Description

Oxytocin peptide (CAS 50-56-6) is a cyclic nonapeptide with the sequence Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH₂ and an intramolecular disulfide bridge between Cys1 and Cys6. This listing is for research-grade oxytocin peptide supplied as a 10mg lyophilized powder at ≥99% purity by HPLC. For laboratory research use only. Not for human consumption, veterinary use, food, or therapeutic use. Not a drug, supplement, or cosmetic. Sold exclusively to qualified research professionals and institutions.

About Oxytocin
Oxytocin is a nonapeptide first chemically synthesized and characterized by du Vigneaud and colleagues in the 1950s [1]. Its structure consists of nine amino acid residues with a C-terminal glycinamide and a disulfide-linked ring formed by cysteine residues at positions 1 and 6, yielding a six-residue cyclic portion and a three-residue acyclic tail. Researchers have characterized oxytocin as a member of the neurohypophysial nonapeptide family, structurally related to vasopressin and differing at two residue positions.

Research Background
Oxytocin has been referenced extensively in the published literature across in vitro and animal model systems. The oxytocin receptor (OTR) and its associated signaling pathways have been characterized in cell culture and isolated tissue preparations. In rodent models, oxytocin has been studied in the context of conspecific recognition, parental behavior, and pair-bond formation, including comparative work in monogamous and polygamous vole species used to map receptor distribution and Neuropeptidergic circuitry. The compound has also been investigated in isolated smooth muscle preparations examining contractility mechanisms. These references describe findings in non-human models and in vitro systems and do not constitute claims about effects in humans.