Urotensin I is, 41-aa neuropeptide, acts as an agonist of CRF receptor with pEC50s of 11.46, 9.36 and 9.85 for human CRF1, human CRF2 and rat CRF2α receptors in CHO cells, and Kis of 0.4, 1.8, and 5.7 nM for hCRF1, rCRF2α and mCRF2β receptors, respectively.
CAT No: R1742
CAS No:83930-33-0
Synonyms/Alias:Urotensin I;9047-54-5;83930-33-0;DTXSID90238178;DTXCID10160669;DA-68500;
Urotensin I is a naturally occurring peptide hormone primarily recognized for its role in vertebrate neuroendocrine regulation. As a member of the corticotropin-releasing factor (CRF) peptide family, it is structurally and functionally related to urotensin II, but displays distinct biological activities, especially in fish and amphibian species. Urotensin I is notable for its involvement in modulating stress responses, osmoregulation, and cardiovascular function, making it a valuable tool for advancing biochemical and physiological research. Its unique receptor binding profile and evolutionary conservation across species have established it as a critical molecule for dissecting neuropeptide signaling pathways and their physiological consequences.
Neuroendocrine signaling research: Urotensin I serves as a robust model peptide for investigating the molecular mechanisms underlying neuroendocrine communication. Its ability to activate specific G protein-coupled receptors (GPCRs) allows researchers to explore downstream signaling cascades that regulate the hypothalamic-pituitary-interrenal (HPI) axis in non-mammalian vertebrates. By applying this peptide in in vitro and in vivo systems, scientists can elucidate the cross-talk between stress hormones and other neuropeptides, providing insights into the integration of environmental and physiological cues at the molecular level.
Comparative physiology studies: As a conserved peptide across various vertebrate taxa, Urotensin I is instrumental in comparative endocrinology. Its use enables the characterization of evolutionary adaptations in stress and osmoregulatory systems, particularly in aquatic organisms. By examining its effects on ion transport, water balance, and pituitary hormone release, researchers can better understand the evolutionary pressures that shaped endocrine regulation in diverse environmental contexts.
Receptor pharmacology and ligand-receptor interaction assays: The peptide's high affinity for CRF-related receptors makes it an essential ligand for receptor binding studies. Researchers utilize it to map receptor distribution, determine ligand specificity, and analyze downstream signaling events in both native tissues and recombinant expression systems. These investigations are foundational for delineating the structure-activity relationships that govern peptide-receptor interactions and for identifying potential modulators of neuropeptide signaling.
Peptide synthesis and structural biology: Urotensin I is frequently employed as a reference molecule in peptide synthesis protocols and structural studies. Its defined sequence and physiological relevance make it a benchmark for optimizing solid-phase peptide synthesis, purification strategies, and analytical characterization methods. Furthermore, it is used in conformational analyses, such as NMR and crystallography, to explore the structural determinants of bioactivity and receptor engagement.
Functional assays in stress and osmoregulatory models: The peptide is widely used in experimental models to assess its role in modulating stress-induced hormonal release and osmoregulatory processes. By administering it to cultured cells, organ explants, or whole organisms, researchers can quantify changes in cortisol secretion, ion transporter expression, and other physiological endpoints. These functional assays are essential for dissecting the mechanisms by which neuropeptides orchestrate complex adaptive responses to environmental and internal stressors.
2. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
3. Emu oil in combination with other active ingredients for treating skin imperfections
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