(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 derivative based on the human C-peptide sequence, modified by the addition of a tyrosine residue at the N-terminus. This structural modification facilitates enhanced research utility, particularly in studies requiring peptide labeling or detection. As a non-biologically active fragment of proinsulin, the peptide serves as a valuable tool in a range of biochemical and molecular biology applications. Its stability and ease of synthesis have made it a preferred choice for researchers investigating peptide behavior, receptor interactions, and peptide-based assay development. The presence of the N-terminal tyrosine residue allows for efficient conjugation with labels such as radioactive isotopes or fluorescent dyes, further expanding its versatility in experimental protocols.
Immunoassay Development: (Tyr0)-C-peptide (human) is widely utilized as a calibrator or standard in the development of immunoassays designed to quantify C-peptide levels in biological samples. The N-terminal tyrosine modification provides a convenient site for labeling with detection molecules, such as biotin or radioisotopes, enhancing the sensitivity and specificity of immunoassays. By serving as a reference or tracer, the peptide enables the accurate measurement of endogenous C-peptide, which is crucial for studies focused on insulin secretion and pancreatic function in various research contexts.
Receptor Binding Studies: The synthetic peptide is frequently employed in receptor binding assays to investigate the interaction between C-peptide and its putative receptors. The tyrosine tag enables researchers to label the peptide with iodine-125 or other tracers, facilitating the tracking of binding events in cell-based or membrane-based systems. These studies are instrumental in elucidating the molecular mechanisms by which C-peptide exerts its biological effects, thus advancing the understanding of peptide-receptor signaling pathways.
Peptide Structure-Function Analysis: Researchers leverage (Tyr0)-C-peptide (human) to explore the structure-activity relationships of C-peptide and its analogs. The addition of an N-terminal tyrosine residue allows for the incorporation of various probes or crosslinkers, enabling detailed investigations into the conformational dynamics, stability, and intermolecular interactions of the peptide. Such structure-function studies are essential for mapping functional domains and identifying key residues responsible for biological activity and interaction with other biomolecules.
Analytical Method Validation: The peptide serves as a valuable reference material in the validation of analytical techniques, including mass spectrometry and high-performance liquid chromatography (HPLC). Its well-defined sequence and modifiable N-terminus make it an ideal candidate for spiking experiments, calibration curves, and recovery studies. By providing a consistent and traceable standard, it supports the development and validation of robust analytical methods for peptide quantification and characterization in complex matrices.
Peptide Labeling and Conjugation Research: (Tyr0)-C-peptide (human) is extensively used in studies focused on the development and optimization of peptide labeling and conjugation strategies. The presence of the N-terminal tyrosine residue offers a reactive handle for the attachment of various functional groups, including fluorescent dyes, affinity tags, or imaging agents. This enables the creation of custom-labeled peptides for use in imaging, detection, and tracking experiments, thereby expanding the toolkit available for peptide-based research and assay design.
In summary, (Tyr0)-C-peptide (human) stands out as a versatile and reliable reagent across multiple research domains, including immunoassay development, receptor binding studies, structure-function analysis, analytical method validation, and peptide labeling research. Its unique structural features, particularly the N-terminal tyrosine, provide significant advantages for labeling, detection, and analytical applications, empowering researchers to advance their investigations into peptide biology and assay technology.
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