[Arg8]-Vasotocin (TFA) is a vertebrate neurohypophyseal peptide of the vasopressin/oxytocin hormone family.
CAT No: R1115
[Arg8]-Vasotocin TFA is a synthetic peptide analog structurally related to the neurohypophyseal nonapeptides vasotocin and vasopressin. Characterized by the substitution of arginine at the eighth position, this compound exhibits high sequence homology to vasotocin found in non-mammalian vertebrates and shares functional similarities with mammalian vasopressin and oxytocin. Its unique structure and receptor interactions make it a valuable tool in neuroendocrinology, comparative physiology, and receptor pharmacology research, enabling the exploration of peptide hormone signaling across diverse biological systems.
Receptor characterization: Researchers frequently employ [Arg8]-vasotocin analogs to investigate the binding properties and functional selectivity of vasopressin and oxytocin receptor subtypes. By utilizing this peptide in receptor binding assays, scientists can delineate ligand-receptor interactions, assess receptor affinity, and map the pharmacological profiles of neurohypophyseal hormone receptors in both mammalian and non-mammalian tissues. Such studies are essential for understanding the evolutionary divergence and conservation of peptide hormone signaling pathways.
Neuroendocrine signaling studies: As a potent mimic of endogenous vasotocin, [Arg8]-vasotocin provides a precise means to probe the physiological roles of neuropeptides in the regulation of social behavior, stress response, and osmoregulation. Experimental application in in vitro or ex vivo tissue preparations allows for the dissection of peptide-mediated signaling cascades, facilitating the identification of downstream effectors and second messenger systems involved in neuroendocrine regulation.
Comparative physiology research: The evolutionary conservation of vasotocin-like peptides makes this analog particularly useful in comparative studies across vertebrate species. By applying [Arg8]-vasotocin in model organisms such as fish, amphibians, and birds, investigators can elucidate the functional parallels and distinctions between non-mammalian vasotocin and mammalian vasopressin or oxytocin systems. These insights contribute to a broader understanding of vertebrate endocrine evolution and adaptive physiology.
Peptide structure-activity relationship analysis: The defined sequence and specific arginine substitution in [Arg8]-vasotocin enable systematic studies of structure-activity relationships among neuropeptides. Synthetic analogs such as this are instrumental in mapping critical residues responsible for receptor activation, signal transduction, and biological potency. Such analyses inform rational peptide design and the development of novel analogs with tailored receptor selectivity or activity profiles for biochemical research.
Analytical reference standard: Due to its well-characterized structure and defined peptide sequence, [Arg8]-vasotocin serves as a reliable reference standard in peptide quantification assays, chromatographic method development, and mass spectrometric analyses. Its use ensures accuracy and reproducibility in the identification and quantification of related neuropeptides in complex biological samples, supporting rigorous analytical workflows in peptide research laboratories.
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