RC-3095 (TFA) is a peptide analog enriched in aromatic and basic residues that foster defined conformational states. Researchers employ it in mapping ligand-binding determinants, structural transitions, and helix-associated motifs. Its design supports examination of backbone rigidity and solvent influence. TFA salt form ensures consistent solvation properties.
CAT No: R2191
CAS No:1217463-61-0
Synonyms/Alias:RC-3095 (TFA);1217463-61-0;RC-3095 TFA;138147-78-1;Rc-3095;RC-3095 trifluoroacetate;HY-P0107A;DA-67129;MS-32060;RC-3095, >=95% (HPLC), semisolid;CS-0103539;G17080;
RC-3095 (Tfa) is a synthetic peptide analog known for its role as a selective gastrin-releasing peptide receptor (GRPR) antagonist. Structurally derived from bombesin, it is widely utilized in biochemical and pharmacological research to investigate the physiological and pathological functions of bombesin-like peptides. The trifluoroacetate (Tfa) salt form ensures enhanced stability and solubility, making it suitable for a range of experimental settings. As a research-grade peptide, RC-3095 (Tfa) provides a valuable tool for dissecting GRPR-mediated signaling pathways, exploring receptor-ligand interactions, and studying the downstream effects of bombesin antagonism in cellular and molecular systems.
Receptor binding studies: RC-3095 (Tfa) serves as an essential probe in receptor binding assays designed to characterize the affinity and specificity of ligands for the gastrin-releasing peptide receptor. By competitively inhibiting endogenous or synthetic bombesin analogs, it enables researchers to delineate the pharmacological profile of GRPR and assess the binding kinetics of novel compounds. These studies are fundamental for mapping receptor-ligand interactions and for the development of new receptor-targeted agents in basic biochemical research.
Signal transduction research: The peptide is frequently employed in experiments aimed at elucidating GRPR-mediated signal transduction pathways. By selectively blocking receptor activation, it allows for the investigation of downstream molecular events such as intracellular calcium mobilization, MAPK pathway activation, and gene expression changes. This application is particularly valuable for understanding the cellular mechanisms regulated by bombesin-like peptides and for identifying potential modulators of GRPR signaling.
Functional studies in cell culture: In vitro systems benefit from the use of RC-3095 (Tfa) to modulate GRPR activity in a controlled manner. Researchers utilize the compound to inhibit bombesin-stimulated cellular responses, including proliferation, migration, and secretion activities in various cell lines. Such functional assays are instrumental in dissecting the physiological roles of GRPR in normal and transformed cells, providing insight into receptor-driven cellular behavior under experimental conditions.
Peptide antagonist validation: The compound is a reference standard for validating the specificity and efficacy of newly developed GRPR antagonists. By serving as a benchmark in comparative studies, it assists in confirming the antagonist activity of novel peptides or small molecules. This application is integral to the optimization of antagonist design and the advancement of structure-activity relationship (SAR) research in the field of peptide-based drug discovery.
Analytical method development: RC-3095 (Tfa) is also utilized in the development and validation of analytical techniques for peptide quantification and characterization. Its defined structure and receptor selectivity make it a suitable internal control or calibration standard in high-performance liquid chromatography (HPLC), mass spectrometry, and other peptide analysis methodologies. Employing the compound in these contexts enhances the accuracy and reproducibility of peptide detection and quantification in complex biological samples.
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