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 peptide hormone primarily expressed in the intestinal epithelium of rodents, where it plays a key role in regulating electrolyte and water transport. Structurally, it belongs to the family of natriuretic peptides and is characterized by its cysteine-rich sequence, which enables the formation of specific disulfide bonds crucial for its biological activity. The peptide exerts its effects by binding to and activating the guanylate cyclase-C (GC-C) receptor, a pivotal step in modulating cyclic GMP production within target cells. Researchers value Guanylin for its high specificity and functional relevance in gastrointestinal physiology, making it an indispensable tool for studies focused on fluid homeostasis, epithelial cell signaling, and intestinal health. Its conserved sequence across rat and mouse models ensures consistency in experimental outcomes, facilitating translational research and comparative analyses across species.
Intestinal Physiology Research: Guanylin serves as an essential molecular probe in studies investigating the mechanisms underlying intestinal fluid and electrolyte secretion. By mimicking endogenous hormone action, it enables researchers to elucidate the signaling pathways that regulate chloride and bicarbonate transport in the gut epithelium. This application is particularly valuable for dissecting the molecular basis of diarrheal diseases, as well as for exploring the physiological roles of GC-C signaling in maintaining intestinal hydration and barrier function. Through in vitro or ex vivo assays, scientists can apply Guanylin to cultured intestinal epithelial cells or tissue explants to observe changes in ion flux, cyclic GMP levels, and downstream effector activation, thereby advancing our understanding of gastrointestinal homeostasis.
Molecular Pharmacology: The peptide is widely used in the field of molecular pharmacology to study the interaction between peptide ligands and the GC-C receptor. By employing Guanylin in binding assays, signal transduction experiments, and receptor characterization studies, investigators can delineate the structural requirements for receptor activation and the dynamics of ligand-receptor interactions. This knowledge is instrumental in guiding the design of novel agonists or antagonists targeting the GC-C pathway, which has implications for modulating intestinal secretion and motility in preclinical models. The use of Guanylin as a reference ligand also aids in the validation of new pharmacological compounds, ensuring robust and reproducible assay systems.
Gastrointestinal Pathophysiology Models: In rodent models of gastrointestinal disorders, Guanylin is utilized to simulate or modulate disease-like conditions, such as secretory diarrhea or impaired fluid balance. By administering the peptide in vivo or in organoid cultures, researchers can induce alterations in gut secretion and investigate the compensatory mechanisms that restore homeostasis. These experimental approaches provide insights into the pathophysiological processes associated with disorders of fluid and electrolyte imbalance, enabling the identification of potential therapeutic targets and the evaluation of candidate interventions in a controlled setting.
Signal Transduction Research: The role of Guanylin in activating the cyclic GMP signaling cascade makes it a valuable tool for exploring broader aspects of intracellular signaling networks. Scientists leverage its ability to selectively stimulate GC-C receptors to dissect downstream pathways involved in cell proliferation, differentiation, and apoptosis within the intestinal epithelium. By integrating Guanylin into studies employing advanced imaging, gene expression analysis, and proteomics, researchers can map the intricate signaling events triggered by peptide-receptor interactions and uncover novel regulatory nodes relevant to intestinal physiology and disease.
Comparative Physiology and Evolutionary Biology: The conserved structure and function of Guanylin across different rodent species allow for comparative studies aimed at understanding the evolution of natriuretic peptides and their physiological roles. Researchers utilize the peptide to investigate species-specific variations in GC-C receptor expression, ligand affinity, and downstream signaling responses. Such comparative analyses contribute to our knowledge of evolutionary adaptations in electrolyte regulation and provide a foundation for cross-species extrapolation of experimental findings. Collectively, these applications underscore the versatility of Guanylin (rat, mouse) as a research tool, supporting advancements in basic science, pharmacology, and translational studies focused on intestinal health and homeostasis.
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