(Tyr0)-C-peptide (human) includes an N-terminal tyrosine substitution that influences aromatic interactions and backbone polarity. Researchers use it to examine residue-dependent effects on folding, solvation, and recognition. The sequence supports mapping of peptide-protein contacts. Its design allows enhanced spectroscopic characterization.
CAT No: R2288
CAS No:57327-90-9
Synonyms/Alias:(TYR0)-C-PEPTIDE (HUMAN);57327-90-9;MFCD00079971;(Tyr0)-c-peptide(human);DA-69296;FT109409;(Tyr0)-C-Peptide (human) (H-Tyr-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-OH);H-Tyr-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-OH ; H-YEAEDLQVGQVELGGGPGAGSLQPLALEGSLQ-OH;
(Tyr0)-C-peptide (human) is a synthetic peptide analog derived from the human C-peptide sequence, modified by the addition of a tyrosine residue at the N-terminus. As a specialized research-grade peptide, it serves as a valuable molecular tool for studies involving insulin biosynthesis, proinsulin processing, and peptide hormone signaling. The presence of the N-terminal tyrosine facilitates specific labeling or conjugation strategies, enhancing its utility in various biochemical and analytical applications. Its structural fidelity to the native C-peptide sequence allows for the investigation of peptide-receptor interactions, metabolic pathways, and cellular signaling mechanisms relevant to endocrinology and metabolic research.
Peptide hormone research: The modified C-peptide analog is widely employed in the study of peptide hormone biology, particularly in elucidating the physiological and biochemical roles of C-peptide in pancreatic β-cell function and insulin secretion. By closely mimicking the endogenous peptide, it enables researchers to dissect the downstream signaling pathways and cellular responses triggered by C-peptide engagement with its putative receptors, thereby advancing understanding of its non-insulin-mediated effects in metabolic regulation.
Immunoassay development: The addition of an N-terminal tyrosine residue provides a convenient site for radioiodination or other labeling techniques, making the peptide especially suited for immunoassay calibration and tracer studies. Researchers can generate highly specific antibodies or develop sensitive detection assays for quantifying C-peptide or monitoring its dynamics in experimental systems. This capability is critical for the standardization and validation of immunoanalytical platforms in both basic and translational research settings.
Receptor binding studies: As a structurally defined peptide, the analog is instrumental in receptor binding assays aimed at characterizing the interaction between C-peptide and its cellular binding partners. The synthetic nature and precise modification allow for controlled experimental conditions, facilitating kinetic and affinity measurements that help clarify the molecular determinants of C-peptide recognition and signaling. Such studies are essential for mapping receptor specificity and for the rational design of peptide-based probes or modulators.
Peptide labeling and conjugation: The presence of the tyrosine residue at the N-terminus enables efficient site-specific conjugation with a range of reporter molecules, such as fluorescent dyes, biotin, or isotopic labels. This feature supports the creation of customized peptide probes for imaging, tracking, or pull-down experiments, thereby expanding the repertoire of analytical tools available for peptide localization, trafficking, and interaction analysis in vitro and in cell-based systems.
Peptide structure-function analysis: The analog serves as a model substrate in studies investigating the structural features and functional domains of C-peptide. By introducing defined modifications, researchers can systematically probe the impact of sequence alterations on biological activity, stability, and receptor engagement. Such structure-activity relationship investigations contribute to a deeper understanding of peptide function and inform the design of novel analogs with tailored properties for advanced biochemical research.
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