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| Weight | .03125 lbs |
|---|
⚠️ Disclaimer: THIS PRODUCT, SOLD BY LOTI LABS, IS INTENDED AS A RESEARCH CHEMICAL ONLY.
This designation allows the use of this chemical strictly for in-vitro laboratory testing and experimentation. No other uses or purposes are permitted. All information provided on this website is for educational purposes and has been compiled from multiple sources believed to be accurate. Human or animal use of this product is strictly forbidden by law. This product is not a drug, food or cosmetic and may not be misbranded, mislabeled or misused as such. Anyone not adhering to these terms will be blacklisted and forbidden from purchasing.
For more information on the naming of this product CLICK HERE
Oxytocin is a nine-amino acid neuropeptide synthesised in the hypothalamic paraventricular (PVN) and supraoptic nuclei (SON) and released from the posterior pituitary. While it’s classically associated with parturition and lactation, the research landscape has expanded significantly over the last two decades. We now recognise it as a major modulator of social bonding, trust, stress responses, appetite regulation, and pain modulation. Through its central and peripheral actions, it also affects a broad range of autonomic and metabolic functions. This pleiotropic profile has turned oxytocin into one of the most studied neuropeptides in contemporary neuroscience and endocrinology research.
Oxytocin works through a single G-protein coupled receptor (OXTR) that’s spread throughout the brain and peripheral tissues. Activating OXTR in the uterus and mammary glands drives smooth muscle contraction and milk ejection—the peptide’s classic peripheral actions. It’s also heavily expressed in limbic regions like the amygdala, nucleus accumbens, hippocampus, and prefrontal cortex, which explains its influence on social cognition and emotional regulation.
On a cellular level, OXTR signalling triggers Gq proteins, leading to PLC activation, IP3-mediated calcium release, and downstream PKC activation. In neurons, oxytocin shifts firing patterns and synaptic transmission; it’s generally linked to anxiolytic and pro-social effects through interactions with GABAergic and dopaminergic systems. Its cross-talk with the dopaminergic reward system—specifically in the nucleus accumbens—is a key focus in research on social reward and pair bonding.
Social neuroscience has found a goldmine in oxytocin, making it one of the most active areas of modern neuropeptide research. Early evidence for its role in pair bonding came from studies on prairie voles, a monogamous rodent species that naturally carries high OXTR density in its limbic regions. In human trials, researchers use intranasal oxytocin to gain partial CNS access. These studies have reported changes in facial recognition, gaze behaviour, and trust during economic games, alongside reduced amygdala reactivity when facing threatening stimuli. It is a complex field, though; recent replication challenges have pushed scientists toward more nuanced interpretations of how the peptide actually functions.
Researchers are looking closer at oxytocin’s impact on energy homeostasis. OXTR-expressing neurons in the hypothalamus help control food intake, and when oxytocin’s administered to rodent models, it reduces feeding behaviour. Evidence also suggests it might influence lipid metabolism and brown adipose tissue thermogenesis. It is a compelling subject for obesity-related research beyond its traditional neuroendocrine roles.
Researchers often look at Oxytocin alongside PT-141 10mg when they’re exploring reward and sexual motivation circuits. This is because melanocortin and oxytocinergic pathways overlap right in the paraventricular nucleus. When studies involve Kisspeptin-10 5mg or Gonadorelin 5mg, oxytocin’s often used as a marker for hypothalamic activity. It makes sense, since kisspeptin and OXT neurons sit so close to each other in the hypothalamus.
We provide Oxytocin 2mg as a lyophilised peptide. To maintain peptide stability once in solution, researchers should use sterile bacteriostatic water or acidified saline (0.1% acetic acid) for reconstitution. Once prepared, the solution should be kept at 4°C and used within a few days. If extended storage is required, it is best to aliquot the liquid and freeze it at −20°C. Because Oxytocin’s disulfide bond can oxidise under harsh conditions, the peptide should not be left exposed to air or high temperatures for long.
This product is for research purposes only. It’s not for clinical use and is not intended for human administration.
For more information on Oxytocin please visit Wikipedia.
| Weight | 0.0099 lbs |
| Appearance | Fine White Lyophilized Powder |
| Residue Sequence | CYIQNCPLG-NH2 |
| Solubility | 100 µg/mL sterile diluent (distilled de-ionized water) |
| Source | Biosynthetic production |
| Stability | Lyophilized protein is to be stored at -20°C. It is recommended to divide the remaining reconstituted peptide into multiple vials so as to avoid a cycle of freezing and thawing. Reconstituted protein can be stored at 4°C. |
| Molar Mass | 1007.19 g/mol |
| CAS Number | 158861-67-7 |
| PubChem | CID 439302 |
| Molecular Formula | C43H66N12O12S2 |
| MG | 2mg |
| Terms | This product is sold for research/laboratory usage only. No other uses are permited. |
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