Disclaimer: All products are for laboratory research only and not for human or animal use or consumption. For in-vitro research by qualified professionals only

Disclaimer: All products are for laboratory research only and not for human or animal use or consumption. For in-vitro research by qualified professionals only

Oxytocin

$64.90

CAS #: 50-56-6
Molecular Formula: C₄₃H₆₆N₁₂O₁₂S₂
Molecular Weight (M.W.): 1007.2 g/mol
Sequence: Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH₂
One-Letter Sequence: CYIQNCPLG
Structural Representation: H-Cys(1)-Tyr-Ile-Gln-Asn-Cys(1)-Pro-Leu-Gly-NH₂
Product Type: Cyclic Research Nonapeptide

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Description

Product Description

Oxytocin is a cyclic nine-amino-acid peptide supplied for controlled laboratory and analytical research. Its defined structure includes a disulfide linkage between the cysteine residues at positions 1 and 6, creating the molecule’s characteristic cyclic portion.

The peptide also contains a C-terminal glycinamide group. These structural features are important for accurate chemical identification and should be considered when comparing analytical or sequence data.

Oxytocin may be used in non-clinical scientific research involving peptide characterization, receptor-associated biochemical systems, molecular interactions, structural analysis, and related experimental models.

Research Applications

Oxytocin may be examined in controlled scientific environments involving:

  • Cyclic peptide characterization
  • Ligand-receptor interaction research
  • Molecular signaling studies
  • Peptide structure-function analysis
  • Biochemical interaction studies
  • Analytical peptide comparison
  • Stability and structural investigations
  • Non-clinical cellular models

Any observations should remain limited to the specific experimental design and should not be interpreted as demonstrating therapeutic, behavioral, reproductive, or clinical effects in humans.

Structural Information

Oxytocin consists of nine amino-acid residues:

Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH₂

One-letter representation:

CYIQNCPLG

The cysteine residues at positions 1 and 6 form an intramolecular disulfide bridge, producing the cyclic peptide structure. The C-terminal glycine is amidated.

Analytical Identification

Analytical characterization may include:

  • Peptide identity confirmation
  • Sequence verification
  • Molecular mass analysis
  • Disulfide-bond characterization
  • Chromatographic purity assessment
  • Structural testing
  • Lot-specific analytical analysis

Care should be taken to distinguish standard amidated oxytocin from alternative forms such as oxytocin free acid, which has different molecular specifications.

Specifications & Documentation

Lot-specific documentation should be reviewed for:

  • Compound identity
  • Peptide sequence
  • Molecular formula
  • Molecular weight
  • Disulfide configuration
  • Salt or counter-ion form
  • Purity specification
  • Analytical testing
  • Lot or batch information
  • Certificate of Analysis
  • Storage requirements

Authenticated product documentation should take precedence if the supplied form differs from the standard reference structure.

Storage & Handling

Store according to the conditions specified on the product label and Certificate of Analysis. Protect the material from environmental conditions that may compromise peptide integrity.

Follow established laboratory procedures appropriate for research peptides.

Research Use Only

Oxytocin is supplied exclusively for laboratory research, analytical testing, and scientific reference purposes.

Disclaimer

For research use only. Not for human or veterinary use. Not intended for consumption, administration, reproductive use, behavioral use, diagnosis, treatment, mitigation, cure, or prevention of any disease. No therapeutic, hormonal, reproductive, medical, or clinical claims are made or implied. Product information is supplied solely for scientific identification, documentation, and research reference.

Additional information

dose

5mg

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