Oxytocin Free Acid is the non-amidated form of the cyclic nonapeptide, leaving a free carboxyl terminus. The change in terminal charge influences overall dipole, solubility, and hydrogen-bond patterns. Researchers compare its conformation and receptor-binding features with C-terminally amidated analogs. Applications include cyclic-peptide structure studies, acid-amide effects analysis, and analog design.
CAT No: R2383
CAS No:24346-32-5
Synonyms/Alias:Oxytocin free acid;24346-32-5;Oxytocin (free acid);2-[[(2S)-2-[[(2S)-1-[(4R,7S,10S,13S,16S,19R)-19-amino-7-(2-amino-2-oxoethyl)-10-(3-amino-3-oxopropyl)-13-[(2S)-butan-2-yl]-16-[(4-hydroxyphenyl)methyl]-6,9,12,15,18-pentaoxo-1,2-dithia-5,8,11,14,17-pentazacycloicosane-4-carbonyl]pyrrolidine-2-carbonyl]amino]-4-methylpentanoyl]amino]acetic acid;HY-P3216;AS-86440;CS-0169706;G77862;H-CYS-TYR-ILE-GLN-ASN-CYS-PRO-LEU-GLY-OH;[(2S)-2-{[(2S)-1-[(4R,7S,10S,13S,16S,19R)-19-amino-13-[(2S)-butan-2-yl]-10-(2-carbamoylethyl)-7-(carbamoylmethyl)-16-[(4-hydroxyphenyl)methyl]-6,9,12,15,18-pentaoxo-1,2-dithia-5,8,11,14,17-pentaazacycloicosane-4-carbonyl]pyrrolidin-2-yl]formamido}-4-methylpentanamido]acetic acid;
Oxytocin free acid is a nonapeptide hormone and neuropeptide, distinguished by its unmodified C-terminal carboxylic acid group. As a naturally occurring peptide, oxytocin plays a central role in social behavior, neuroendocrine signaling, and smooth muscle contraction in mammals. The free acid form is particularly valued in biochemical research because it closely mirrors the peptide's endogenous state, enabling precise investigations into its structure-function relationships and receptor interactions. Its well-characterized sequence and defined biological activity make it an essential tool for studies in peptide biochemistry, receptor pharmacology, and neurobiology.
Peptide-receptor interaction studies: Oxytocin free acid serves as a critical standard for elucidating the binding dynamics and specificity of the oxytocin receptor, a G protein-coupled receptor involved in diverse physiological processes. Researchers utilize the free acid form to probe ligand-receptor affinities, dissect downstream signaling pathways, and compare the effects of native versus synthetic analogs. This application is central to advancing the understanding of peptide hormone signaling, receptor selectivity, and the molecular determinants governing neuropeptide function.
Peptide synthesis and analog development: The compound is frequently employed as a reference substrate in solid-phase peptide synthesis protocols and as a benchmark for quality control in the production of oxytocin analogs. Its defined structure and physicochemical properties facilitate the optimization of synthetic strategies and enable accurate assessment of purity, folding, and bioactivity in newly developed peptide variants. This use is particularly significant for laboratories engaged in the design and modification of peptide-based research tools.
Neuroendocrine research: Oxytocin free acid is widely used in experimental models to investigate the mechanisms of neuropeptide release, transport, and signaling within the central nervous system and peripheral tissues. By applying this peptide in controlled settings, scientists can dissect its role in modulating neuronal activity, synaptic plasticity, and neuroendocrine feedback loops. Such studies contribute valuable insights into the molecular underpinnings of behavior, stress response, and social cognition.
Biochemical assay development: The compound is an important reagent in the development and validation of biochemical assays designed to quantify oxytocin or assess enzyme activity related to peptide processing. Its use in immunoassays, binding assays, and chromatographic methods supports the generation of reliable, reproducible data for both basic and applied research. The free acid form's structural fidelity ensures compatibility with antibody recognition and enzymatic specificity, making it a preferred standard in analytical workflows.
Structure-activity relationship analysis: Oxytocin free acid is instrumental in systematic studies that explore how modifications to peptide sequence or conformation affect biological function. By serving as a reference molecule, it enables comparative analyses with synthetic analogs, truncated peptides, or site-specific mutants. This approach aids in mapping the critical residues required for receptor binding and activation, informing the rational design of novel peptide ligands and advancing the broader field of peptide therapeutics research.
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