Urotensin II (114-124), human TFA, an 11-amino acid residue peptide, is a potent vasoconstrictor and agonist for the orphan receptor GPR14.
CAT No: R1744
Urotensin II (114-124), human TFA is a synthetic peptide fragment corresponding to amino acid residues 114 to 124 of the human urotensin II sequence, supplied as the trifluoroacetate salt. As a bioactive peptide, it represents a critical portion of the full-length urotensin II, a well-characterized cyclic peptide hormone implicated in diverse physiological functions, particularly within the cardiovascular and nervous systems. The 114-124 fragment is of significant interest for researchers investigating the structure-activity relationships of urotensin II, as well as those studying G protein-coupled receptor (GPCR) signaling and peptide-receptor interactions. Its defined sequence and human origin make it a valuable tool for probing the functional domains of urotensin II and for developing targeted assays in peptide pharmacology and biochemistry.
Peptide receptor studies: The urotensin II (114-124) fragment is widely employed in studies aimed at elucidating the binding properties and activation mechanisms of the urotensin II receptor (UT, also known as GPR14). By isolating the C-terminal active core, researchers can dissect the minimal structural features necessary for receptor recognition and activation, facilitating a deeper understanding of ligand-receptor specificity and affinity. This application is crucial for mapping receptor-ligand interactions and for the rational design of receptor modulators.
Structure-activity relationship (SAR) analysis: The defined sequence of this peptide fragment enables detailed SAR investigations, allowing scientists to systematically modify residues within the 114-124 region and assess the impact on biological activity. Such studies are instrumental in identifying key amino acids responsible for receptor binding and downstream signaling, providing a foundation for the development of novel peptide analogs with altered potency or selectivity. SAR data derived from this fragment inform both basic biochemical research and applied drug discovery efforts.
Peptide synthesis and assay development: As a synthetic standard, the 114-124 sequence serves as a reference material in peptide synthesis optimization and analytical method validation. Its well-characterized properties support the calibration of chromatographic and mass spectrometric assays, ensuring reliable peptide quantification and purity assessment. Additionally, it is frequently used as a positive control in bioassays designed to monitor urotensin II-like activity, contributing to assay reproducibility and comparability across laboratories.
Signal transduction research: The ability of the urotensin II (114-124) fragment to activate or modulate GPCR-mediated pathways makes it a valuable probe in cellular signaling studies. By applying this peptide to cell-based systems, researchers can investigate downstream effects such as intracellular calcium mobilization, second messenger generation, or kinase activation. These experiments help delineate the specific signaling cascades triggered by urotensin II receptor engagement and offer insights into the physiological and pathophysiological roles of this peptide system.
Comparative pharmacology and species specificity: The human-derived 114-124 fragment facilitates comparative studies across different species and peptide variants, enabling the assessment of evolutionary conservation and species-dependent pharmacological responses. Such investigations are essential for understanding the translational relevance of animal models and for identifying interspecies differences in receptor activation profiles. This comparative approach aids in the selection of appropriate experimental systems and informs the broader field of peptide hormone research.
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