
Oxytocin is a nine-residue cyclic peptide synthesised in the hypothalamus and released from the posterior pituitary. A disulfide bridge between Cys1 and Cys6 closes a six-residue ring with a three-residue tail, the conformation its receptor recognises. It acts on the oxytocin receptor, a class-A GPCR coupling through Gq to phospholipase C and intracellular calcium release. Research contexts divide between peripheral smooth-muscle work and central studies of social recognition and affiliative behaviour, where its close structural relationship to vasopressin — the two differ at only two residues — is a recurring subject.
Learn more about the science →LC-MS identity, HPLC purity, mass spec confirmation, endotoxin by LAL, appearance. Third-party ISO-17025 verified.
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Two residues. Both are cyclic nonapeptides sharing the Cys1–Cys6 disulfide architecture, differing at positions 3 and 8, which is enough to separate their receptor selectivity — and enough that cross-reactivity is a documented consideration in assay design.
Neuro collects cofactors and peptides studied for neural work. Oxytocin is synthesised in the hypothalamus and much of its published research concerns central signalling rather than its peripheral role.
Oxytocin is potent by mass and the published research concentrations are low, so a 2mg vial covers more protocol than the size suggests.
Mass spec against 1,007.19 g/mol, plus confirmation that the disulfide is intact — a reduced peptide has the same sequence and a different mass.
Provided for context only. None of the studies cited below evaluate hábit material specifically; they document the published literature on the compound and its mechanism. Research-use claims are not therapeutic claims.
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“COA matched what we ran in-house. Powder reconstituted clean, no haze. Did exactly what we needed it to.”
“Switched after two bad lots from a previous source. Three orders in, zero issues.”
“Asked support a purity question and got the raw HPLC trace back within the hour. That transparency is why we reorder.”