Mini Gastrin I, human is a shorter version of human gastrin 1, consists of amino acids 5-17 of the parent peptide, and binds with the CCK2i4svR.
CAT No: R1514
CAS No:54405-27-5
Synonyms/Alias:54405-27-5;Mini Gastrin I, human;22-34-Gastrin I (pig), 22-l-leucine-;EINECS 259-152-3;Minigastrin I (human);Gastrin-I-(5-17);BDBM82236;HY-P5109;MFCD00133359;DA-75549;CS-0676447;
Mini Gastrin I, human is a synthetic peptide corresponding to the biologically active C-terminal fragment of human gastrin. As a member of the gastrin peptide family, it plays a central role in gastrointestinal physiology, notably in stimulating gastric acid secretion and regulating digestive processes. Its truncated structure preserves the essential bioactive motif, making it a valuable molecular tool for dissecting receptor interactions and downstream signaling pathways. The compound's defined sequence and high specificity have rendered it a prominent reagent in studies of peptide-receptor dynamics, gastrointestinal hormone biology, and the broader field of peptide-mediated cellular communication.
Receptor binding studies: Mini Gastrin I is extensively utilized in research focused on characterizing the interactions between gastrin peptides and cholecystokinin-B/gastrin receptors (CCK-B/GR). By employing this peptide in radioligand binding assays or fluorescence-based detection systems, researchers can quantitatively assess receptor affinity, binding kinetics, and specificity. Its well-defined structure makes it ideal for competitive binding experiments, facilitating the elucidation of receptor-ligand recognition principles and informing the design of receptor-targeted probes or antagonists.
Signal transduction analysis: The peptide serves as a robust agonist in cellular models designed to study intracellular signaling cascades initiated by gastrin receptor activation. Upon binding to its cognate receptor, Mini Gastrin I triggers downstream pathways such as phospholipase C activation, inositol phosphate turnover, and calcium mobilization. These features enable detailed investigation of G protein-coupled receptor (GPCR) signaling mechanisms, allowing researchers to dissect the molecular events underlying hormone-driven cellular responses in gastric and non-gastric tissues.
Gastrointestinal physiology research: By mimicking the endogenous activity of gastrin, this peptide is instrumental in experimental systems that model gastric acid secretion, mucosal growth, and enteroendocrine regulation. Its application in ex vivo tissue preparations or cell-based assays supports the study of paracrine and autocrine signaling within the digestive tract. These models help clarify the physiological consequences of altered peptide levels, contributing to a deeper understanding of digestive homeostasis and the regulation of gastric function.
Peptide structure-activity relationship (SAR) studies: Mini Gastrin I provides a powerful platform for SAR investigations aimed at mapping the functional domains of gastrin and related peptides. By systematically modifying its amino acid sequence or comparing its activity to longer and shorter analogs, researchers can pinpoint residues critical for receptor activation, stability, and bioactivity. Such insights drive the rational design of novel peptide analogs with tailored biological properties for research applications.
Analytical method development: The defined chemical nature and bioactivity of Mini Gastrin I make it a valuable standard for the development and validation of analytical techniques, including high-performance liquid chromatography (HPLC), mass spectrometry, and immunoassays. Its use as a calibration reference or positive control enhances method reliability when quantifying gastrin-like peptides in complex biological samples. This supports advancements in peptide detection, quantitation, and quality control across basic and applied research settings.
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