Oxytocin Acetate for Laboratory Research

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≥ 99 % purity (HPLC)

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What is Oxytocin Acetate for Laboratory Research

Oxytocin Acetate for Laboratory Research at a glance

Oxytocin acetate is the acetate salt of a cyclic, C-terminally amidated nonapeptide. Its defining structural feature is a Cys1-Cys6 disulfide bridge. The free base and the oxytocin acetate salt carry separate identity records: the monoacetate is recorded as oxytocin CAS 6233-83-6, the free base as CAS 50-56-6. A database record does not identify the form of a received batch, and salt equivalence, peptide content and purity remain properties of the documented batch.

This reagent is supplied strictly for laboratory research and is not for use in humans or animals. Product identity and analytical results require matching product, batch and COA documentation with the chemical form stated consistently.

Research overview

Oxytocin acetate is a cyclic, amidated nonapeptide associated with the oxytocin receptor, OXTR, a G-protein-coupled receptor. The oxytocin peptide sequence comprises nine amino-acid residues, Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH2, placing the compound in the structural class of an oxytocin nonapeptide. Acetate is a counterion rather than an additional amino-acid residue, so gross salt mass and peptide content are not interchangeable.

The cited literature covers human receptor cloning and structure, cell-based receptor pharmacology, a preclinical rat model, a human imaging study and an observational human cohort. Every observation remains limited to its stated material, model, method and endpoint and does not establish a characteristic of supplied reagent.

Chemical identity, biological findings and batch analysis are separate evidence layers. HPLC can report a method-specific chromatographic result for the analysed batch, while MS can support molecular identity. Neither method alone answers every identity question.

For laboratory procurement, the label, specification and COA should consistently identify the acetate form and analysed batch. Physical form and binding storage conditions require confirmation against the applicable approved product and batch records.

Technical data
CAS number50-56-6
SummenformelC₄₃H₆₆N₁₂O₁₂S₂
Molekulargewicht1007,2 g/mol
SequenzCys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH₂ (Disulfid Cys1-Cys6)
Amino acids9
Purity≥ 99 % (HPLC)
PubChem CID439302
Target structureHuman OXTR receptor identity and seven-transmembrane architecture in a human receptor expression-cloning study; human OXTR structure in complex with a nonpeptide antagonist, receptor-associated cholesterol and Mg2+ coordination in an in-vitro human receptor structural study; ligand binding and phosphoinositide turnover in transiently transfected COS-7 cells with an ovine endometrial OXTR construct; human OXTR properties in cholesterol-rich versus cholesterol-poor membrane fractions in an in-vitro membrane study of human receptor expressed in HEK293 cells; recruitment of G-protein subtypes in comparisons of structurally modified peptide ligands in biosensor-based in-vitro pharmacology at human OXTR; amygdala activation and amygdala-to-brainstem coupling in a human imaging study with paradigm-bound signals; basal and experimentally induced HPA-axis activity, including work concerning the paraventricular nucleus, in a preclinical rat model; associations between endogenous oxytocin measurements and cortisol-related HPA-axis reactivity in a human cohort study of endogenous measurements; identity and analytical endpoints comprising the sequence, Cys1-Cys6 disulfide bridge and amidated C-terminus assessed together, separate free-base and acetate-salt records for formula, mass, CAS and PubChem, reconciliation of label, specification, batch code and COA, HPLC purity as a batch- and method-specific value, and MS as complementary identity evidence
Molekülstruktur
Oxytocin Acetate for Laboratory Research
In vitroAnimal modelHuman pilot4RCT5Approval
OXTR molecular identity
Receptor structure
Cell-based pharmacology
Model-qualified biological literature
Batch documentation

Evidence

Research highlights

An expression-cloning study reported a seven-transmembrane G-protein-coupled receptor architecture for human OXTR.

Kimura et al. 1992 · PMID 1313946

A crystallography study resolved human OXTR in complex with a nonpeptide antagonist under the reported structural conditions.

Waltenspühl et al. 2020 · PMID 32832646

Transfected-cell studies examined ligand binding, phosphoinositide turnover, membrane-domain properties and G-protein subtype engagement in defined OXTR systems.

Riley et al. 1996 · PMID 8691097 · Gimpl et al. 2000 · PMID 10785367 · Busnelli et al. 2012 · PMID 22069312

Human imaging, a preclinical rat model and an observational human cohort address distinct endpoints that cannot be treated as equivalent or as batch evidence.

Kirsch et al. 2005 · PMID 16339042 · Neumann et al. 2000 · PMID 10718919 · Cox et al. 2015 · PMID 25768266

Identity, salt form, content and analytical results must refer to the same analysed batch; purity claims apply only to that batch and method.

