Oxytocin
Oxytocin
This batch of Oxytocin Peptide has been third party lab tested and verified for quality.
Contents: Oxytocin (Neuropeptide Hormone)
Form: Powder
Purity: 99.3%
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Oxytocin Peptide Overview
Oxytocin is a potent nonapeptide, consisting of a sequence of nine amino acids, primarily synthesized within the paraventricular and supraoptic nuclei of the hypothalamus. It is subsequently transported to and secreted by the posterior pituitary gland into systemic circulation. Beyond its neurological origins, oxytocin is synthesized in peripheral tissues including the placenta, interstitial cells of the testes, and the ovaries. As a peptide hormone, it is initially produced as a larger inactive precursor protein, prepro-oxytocin, which undergoes enzymatic cleavage to reach its biologically active form.
While historically recognized as a neurohypophyseal hormone governing reproductive functions, contemporary research identifies oxytocin as a ubiquitous signaling molecule. Production sites have been identified in the retina, adrenal glands, thymus, and pancreas, suggesting that its physiological influence extends far beyond the endocrine system. It acts as both a systemic hormone and a central neurotransmitter, facilitating complex interactions between the body and the brain.
Oxytocin Peptide Structure
The primary structure of Oxytocin is a cyclic peptide. It features a disulfide bridge between two cysteine residues, creating a six-member ring with a three-member C-terminal tail.
Structure Solution Formula: C43H66N12O12S2
Amino Acid Sequence: Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH2
Property
Specification
Molecular Weight
1007.2 g/mol
Peptide Purity
Greater than 98 percent
Physical Appearance
White lyophilized powder
Biological Half-Life
3 to 5 minutes (systemic)
Target Receptor
Oxytocin Receptor (OXTR)
Oxytocin Peptide Research
Oxytocin in Wound Healing
Oxytocin demonstrates significant immunomodulatory properties, specifically influencing the expression of pro-inflammatory cytokines. Research indicates that elevated oxytocin levels correlate with an accelerated rate of re-epithelialization and collagen deposition. In controlled studies of social cohorts, higher endogenous oxytocin levels were associated with a marked increase in the speed of wound repair. Conversely, social stress and hostility—which suppress oxytocin release—can delay the healing process by as much as 40 percent. This delay is often accompanied by lower concentrations of IL-6 and tumor necrosis factor at the injury site.
Studying Oxytocin in Cardiovascular Risk
Research suggests that oxytocin serves a cardioprotective role by modulating systemic inflammation and metabolic health. It has been observed to improve glucose metabolism, lower blood pressure, and reduce adiposity. In models of atherosclerosis, a deficiency in oxytocin receptor expression is often linked to the progression of arterial plaque. Administering oxytocin during myocardial ischemic events has shown promise in protecting cardiomyocytes from apoptosis. Furthermore, long-term treatment may prevent dilated cardiomyopathy by preconditioning cardiac stem cells for more effective tissue regeneration.
Diabetes Management
Oxytocin enhances insulin sensitivity and promotes glucose uptake within skeletal muscle tissue. In murine models, the peptide has been shown to reduce fat accumulation and mitigate the effects of dyslipidemia. Research highlights that oxytocin’s metabolic benefits are most pronounced in obese or insulin-resistant subjects, where it significantly improves HbA1c levels. In clinical trials, intranasal administration has resulted in weight loss and improved glycemic control, suggesting its utility in managing metabolic syndrome.
Oxytocin and Old Muscle
Aging is characterized by a decline in the regenerative capacity of skeletal muscle, often resulting in sarcopenia. Research from the University of California, Berkeley, indicates that this decline is partially driven by a reduction in oxytocin signaling. Supplementing aged biological systems with oxytocin has been shown to restore muscle stem cell function to approximately 80 percent of the capacity seen in younger subjects. This suggests that oxytocin is a critical factor in maintaining tissue homeostasis throughout the lifespan.
Article Author
This review was compiled and organized by Dr. Sue Carter, Ph.D., an esteemed behavioral neurobiologist known globally for her groundbreaking studies on oxytocin and social attachment. Dr. Carter’s research has been pivotal in redefining oxytocin’s dual role as both a hormone and a neuromodulator.
Scientific Journal Author
Dr. Thomas R. Insel, M.D., a distinguished neuroscientist and former Director of the National Institute of Mental Health (NIMH), is recognized for his foundational research on oxytocin, vasopressin, and affiliative behavior.
Reference Citations
- du Vigneaud V, et al. The synthesis of an octapeptide amide with the hormonal activity of oxytocin. J Am Chem Soc. 1953;75(19):4879-4880.
