Guanylin (rat, mouse) features a compact peptide stabilized by disulfide bonds that support studies of receptor-associated pathways. Its structural rigidity facilitates probing of conformation-dependent signaling events. Researchers analyze its folding, charge distribution, and solvent interactions. Use spans toxin-motif analysis, regulatory-peptide modeling, and molecular recognition studies.
CAT No: R2634
CAS No:145257-03-0
Synonyms/Alias:Guanylin (rat, mouse);144940-98-7;Guanylin (mouse, rat);GUANYLIN (RAT);Guanylin, rat, mouse;145257-03-0;Guanylin(rat,mouse);MFCD00187932;HY-P5077;DA-53780;CS-0675969;
Guanylin (rat, mouse) is a naturally occurring peptide hormone found in the intestinal tract of rodents, where it plays a pivotal role in regulating electrolyte and fluid balance through the modulation of guanylate cyclase C (GC-C) signaling pathways. As a member of the guanylin peptide family, it is structurally characterized by specific disulfide bonds that are critical for its biological activity. The compound is widely recognized for its involvement in intestinal homeostasis, making it a valuable tool for researchers investigating gastrointestinal physiology, peptide signaling mechanisms, and related cellular processes. Its relevance extends to studies of epithelial function, signal transduction, and the broader exploration of peptide-mediated regulatory networks in mammalian systems.
Peptide signaling research: Guanylin peptides are instrumental in elucidating the molecular mechanisms underlying GC-C receptor activation and downstream cGMP signaling. By serving as a selective agonist in experimental systems, the compound enables detailed investigations into the regulatory effects on ion transport, water secretion, and the maintenance of epithelial barrier integrity. Researchers utilize it to dissect the complex interplay between peptide hormones and their receptors, providing insights into the physiological control of electrolyte balance in the gastrointestinal tract.
Intestinal physiology studies: In rodent models, guanylin facilitates the exploration of fluid and electrolyte transport across intestinal epithelia. Experimental application of the peptide allows for the assessment of transepithelial chloride and bicarbonate secretion, shedding light on the hormonal regulation of intestinal fluid movement. These studies are essential for understanding the fundamental processes that govern nutrient absorption, mucosal hydration, and the prevention of dysregulated secretion associated with disease states.
Peptide structure-function analysis: The defined primary and secondary structure of guanylin makes it an ideal candidate for probing the relationship between peptide conformation and biological activity. Researchers employ synthetic and recombinant forms of the molecule to perform mutagenesis, analog development, and structure-activity relationship studies. Such work is critical for identifying key residues involved in receptor binding and activation, as well as for designing novel peptide analogs with tailored functional profiles.
Cell signaling pathway elucidation: Guanylin is frequently used to activate the GC-C/cGMP pathway in cultured cells and tissue preparations, providing a controlled means of studying downstream signaling cascades. Through its specific action on guanylate cyclase C, the peptide helps clarify the roles of cGMP-dependent protein kinases, ion channels, and phosphodiesterases in modulating cellular responses. These investigations contribute to a broader understanding of how extracellular peptides orchestrate intracellular signaling events in epithelial and non-epithelial contexts.
Comparative endocrinology: The availability of guanylin from rat and mouse sources supports comparative studies aimed at delineating species-specific differences in peptide signaling and physiological regulation. By examining its activity across different rodent models, scientists can investigate evolutionary adaptations in hormone function, receptor specificity, and the conservation of regulatory pathways. Such comparative analyses are invaluable for translating basic findings from animal models to broader mammalian systems and for refining experimental approaches in gastrointestinal research.
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