Reborn batch documentation · COA with HPLC and MS

Research Deep Dive

The research in depth

Model-qualified findings in depth — every claim tied to a PubMed-indexed source.

9 residuesDefined peptide sequence
2 identity recordsFree base and monoacetate
Cys1–Cys6Disulfide bridge
8 sourcesModel-qualified evidence map
01Molecular identity: a cyclic, amidated nonapeptide

Oxytocin acetate is the acetate salt of a cyclic, C-terminally amidated nonapeptide. The defined sequence contains nine amino-acid residues. Its Cys1–Cys6 disulfide closes a six-residue ring, while the short C-terminal segment ends in glycinamide. The disulfide bridge and terminal amide are integral parts of the covalent identity, not presentation details.

FieldReference specification
NameOxytocin Acetate
ClassCyclic nonapeptide; Cys1–Cys6 disulfide; C-terminally amidated
SequenceCys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH2 (CYIQNCPLG-NH2)
Disulfide bridgeCys1–Cys6
C-terminusAmidated
Molecular formula, free baseC43H66N12O12S2, free base
Average molecular mass, free base1007.2 g/mol, free base
CAS, free base50-56-6, free base
PubChem CID, free base439302, free base
Molecular formula, monoacetateC45H70N12O14S2, monoacetate salt
Average molecular mass, monoacetate1067.2 g/mol, monoacetate salt
CAS, acetate salt6233-83-6, acetate salt
PubChem CID, monoacetate12004215, monoacetate salt
Receptor research targetOxytocin receptor (OXTR), GPCR
Salt stoichiometry / peptide contentBatch-specific; to be confirmed against applicable quality documentation

The free-base formula and average mass differ from the monoacetate-salt formula and average mass by one equivalent of acetic acid. These paired database identities do not establish which form is present in received material. A product designation, chemical form, batch code and applicable documentation should therefore remain connected.

Identity source: Kimura et al. 1992 · PMID 1313946

02Free base against acetate salt: why the records stay apart

Acetate is a counterion rather than an additional amino-acid residue. Gross salt mass and peptide content are consequently not interchangeable quantities. Documented water and other recorded components can also affect material balance. Any quantitative interpretation should follow the batch-specific assay and applicable quality documentation rather than the theoretical formula alone.

Two records

The free base and monoacetate salt retain separate formulae, average masses, CAS identifiers and PubChem records. Each value must stay assigned to its stated molecular form.

Covalent identity

Reduction changes the disulfide-defined covalent structure. Oxidation conditions may affect disulfide state and permit additional species such as dimers, without establishing their presence in any particular batch.

Analytical boundary

Changes in molecular state or associated impurities can change chromatographic retention. This is an analytical consideration, not a finding about supplied material.

HPLC may document a method-specific chromatographic result for the tested batch, while MS may support molecular identity when recorded for that batch. Neither method answers every question alone. The useful documentary chain connects the batch, method, result and acceptance criterion, while maintaining the distinction between free-base identity and acetate-salt composition.

Study source: Riley et al. 1996 · PMID 8691097

03Study landscape

This section describes findings in controlled research and makes no statement about use. The records progress chronologically across eight distinct evidence settings. Model, material, method and measured endpoint delimit every entry.

Human receptor cloning
Kimura et al., 1992, Nature

A human receptor expression-cloning study measured isolation of human OXTR cDNA and assigned seven-transmembrane GPCR receptor architecture.

PMID 1313946
In-vitro ovine receptor
Riley et al., 1996, Journal of Endocrinology

An in-vitro ovine receptor pharmacology study measured ligand binding and phosphoinositide turnover for an ovine endometrial OXTR construct in transiently transfected COS-7 cells.

PMID 8691097
Preclinical rat model
Neumann et al., 2000, Journal of Neuroendocrinology

A preclinical rat model measured basal and experimentally induced HPA-axis activity in male and female rats, including work concerning the paraventricular nucleus.

PMID 10718919
Human receptor membranes
Gimpl and Fahrenholz, 2000, European Journal of Biochemistry

An in-vitro human receptor membrane study measured OXTR properties in cholesterol-rich and cholesterol-poor membrane fractions using a modified receptor expressed in HEK293 cells.

PMID 10785367
Human neuroimaging
Kirsch et al., 2005, The Journal of Neuroscience

A human neuroimaging study measured model-specific changes in amygdala activation and amygdala-to-brainstem coupling.

PMID 16339042
Human receptor pharmacology
Busnelli et al., 2012, Journal of Biological Chemistry

An in-vitro human receptor pharmacology study used biosensors to measure recruitment of G-protein subtypes by oxytocin and structurally modified peptide ligands.