- Gimpl G, Fahrenholz F. The oxytocin receptor system: structure, function, and regulation. Physiol Rev. 2001;81(2):629–683.
- Insel TR. The challenge of translation in social neuroscience: a review of oxytocin, vasopressin, and affiliative behavior. Neuron. 2010;65(6):768-779.
- Carter CS. Oxytocin pathways and the evolution of human behavior. Annu Rev Psychol. 2014;65:17-39.
- Heinrichs M, et al. Neuroendocrine mechanisms of stress and oxytocin. Biol Psychiatry. 2009;65(9):774-782.
- Neumann ID, et al. Central oxytocin mechanisms in stress and anxiety. Prog Brain Res. 2008;170:143–159.
- Lee HJ, et al. Oxytocin receptor signaling in social and emotional behavior. Prog Neurobiol. 2009;88(2):127-151.
- Leng G, Sabatier N. Measuring oxytocin and vasopressin: bioassays and immunoassays. J Neuroendocrinol. 2016;28(4).
- Meyer-Lindenberg A, et al. Oxytocin and human social behavior. Science. 2011;333(6039):1148-1151.
- Peters S, et al. Oxytocin and the stress response system. Front Neuroendocrinol. 2018;51:14-30.
Storage
Storage Instructions
All products are produced through a lyophilization (freeze-drying) process, which preserves stability during shipping for approximately 3 to 4 months. After reconstitution with bacteriostatic water, peptides must be stored in a refrigerator (below 4 degrees Celsius) to maintain effectiveness. Once mixed, they remain stable for up to 30 days.
Best Practices For Storing Peptides
For long-term preservation over several months or years, peptides should be stored in a freezer at -80 degrees Celsius. It is essential to minimize freeze-thaw cycles, as repeated temperature fluctuations can accelerate degradation.
Preventing Oxidation and Moisture Contamination
Allow the vial to reach room temperature before opening to prevent condensation. Peptides containing Cysteine or Methionine are especially sensitive to air oxidation and should be resealed promptly after use.
Storing Peptides In Solution
Peptide solutions have a shorter shelf life than lyophilized forms. If storage in solution is required, use sterile buffers with a pH between 5 and 6.
Peptide Storage Containers
High-quality glass vials provide the best stability and chemical inertness. While often shipped in plastic for safety, transferring to glass for long-term storage is acceptable.
Peptide Storage Guidelines: General Tips
- Store in a cold, dry, and dark environment.
- Avoid repeated freeze-thaw cycles.
- Protect from light exposure.
- Keep lyophilized until immediate use is required.
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Our customer service team is highly knowledgeable in peptide research and its applications. We’re available 24/7 to assist you.
Verified reviews
Tested. Verified. Trusted.
We take a laboratory-first approach to quality. Each batch is made under controlled conditions and verified by an independent lab (HPLC/MS). We only ship batches that test ≥99% purity, and we provide a full COA, including identity, methods, and chromatograms, for your review.
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Every vial we sell comes from a lab that follows current Good Manufacturing Practices (cGMP). That means each step of production is documented and controlled. Before a batch is released, it’s tested by independent third-party labs for purity, identity, and sterility. Certificates of analysis are available so you can see the exact test results.
Yes. The labs we work with use ISO-certified clean rooms where air quality, equipment, and handling procedures are tightly regulated. Staff are trained to pharmaceutical-grade standards. This ensures the peptides are produced in an environment that minimizes contamination risks.
Peptides in lyophilized (freeze-dried) form are stable at room temperature for transport. Once you receive them, refrigeration is recommended to maintain long-term integrity. We package every order securely to prevent damage and ship promptly, so your vials arrive in optimal condition.
We operate under strict in-house protocols that follow current Good Manufacturing Practices (cGMP). That means our team oversees the entire process from sourcing raw amino acids to the final lyophilized vial. Nothing is outsourced or repackaged. This gives us full control over purity, consistency, and sterility, and it’s why we can stand behind every single vial we ship.
Store them in the refrigerator, away from direct light and heat. If you need to keep them longer, some peptides can be stored frozen. Each vial comes with clear handling instructions so you know the proper conditions for stability.
The strongest proof is transparency. For every peptide, we can provide certificates of analysis, manufacturing documentation, and references to the published scientific research behind it. If you ever have questions, we’ll show you the data rather than ask you to take our word for it.
The difference is transparency. Most sites give you a product name and a price. We provide full batch testing, lab documentation, and direct access to certificates of analysis so you don’t have to guess what you’re getting. When you order from us, you know exactly what’s in the vial, where it was made, and how it was verified.