Urotensin II (114-124), human

Urotensin II (114-124), human is a synthetic peptide fragment corresponding to amino acid residues 114 through 124 of the human urotensin II precursor. As a member of the urotensin peptide family, this sequence represents the biologically active region implicated in the modulation of cardiovascular, renal, and neuroendocrine functions in various species. The peptide is of particular interest for researchers investigating the molecular mechanisms of peptide-receptor interactions, signal transduction pathways, and physiological regulation mediated by urotensin II and its receptor, UT (GPR14). Its defined sequence and conserved structure make it a valuable tool for dissecting the functional domains responsible for ligand activity and receptor specificity in both fundamental and applied biochemical research.

Receptor binding studies: The synthetic peptide serves as a critical reagent for the characterization of urotensin II receptor (UT) binding properties. By employing radioligand binding assays or fluorescence-based detection methods, researchers can use this fragment to quantify receptor affinity, elucidate binding kinetics, and map the structural determinants necessary for high-affinity interactions. Such studies are essential for advancing the understanding of G protein-coupled receptor pharmacology and for the development of selective agonists or antagonists targeting the urotensinergic system.

Signal transduction research: Urotensin II (114-124), human is widely utilized in investigations of downstream signaling events following UT receptor activation. Its application in cellular assays enables the assessment of intracellular calcium mobilization, phosphorylation cascades, and second messenger production in response to peptide stimulation. These experiments provide insights into the coupling efficiency, pathway selectivity, and regulatory mechanisms associated with urotensin II-mediated signaling, facilitating the dissection of complex physiological responses.

Structure-activity relationship (SAR) analysis: The defined sequence of this peptide fragment allows for systematic exploration of structure-activity relationships within the urotensin II family. By comparing the biological activity of full-length versus truncated or modified peptides, researchers can identify critical residues responsible for receptor activation, potency, and selectivity. Such SAR studies inform the rational design of novel peptide analogs with tailored pharmacological profiles, supporting both basic research and drug discovery initiatives.

Vascular and smooth muscle studies: The peptide is frequently employed in ex vivo and in vitro models to examine its direct effects on vascular tone and smooth muscle contractility. By applying the peptide to isolated tissue preparations, investigators can assess concentration-dependent responses, characterize receptor-mediated contractile mechanisms, and elucidate the role of urotensin II in vascular pathophysiology. These studies contribute to a broader understanding of peptide-regulated hemodynamics and may inform the identification of new targets for modulating vascular function.

Neuroendocrine system investigations: Urotensin II (114-124), human is also valuable for probing the regulatory functions of the urotensinergic system within neuroendocrine tissues. Its use in neuronal or endocrine cell models enables the study of peptide-induced secretion, gene expression changes, and receptor signaling dynamics. Such research aids in clarifying the physiological significance of urotensin II in neuroendocrine integration, stress responses, and hormonal regulation, supporting a comprehensive view of peptide-mediated control mechanisms in mammalian systems.

1. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists

2. C-peptide and its C-terminal fragments improve erythrocyte deformability in type 1 diabetes patients

3. Multifunctional peptide-oligonucleotide conjugate promoted sensitive electrochemical biosensing of cardiac troponin I

4. Investigating Potential Interactions Between Neurohypophyseal Peptides, their Drug Analogs, and Coagulation Factor VIII

5. An Isolated TCR αβ Restricted by HLA-A* 02: 01/CT37 Peptide Redirecting CD8+ T Cells to Kill and Secrete IFN-γ in Response to Lung Adenocarcinoma Cell Lines