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Oxytocin

CAS #: 50-56-6

Oxytocin

Research Use Only

All products are intended solely for laboratory research and are not for human or animal consumption. By purchasing, the buyer agrees to use these products in compliance with all applicable laws.

Oxytocin Overview

Oxytocin is a cyclic nonapeptide with a disulfide bridge between cysteine residues at positions 1 and 6, synthesized as a prohormone in hypothalamic magnocellular neurons and transported to the posterior pituitary for release. Through binding to its target receptor (OXTR), a G-protein-coupled receptor, it activates phospholipase C-mediated pathways leading to intracellular calcium release and protein kinase C activation. Research models examine oxytocin’s effects on smooth muscle signaling dynamics, myoepithelial contraction modeling, CNS behavioral pathways, stress response signaling, and autonomic nervous system modulation in laboratory settings.

Lee et al. (2009). Gimpl & Fahrenholz (2001).

History

Oxytocin was first isolated from the posterior pituitary gland by Henry Dale in 1906, who observed its smooth muscle signaling properties. The complete amino acid sequence was determined by Vincent du Vigneaud in 1953, and he successfully synthesized the peptide shortly thereafter, earning the Nobel Prize in Chemistry in 1955. This represented the first synthesis of a polypeptide hormone and established oxytocin as a foundational molecule in peptide biochemistry and neuroendocrinology.

Du Vigneaud et al. (1953).

Oxytocin Structure

CAS#: 50-56-6

Molecular Formula: C₄₃H₆₆N₁₂O₁₂S₂

Molecular Weight: 1007.19 g/mol

PubChem ID: 439302

Research Findings

Oxytocin has been extensively studied in neuroendocrinology, behavioral neuroscience, and endocrine signaling research, with investigations focusing on receptor-mediated signaling, CNS behavioral pathways, autonomic function, and neuromodulation in various experimental models. Studies examine central and peripheral oxytocin system functions.

Key Areas of Research:

  • Endocrine: Smooth muscle signaling, contraction dynamics, secretory pathways

  • CNS: Behavioral pathways, affiliation modeling, recognition

  • Neuroendocrine: HPA axis modulation, stress signaling, autonomic dynamics

  • Signaling: Neurotransmitter modulation, synaptic plasticity, reward pathways

These findings demonstrate oxytocin’s diverse actions across reproductive, social, and stress-regulatory systems. As both a peripheral hormone and central neuropeptide, oxytocin provides a research framework for examining neuroendocrine integration, social cognition mechanisms, and autonomic nervous system regulation in diverse experimental contexts.

Lee et al., Progress in Neurobiology, 2009

Our Process

STEP 1

Precision Lyophilization

Manufactured in a controlled U.S. facility under strict compounding standards.

STEP 2

Verified Purity

Every batch third-party tested with HPLC and mass spectrometry.

STEP 3

Same-Day Fulfillment

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Frequently Asked Questions

Orders dispatched same-day from our U.S. facility.

Each vial contains exactly what’s shown on the label. For example, a 10mg vial has exactly 10mg of lyophilized peptide. Researchers can divide it into smaller portions—like four 2.5mg measurements—but the total amount remains 10mg.

Peptides are supplied as lyophilized powder. They do not come reconstituted, and any extra supplies must be sourced separately for research applications.
In lyophilized powder form, peptides stay stable for up to 2 years. After reconstitution, it should be refrigerated and is generally stable for up to 2 months.

Products from Raw Peptides do not include usage instructions, as they are strictly for in vitro research and prohibited by law for human or animal use. Misuse or unlawful application will result in permanent denial of service.

Lyophilized peptides should be stored away from heat and light. Once reconstituted, they must be refrigerated to maintain stability and efficacy.