Gastrin-1, human is the endogenous peptide produced in the stomach, and increases gastric acid secretion via cholecystokinin 2 (CCK2) receptor.
CAT No: HB00095
CAS No:10047-33-3
Synonyms/Alias:Gastrin I human;Gastrin-17;Gastrin I (human);Little gastrin I;10047-33-3;Gastrin 17;Gastrin heptadecapeptide;Heptadecapeptide gastrin;60748-06-3;Little gastrin;G 17;Gastrin centn, human;CHEMBL4451154;Shg17NS;C97H124N20O31S;GastrinIHuman;Gastrin-1;Gastrin-I (human);MFCD00076500;desulfated gastrin-17;XGPWLEEEEEAYGWMDF;18-34-Gastrin, 18-(5-oxo-L-proline)-;GTPL8408;CHEBI:75441;DTXSID601028770;BDBM50517370;HB3575;Gastrin I human, >=95% (HPLC);AKOS024457376;AS-56740;DA-63707;(X = Glp, Phe-17 = C-terminal amide);A11815;Q6652696;Glp-Gly-Pro-Trp-Leu-Glu-Glu-Glu-Glu-Glu-Ala-Tyr-Gly-Trp-Met-Asp-Phe-NH2;5-oxo-L-prolylglycyl-L-prolyl-L-tryptophyl-L-leucyl-L-alpha-glutamyl-L-alpha-glutamyl-L-alpha-glutamyl-L-alpha-glutamyl-L-alpha-glutamyl-L-alanyl-L-tyrosylglycyl-L-tryptophyl-L-methionyl-L-alpha-aspartyl-L-phenylalaninamide;
Gastrin I (human) is a biologically significant peptide hormone that plays a central role in the regulation of gastric acid secretion and gastrointestinal physiology. As a member of the gastrin peptide family, it is synthesized and secreted primarily by G cells in the gastric antrum, exerting its effects through specific interactions with the cholecystokinin B/gastrin receptor (CCK-BR) on target cells. The sequence and structure of human Gastrin I make it a valuable molecular tool for investigating peptide-receptor interactions, signal transduction pathways, and the broader mechanisms underlying digestive system function. Its utility in experimental research extends across multiple disciplines, including endocrinology, cell signaling, gastrointestinal biology, and peptide pharmacology.
Receptor binding studies: Gastrin I is extensively used in receptor binding assays to elucidate the specificity, affinity, and kinetics of ligand interactions with the CCK-B/gastrin receptor. By employing radiolabeled or fluorescently tagged forms, researchers can quantify receptor density, characterize receptor subtypes, and map binding domains, thereby advancing the understanding of peptide hormone recognition and receptor-mediated signaling events in gastric and extra-gastric tissues.
Signal transduction research: The peptide serves as a model agonist for dissecting downstream signaling cascades initiated by gastrin receptor activation. Experimental systems utilizing Gastrin I enable the study of intracellular pathways such as phospholipase C activation, inositol phosphate generation, calcium mobilization, and protein kinase cascades. These investigations provide critical insights into the molecular mechanisms governing hormone-induced cellular responses, proliferation, and differentiation in the gastrointestinal tract.
Gastrointestinal physiology modeling: In vitro and ex vivo preparations frequently employ Gastrin I to mimic physiological stimulation of parietal cells and enterochromaffin-like cells, allowing for detailed analysis of acid secretion, histamine release, and mucosal adaptation. Such models are instrumental in elucidating the regulatory networks that maintain gastric homeostasis and in exploring the adaptive responses of the stomach to various physiological and pathological stimuli.
Peptide structure-function analysis: The defined amino acid sequence and post-translational modifications of Gastrin I make it an ideal reference compound for structure-activity relationship (SAR) studies. By synthesizing and testing analogs or truncated variants, researchers can identify essential residues for receptor binding and biological activity, facilitating the rational design of novel peptide ligands or antagonists for investigative or industrial applications.
Analytical method development: Gastrin I is frequently employed as a standard or calibrator in the development and validation of immunoassays, chromatographic techniques, and mass spectrometry protocols aimed at quantifying endogenous gastrin levels. Its use enhances the accuracy and reliability of analytical workflows, supporting both basic research and applied studies in gastrointestinal peptide biochemistry.
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