Product

Oxytocin Peptide | Oxytocin 2mg

Oxytocin nonapeptide cyclic, is used for calcium signaling and GPCR Pharmacology research. Purity≥99%. This product is for laboratory research use only.

Oxytocin Peptide Information

PropertyValue
NameOxytocin
CAS Number50-56-6
Peptide SequenceCYIQNCPLG
Molecular FormulaC43H66N12O12S2
Molecular Weight1007.2 g/mol
PubChem CID439302
SynonymsOXYTOCIN, 50-56-6, Pitocin, Endopituitrina, Ocytocin
Vial SizeOxytocin 2mg, Oxytocin 5mg
Purity (HPLC)≥99.0%

Oxytocin Peptide Key Features

  • Research Only: Synthesized for in vitro laboratory experimentation and structural analysis, this compound has been specifically synthesized.
  • Lyophilized Format: Supplied as a dry powder to preserve structural integrity during transport and storage.
  • High Chemical Purity: Subjected to extensive laboratory analyses such as HPLC and Mass Spectrometry to verify compound identity and purity.
  • Optimized Storage Stability: Formulated to maintain long-term stability when stored under recommended ultra-low temperature conditions.
  • Targeted Receptor Research: Ideal for studying non-peptide interactions, binding affinity studies and cell signaling networks.
  • Contamination Control: Produced under stringent quality standards designed to detect and remove trace elemental and microbial impurities, guaranteeing 100% purity of our final products.

Oxytocin Peptide Overview

Oxytocin serves as a foundational model in biochemistry and molecular biology to study structural dynamics of nonapeptide cyclic nonapeptides. Since being isolated and structurally characterized in the mid-20th century, its study remains of great interest within life science research. Researchers use Oxytocin Peptide to investigate basic cell mechanics, receptor-ligand kinetics and conserved signaling systems across various biological models.

Oxytocin investigations focus on its unique structural features, particularly its disulfide bridge. Because this peptide plays such an integral role in conserved biochemical pathways, access to highly purified synthetic iterations is key for producing reproducible data and isolating variables under controlled environments without the hassle of extracting endogenous molecules from biological matrices.

Research Use Only Oxytocin can be utilized across several subdisciplines, including analytical chemistry, neuroendocrinology and molecular pharmacology. By employing its highly refined, lyophilized counter-ion format researchers can ensure precise control over concentration, structural integrity and experimental parameters when performing automated assays or structural profiling experiments.

What Is Oxytocin?

Oxytocin can be divided into three biological classes and structures. Oxytocin belongs to the nonapeptide class and contains nine amino acid residues organized into a specific sequence, typically represented as C43H66N12O12S2. Oxytocin Peptides can be identified by their intramolecular disulfide bond created between cysteines at positions 1 and 6. This covalent bond forms a six-membered ring structure paired with three amino-acid C-terminal tails.

Oxytocin peptide sequence with disulfide bond

Historical Scientific Background

This discovery and its subsequent synthesis represent a stunning achievement in organic chemistry and peptide biology. As the first polypeptide hormone ever sequenced and chemically synthesized, Vincent du Vigneaud received the Nobel Prize in Chemistry for this achievement in 1955. This breakthrough demonstrated that complex, biologically active molecules could be accurately replicated in a laboratory setting, effectively inaugurating modern synthetic peptide research.

Research Significance

Nowadays, this molecule is studied both for its individual properties as well as to serve as a structural benchmark when comparing related neurohypophyseal peptides, such as vasopressin. As only two amino acids separate these distinct lineages of neurohypophyseal peptides from one another, Oxytocin Peptide remains central in structural biology studies on molecular evolution, receptor selectivity and architectural principles governing peptide-receptor docking interfaces.

Oxytocin in Scientific Research

Laboratory Investigations and Receptor Biology

Recent Oxytocin research is centered around its interaction with the Oxytocin Receptor (OXTR), a prominent member of the G-protein coupled receptor superfamily. Oxytocin is being utilized to map specific hydrophobic and electrostatic interactions governing OXTR’s transmembrane domain binding sites as well as identify how modifications in its sequence affect downstream signal transduction pathways. Researchers use site-directed mutagenesis along with high resolution structural modeling to explore how small changes affect signal transduction pathways.

Experimental Peptide Signaling Studies

Peptides that bind to their receptors activate an intracellular signaling cascade typically mediated by Gq/11 heterotrimeric G-proteins, leading to activation of PLC signaling pathways that involve hydrolysis of PIP2 into IP3 and diacylglycerol (DAG), followed by downstream activation cascades for mitogen-activated protein kinases (MAPKs). Research laboratories often track these pathways in order to measure intracellular calcium mobilization as well as assess downstream MAPK cascades.

Scientists of continuing scientific investigation

  • Receptor Desensitization: Elucidating the molecular mechanisms underlying GPCR desensitization after long term ligand exposure.
  • Cross-Reactivity Matrix: Mapping synthetic analogue binding affinities to determine cross-reactivity with vasopressin receptors (V1a, V1b and V2).
  • Allosteric Modulation: Locating small-molecule binding sites on receptor complexes that enhance or restrict peptide efficacy.
  • Peptidomimetic Design: Utilizing native peptide structure as a basis for designing non-peptide stable agonists and antagonists.

