Oxytocin 5mg
Oxytocin (Oxt) is a synthetic cyclic nonapeptide (CYIQNCPLG-NH₂, CAS 50-56-6, MW 1007.19) supplied as a ≥99% HPLC-UV-tested lyophilized powder, 5 mg net peptide per vial, for in-vitro and laboratory research applications only. Research Use Only — not for human or veterinary use.
$34.00
| Quantity | Price | Discount |
|---|---|---|
| 5-10 | $32.64 | 4% |
| 11-15 | $31.28 | 8% |
| 16-20 | $29.92 | 12% |
| 21+ | $28.56 | 16% |
🧬 99%+ HPLC Purity
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Oxytocin is a synthetic cyclic nonapeptide composed of nine amino acid residues in the sequence Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH₂ (CYIQNCPLG-NH₂), featuring an intramolecular disulfide bridge between the two cysteine residues and a C-terminal primary amide. It is structurally classified within the neurohypophyseal nonapeptide family and is closely related to vasopressin, from which it differs by two amino acid residues.
This product is supplied as a lyophilized powder containing 5 mg net peptide per vial, synthesized by solid-phase peptide synthesis (SPPS) and characterized by HPLC-UV (purity) and LC-MS (identity). It is intended exclusively for in-vitro laboratory research and analytical applications.
In the research literature, oxytocin is referenced in the context of the oxytocin receptor (OXTR), a class A (rhodopsin-type) G-protein-coupled receptor, and is frequently used as a reference peptide in receptor-binding, structure-activity, and peptide-stability investigations.
| Compound Name | Oxytocin |
|---|---|
| Synonyms / Also Known As | Oxt, OT, α-Hypophamine |
| CAS Number | 50-56-6 |
| Molecular Formula | C₄₃H₆₆N₁₂O₁₂S₂ |
| Molecular Weight | 1007.19 g/mol |
| Sequence (1-letter) | CYIQNCPLG-NH₂ |
| Sequence (3-letter) | Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH₂ |
| Structure | Cyclic nonapeptide; disulfide bridge between Cys¹ and Cys⁶; C-terminal primary amide |
| Peptide Class | Neurohypophyseal nonapeptide |
| Purity | ≥99% (HPLC-UV) — Lot OXYT-162-TPL: 99.76% |
| Identity Confirmation | Confirmed by LC-MS |
| Appearance | White lyophilized powder |
| Solubility | Soluble in water; HPLC-grade water or 0.1% acetic acid recommended |
| Vial Contents | 5 mg net peptide (label); Lot OXYT-162-TPL net content 5.08 mg |
| Storage (lyophilized) | -20°C, sealed, protected from light/moisture |
| Storage (reconstituted) | 2–8°C short-term; aliquot & freeze -20°C for longer; avoid freeze-thaw cycles |
| Synthesis | Solid-phase peptide synthesis (SPPS) |
| Testing Lab | Freedom Diagnostics (third-party, USA) |
| Test Methods | Purity by HPLC-UV; identity by LC-MS |
| Lot Number | OXYT-162-TPL |
| Shipped From | USA |
| Certificate of Analysis | Lot-specific COA available — [LINK: Oxytocin Lot OXYT-162-TPL COA] |
Oxytocin — Frequently Asked Questions
What is oxytocin?
Oxytocin is a synthetic cyclic nonapeptide (CYIQNCPLG-NH₂) classified within the neurohypophyseal nonapeptide family. This product is supplied as a lyophilized powder for laboratory research use only.
What is the molecular weight and formula of oxytocin?
Oxytocin has a molecular weight of approximately 1007.19 g/mol and the molecular formula C₄₃H₆₆N₁₂O₁₂S₂ (CAS 50-56-6).
What is the amino acid sequence of oxytocin?
The sequence is Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH₂ (CYIQNCPLG-NH₂), with a disulfide bridge between the two cysteine residues.
What purity is this oxytocin?
This product is ≥99% pure as verified by HPLC-UV, with identity confirmed by LC-MS. The most recent lot (OXYT-162-TPL) tested at 99.76% purity. A lot-specific Certificate of Analysis from a third-party laboratory is available.
How should oxytocin be stored?
Store lyophilized material sealed at -20°C, protected from light and moisture. After reconstitution, store at 2–8°C for short-term use or aliquot and freeze at -20°C, avoiding repeated freeze-thaw cycles.
Is a Certificate of Analysis (COA) available?
Yes. Each lot has a Certificate of Analysis from Freedom Diagnostics, an independent third-party laboratory, documenting HPLC-UV purity and LC-MS identity confirmation, tied to the vial lot number.
Where is this product made and how does it ship?
This research compound is supplied for research use only and ships within the USA. See our shipping information for current options and delivery times.
Research Context
The following describes investigative contexts in which oxytocin appears in the scientific literature. Provided for scientific background only; this does not describe any product use.
- Receptor-interaction studies — as a reference ligand in OXTR binding and class A GPCR signaling models.
Structure–activity relationship (SAR) research — its compact disulfide-bridged scaffold is common in peptide analog-design studies. - Peptide stability & formulation research — studied for disulfide stability, oxidative degradation, aggregation, and lyophilization behavior.
- Comparative neuropeptide studies — frequently compared with vasopressin due to the two-residue structural difference.
- Analytical method development — used as a nonapeptide model compound in HPLC, qNMR, and amino-acid-analysis quantitation studies.
For laboratory research handling only.
Reconstitution. Reconstitution solvent should be selected according to your experimental protocol and stability requirements. Common research-grade options include HPLC-grade ultrapure water or dilute acetic acid; for assays requiring multi-day stability from a single vial, some laboratories select preservative-containing sterile water. Validate compatibility with your assay system before use. Add solvent slowly down the vial wall; do not shake vigorously, and allow to dissolve fully before use.
Storage — lyophilized. Store sealed at -20°C, protected from light and moisture. Lyophilized oxytocin is resistant but hygroscopic; keep desiccated and open only at equilibrated temperature to prevent condensation on the cold powder.
Storage — reconstituted. Store at 2–8°C for short-term use, or aliquot and freeze at -20°C for longer-term storage. Avoid repeated freeze-thaw cycles. Solutions degrade faster at room temperature.
Handling notes. Metal ions in some buffers/water can catalyze oxidative degradation of the disulfide bridge; HPLC-grade water (or chelating agents such as EDTA where compatible) reduces this risk. Determine working concentrations using your own validated laboratory methods.
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