PI3K/Akt, or calcium signaling. These experiments contribute to a deeper understanding of how C-peptide may modulate cellular homeostasis, stress responses, or metabolic adaptation at the molecular level.
Peptide synthesis and analytical method validation: The availability of a well-defined synthetic human C-peptide fragment supports method development in peptide synthesis, purification, and analytical characterization. Laboratories utilize this peptide as a reference standard for optimizing chromatographic separation, mass spectrometric detection, or peptide quantification protocols. Its consistent structure and stability make it an ideal benchmark for quality control and validation procedures in peptide research and production environments.
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