Scientific Background

Scientific literature highlights the Oxytocin Research Peptide’s structural significance for unraveling fundamental neurochemical pathways. By using in vitro systems, cell cultures and isolated tissue arrays as models for study purposes, researchers can observe localized cell responses without the confounding variables inherent to complex organismal systems.

Oxytocin signaling leading to intracellular Ca²⁺ flux

High-throughput screening technologies often utilize Lyophilized Oxytocin as a benchmark peptide, to establish baseline parameters for binding kinetics (Kd) and functional potency (EC50). As structural biology moves deeper into cryogenic electron microscopy modeling, Lyophilized Oxytocin remains an invaluable reference compound in validating high-resolution molecular maps of receptor complexes bound by its molecules.

Storage and Handling Guidelines

Recommended Storage Temperatures

In order to preserve structural stability, Oxytocin Storage protocols require precise temperature regulation. Once unopened lyophilized vials have been received they should be stored at 20deg or lower and for extended shelf-lives of 12 months or greater ultra-low storage at -80 is advised; standard frost-free freezers should be avoided as fluctuations can accelerate peptide degradation.

Moisture and Light Protection

Peptides in their lyophilized state are extremely moisture sensitive, and exposure to atmospheric moisture may result in deliquescence and hydrolytic cleavage of their bonds. Therefore, keep vials tightly sealed within an environment which has low humidity or desiccated atmosphere; additionally certain amino acid residues are susceptible to photo-oxidation, so store the product away from direct light exposure by placing in opaque secondary packaging.

Laboratory Handling Practices

Prior to opening a vial, allow the product to reach room temperature by placing it in a desiccating chamber – this prevents ambient moisture from condensing onto lyophilized powder and congealing on it. All reconstitution steps must take place within a sterile laminar flow hood using laboratory-grade solvents such as deionized water or bacteriostatic water depending on your assay requirements.

Oxytocin is a naturally-occurring cyclic nonapeptide found across mammalian species. To produce pure chemical forms for molecular and cellular evaluation, its production via solid-phase peptide synthesis is often utilized.

Frequently Asked Questions

What Is Oxytocin Peptide?

Its Oxytocin Peptide refers to a highly purified synthetic sequence of nine amino acids created specifically for scientific research purposes. This material boasts an intramolecular disulfide bond which defines its chemical properties and receptor binding profile.

Is this product for research use only?

Yes. This oxytocin product has been designated strictly as Research Use Only Oxytocin and should only be used in lab experiments, analytical testing or life science research methodologies – they should never be used diagnostically, veterinary medically or human medically.

How should Oxytocin be stored?

Oxytocin Storage should involve keeping lyophilized powder at -20 or below in a dry and dark environment, while once reconstitution into solution it may be kept at 4 for short-term use or aliquoted and frozen at -20 to reduce freeze-thaw cycles.

What does “Lyophilized Peptide” refer to?

Lyophilization is a freeze-drying preservation method which utilizes vacuum pressure in order to extract any water present, thus creating a stable powder with minimal structural degradation, thus increasing shelf life during storage and shipping of Oxytocin Research Peptides.

What Is Peptide Reconstitution?

Peptide reconstitution refers to the process of dissolving lyophilized powder into liquid solvent for laboratory assays, with the specific solvent chosen depending on experiment design and desired compound stability.

What lab fields study Oxytocin?

This compound has wide application in biochemistry, neurobiology, molecular pharmacology and structural biology research fields. Researchers utilize it for investigating GPCR activation patterns, cell signaling cascades and receptor binding affinities.

Research Notes

Laboratory Compliance Notice

This material is synthesized, packaged, and distributed exclusively for laboratory research purposes, scientific investigations, and in vitro experimentation. This product does not constitute medical advice, nor is it intended for diagnostic, therapeutic, or clinical intervention. Standard laboratory safety protocols, including the use of personal protective equipment (PPE), must be strictly enforced when handling this chemical compound.

Suggested Scientific References

  • National Center for Biotechnology Information (NCBI): PubChem Compound Summary for CID 439302 (Oxytocin).
  • The Journal of Biological Chemistry: Published articles focusing on G-protein coupled receptor kinetics and cyclic peptide synthesis parameters.
  • International Union of Basic and Clinical Pharmacology (IUPHAR): Database classifications detailing the properties and signaling mechanisms of the Oxytocin Receptor family.

Get a Quick Quote

Name

⚠ Intended Use

All products are intended for in vitro laboratory research use only.
They are strictly prohibited for administration to humans or animals, and must not be used for diagnostic, therapeutic, or clinical applications.

Storage and Handling

Store lyophilized powder at –20°C.
After reconstitution (for laboratory analysis), store at 2–8°C.
Avoid repeated freeze-thaw cycles.
Maintain aseptic technique during handling.

Submit your requirements

Name