β-Endorphin is an endogenous opioid peptide that acts as an agonist at μ-opioid receptors (μORs) and exhibits immunomodulatory, neuromodulatory, antidepressant, and antinociceptive/analgesic activities. In vivo, β-endorphin increases levels of B-cells and production of antibodies as well as secretion of IL-4 and proliferation of splenocytes, shifting the immune response toward Th2-specific mediators.
CAT No: R1826
CAS No:59887-17-1
Synonyms/Alias:beta-Endorphin (1-31);59887-17-1;DTXSID20208602;beta-Endorphin, triethoxy(3-isothiocyanatopropyl)-, (6R-(6alpha,7alpha,7(R*)))-;CHEMBL3250455;DTXCID30131093;DA-79185;FE108751;FE108786;beta-Endorphin bovine, camel, ovine, >=97% (HPLC);
Chemical Name:(2S)-5-amino-2-[[2-[[(2S)-6-amino-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-6-amino-2-[[(2S,3S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2S,3R)-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[2-[[2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]acetyl]amino]-3-phenyl-propanoyl]amino]-4-methylsulfanyl-butanoyl]amino]-3-hydroxy-butanoyl]amino]-3-hydroxy-propanoyl]amino]-4-carboxy-butanoyl]amino]hexanoyl]amino]-3-hydroxy-propanoyl]amino]-5-oxo-pentanoyl]amino]-3-hydroxy-butanoyl]pyrrolidine-2-carbonyl]amino]-4-methyl-pentanoyl]amino]-3-methyl-butanoyl]amino]-3-hydroxy-butanoyl]amino]-4-methyl-pentanoyl]amino]-3-phenyl-propanoyl]amino]hexanoyl]amino]-4-oxo-butanoyl]amino]propanoyl]amino]-3-methyl-pentanoyl]amino]-3-methyl-pentanoyl]amino]hexanoyl]amino]-4-oxo-butanoyl]amino]propanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]hexanoyl]amino]hexanoyl]amino]acetyl]amino]-5-oxo-pentanoic acid
β-Endorphin (bovine, camel, mouse) is a naturally occurring endogenous opioid peptide derived from the precursor protein proopiomelanocortin (POMC), found across various mammalian species. Structurally, it consists of a sequence of amino acids that enables it to interact with specific opioid receptors in the central and peripheral nervous systems. Its evolutionary conservation and functional significance in pain modulation, stress response, and neuroendocrine regulation have made β-endorphin a focal point in peptide biochemistry and neurobiology. The bovine, camel, and mouse variants provide valuable comparative models for investigating species-specific differences in peptide structure, receptor affinity, and physiological effects, supporting a broad range of research applications in molecular neuroscience, pharmacology, and peptide signaling studies.
Neuropeptide signaling studies: β-Endorphin is widely used as a research tool to elucidate the mechanisms of neuropeptide signaling within the central nervous system. By applying the peptide to in vitro or ex vivo neuronal preparations, researchers can investigate its effects on synaptic transmission, neuronal excitability, and downstream signaling pathways. Comparative studies using bovine, camel, and mouse β-endorphin variants enable the exploration of evolutionary adaptations in opioid receptor interactions, contributing to a deeper understanding of neuropeptide-receptor dynamics and species-specific regulatory mechanisms.
Receptor binding assays: The peptide serves as a critical ligand in receptor binding and affinity assays, facilitating the characterization of opioid receptor subtypes and their pharmacological profiles. Its high specificity for the mu-opioid receptor allows for quantitative analysis of ligand-receptor interactions, competitive binding studies, and the assessment of receptor density and distribution in various tissue samples. Utilizing β-endorphin from different species can reveal subtle differences in receptor selectivity, informing the development of novel opioid ligands and advancing receptor pharmacology research.
Peptide structure-activity relationship (SAR) analysis: Synthetic and natural β-endorphin peptides are essential for investigating structure-activity relationships within the opioid peptide family. By introducing sequence modifications or employing cross-species variants, researchers can identify critical residues responsible for receptor binding, agonist potency, and metabolic stability. These SAR studies provide valuable insights into the molecular determinants of opioid activity, guiding the rational design of peptide analogs with tailored biological properties for experimental use.
Neuroendocrine function research: β-Endorphin plays a pivotal role in modulating neuroendocrine functions, including the regulation of stress responses, hormonal secretion, and behavioral adaptation. Experimental models utilizing the peptide allow for the dissection of its influence on hypothalamic-pituitary-adrenal (HPA) axis activity, as well as its interactions with other neuropeptides and neurotransmitters. Comparative analysis of bovine, camel, and mouse β-endorphin supports investigations into species-dependent regulatory mechanisms and adaptive physiological responses.
Analytical and quantitative methods development: β-Endorphin is frequently employed as a reference standard or calibration material in the development and validation of analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and immunoassays. Its well-characterized sequence and physicochemical properties make it suitable for assay optimization, sensitivity testing, and quantitative measurement of endogenous peptide levels in biological samples. Access to variants from multiple species enhances the robustness and versatility of analytical protocols, supporting accurate detection and quantification in diverse research contexts.
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