PMID 22069312
Endogenous human cohort
Cox et al., 2015, Psychoneuroendocrinology

A human cohort study of endogenous measurements assessed associations between endogenous oxytocin measurements and cortisol-related HPA-axis reactivity.

PMID 25768266
Human receptor structure
Waltenspühl et al., 2020, Science Advances

An in-vitro human receptor structural study measured human OXTR structure in complex with a nonpeptide antagonist, including receptor-associated cholesterol and Mg2+ coordination.

PMID 32832646

Study sources: the eight linked PubMed records above define this evidence map.

04What the evidence does not establish

A human receptor expression-cloning study and an in-vitro human receptor structural study address receptor architecture under their stated systems. In-vitro ovine receptor pharmacology and in-vitro human receptor pharmacology address assay-specific interactions or signalling measurements. Signals from a human neuroimaging study are indirect and study-specific. A preclinical rat model remains species- and design-bound. These evidence levels cannot be combined as though they were equivalent.

The human cohort study of endogenous measurements assessed endogenous oxytocin measurements and cortisol-related HPA-axis reactivity, and did not characterise externally supplied oxytocin acetate reagent. Endogenous measurement and an experiment with laboratory reagent answer different research questions. Likewise, a database identity describes a referenced molecular entity, study material belongs to a stated publication, and delivered material requires its own documentary chain.

The cited papers do not establish identity, purity, content, salt equivalence or physical form for supplied material. Agreement across biological observations cannot validate a commercial batch. Literature assignment should preserve molecule, model, method and endpoint; product-specific questions require the applicable label, released specification and batch documentation.

Oxytocin acetate is a cyclic nonapeptide associated with OXTR. Kisspeptin-10 is associated with KISS1R; DSIP is a linear nonapeptide without a disulfide ring; VIP is a C-terminally amidated 28-mer; Selank and Semax are neuropeptide fragments; and Thymosin Alpha-1 belongs to a separate peptide class. These are identity distinctions only. Their identifiers, analytical expectations and literature records do not transfer to oxytocin acetate.

Evidence-boundary sources: Kirsch et al. 2005 · PMID 16339042 · Cox et al. 2015 · PMID 25768266

05Form, batch documentation and research supply in the EU

Physical form, stated content, binding storage conditions and stability period remain open points to be established from the released product information and applicable batch documentation. No presentation, numerical content, temperature or stability interval is inferred from molecular literature or database identity.

The documentation chain should connect product designation, chemical form, batch code, analytical method and reported result. A batch COA should connect the product name and batch code to the stated tests. HPLC may provide a batch-specific chromatographic result, while MS may support identity if such evidence is reported. Any numerical purity applies only to the analysed batch and stated method.

Oxytocin acetate is supplied to laboratories in the EU as research material. Publications define research questions and model-qualified measurements; they do not certify delivered identity, content, physical form, purity, salt equivalence or stability. Those properties require reconciliation against the applicable label, released specification and batch documentation.

Research use only. For laboratory research only. Not for human or veterinary use. Not intended to diagnose, treat, cure or prevent any disease. Not a medicinal product, food or cosmetic.

FAQ

Frequently asked questions

What is oxytocin acetate?

Oxytocin acetate is the acetate salt of a cyclic, C-terminally amidated nonapeptide with a Cys1-Cys6 disulfide bridge.

What research target is associated with this peptide?

The literature associates the peptide with OXTR, a G-protein-coupled receptor. This target assignment does not promise an outcome in any experimental system.

Why must the free base and acetate salt be distinguished?

Publications on the oxytocin peptide frequently omit the salt form, and the two forms have different identity records. Labels, specifications and the COA should state the chemical form consistently, while salt equivalence and peptide content remain batch-specific.

What research models appear in the cited literature?

The literature includes receptor expression and structural systems, transfected-cell assays, a preclinical rat model, a human imaging study and an observational human cohort. Findings remain limited to each reported model.

Does the published literature verify a supplied batch?

No. Publications do not establish identity, purity, content, salt equivalence or physical form of supplied material; those properties require batch-specific analytical documentation.

How is this reagent classified?

It is supplied strictly for laboratory research and is not for use in humans or animals.

How are identity and purity documented?

MS can support molecular identity, and HPLC can report method-specific chromatographic purity for the analysed batch. Results must be read with the matching COA.

How can I pay?

We accept prepayment by SEPA bank transfer as well as cryptocurrencies. All payments are processed securely and encrypted.

How fast and how is it shipped?

Discreet shipping from the EU within 4–5 business days. Neutral packaging with no reference to the contents.