Shaanxi BLOOM Tech Co., Ltd. is one of the most experienced manufacturers and suppliers of beta-neoendorphin in China. Welcome to wholesale bulk high quality beta-neoendorphin for sale here from our factory. Good service and reasonable price are available.
Beta-neoendorphin is an endogenous opioid peptide belonging to the Dynorphin family. It was initially isolated and identified from the hypothalamus of pigs by Japanese scientists Matsuo et al. in the 1980s. It is an oligopeptide composed of 9 amino acid residues. Its complete sequence is Tyr Gly Gly Phe Leu Arg Lys Tyr Pro. Another peptide closely related to it is alpha neoendorphin, which consists of 10 amino acids (with an additional Lys residue at the end). Both originate from the same precursor protein.
beta-Neoendorphin COA
 |
||
| Certificate of Analysis | ||
| Compound name | Beta-Neoendorphin | |
| Grade | Pharmaceutical grade | |
| CAS No. | 77739-21-0 | |
| Quantity | 33g | |
| Packaging standard | PE bag+Al foil bag | |
| Manufacturer | Shaanxi BLOOM TECH Co., Ltd | |
| Lot No. | 202601090088 | |
| MFG | Jan 9th 2026 | |
| EXP | Jan 8th 2029 | |
| Structure |
|
|
| Item | Enterprise standard | Analysis result |
| Appearance | White or almost white powder | Conformed |
| Water content | ≤5.0% | 0.26% |
| Loss on drying | ≤1.0% | 0.77% |
| Heavy Metals | Pb≤0.5ppm | N.D. |
| As≤0.5ppm | N.D. | |
| Hg≤0.5ppm | N.D. | |
| Cd≤0.5ppm | N.D. | |
| Purity (HPLC) | ≥99.0% | 99.80% |
| Single impurity | <0.8% | 0.32% |
| Total microbial count | ≤750cfu/g | 337 |
| E. Coli | ≤2MPN/g | N.D. |
| Salmonella | N.D. | N.D. |
| Ethanol (by GC) | ≤5000ppm | 556ppm |
| Storage | Store in a sealed, dark, and dry place below -20°C | |
|
|
||
| Chemical Formula: | C54H77N13O12 |
| Exact Mass: | 1100 |
| Molecular Weight: | 1100 |
| m/z: | 1100 (100.0%), 1101 (58.4%), 1102 (16.7%), 1101 (4.8%), 1103 (3.1%), 1102 (2.8%), 1102 (2.5%), 1103 (1.4%) |
| Elemental Analysis: | C, 58.95; H, 7.05; N, 16.55; O, 17.45 |
As the substance mainly exists as an endogenous neuropeptide, its "uses" not only cover its natural physiological functions in the human body, but also include the exploration of its use as a drug target in scientific research, as well as its application in the field of cosmetic chemistry in recent years.
Biomedical research applications: signal transduction and receptor research
In molecular biology and neuroscience laboratories, it is a standard chemical tool for studying opioid receptor signaling.
1.1 Selective agonists of kappa opioid receptor (KOR)
Researchers use synthesized beta-neoendorphin to study the activation mechanism of KOR. Unlike synthetic opioid drugs, beta endorphins represent the natural activation mode of the organism.
Usage description: Used for in vitro cell experiments to determine receptor affinity (Ki), agonist potency (EC50), and G protein coupling efficiency. By comparing the effects of beta endorphin and dynorphin A, scientists can decipher the subtle differences in KOR subtypes.
Research value: Help understand why natural ligands activate receptors and are less likely to develop severe tolerance like artificial drugs.
1.2 Study on Neural Loop Tracing and Coexistence of Neurotransmitters
Due to its high expression in the hypothalamus and pituitary gland, it is used as an immunohistochemical (IHC) marker to identify and track specific neural pathways.
Purpose description: To study the dopamine regulatory mechanism in the substantia nigra striatum pathway and the coexistence ratio of opioid peptides and vasopressin in the hypothalamic supraoptic nucleus.
Physiological Function Application: Natural regulator in the human body
Inside the human body, it is not a 'foreign drug', but a key molecule that serves multiple physiological purposes.
2.1 Endogenous analgesia (pain management)
This is its core physiological use. When the body is subjected to harmful stimuli, the central nervous system releases the peptide, which acts on the spinal cord and brainstem.
Detailed description: It blocks the release of substance P and glutamate through presynaptic inhibition, thereby reducing the intensity of pain signals.
In the chronic pain model, increasing its concentration in cerebrospinal fluid can significantly increase the pain threshold.
2.2 Stress and Emotional Stability
Beta endorphins play a "brake" role in stress response.
Detailed description: Under stress, the hypothalamus releases this peptide to regulate the HPA axis (hypothalamic pituitary adrenal axis). It can inhibit excessive release of stress hormones and prevent neuronal damage caused by long-term stress in the body.
Reverse regulation: It also participates in generating "dysphoria", a seemingly negative function that is actually a protective negative feedback set by the body to avoid excessive pursuit of certain reward behaviors.
2.3 Neuroendocrine regulation
Regulation of the reproductive system: It can inhibit the pulsatile secretion of gonadotropin-releasing hormone (GnRH), thereby regulating ovulation and fertility function under extreme stress or malnutrition.Water salt balance: works in conjunction with antidiuretic hormone to regulate the reabsorption of water by the kidneys.
Potential medicinal and clinical therapeutic uses
Although beta endorphins have not yet been marketed as first-line prescription drugs, their clinical translational research is extremely active.
3.1 Development of new non addictive analgesics
Traditional mu receptor agonists such as morphine and fentanyl are highly addictive. Beta-neoendorphin tend to activate kappa receptors.
Usage description: Pharmacologists attempt to mimic the structure of beta endorphins and design "Biased Ligands". This drug aims to retain its analgesic effect while avoiding the side effects of hallucinations and irritability through a special receptor coupled pathway.
3.2 Intervention for Drug Addiction
Detailed description: In the treatment of cocaine or alcohol addiction, the system is used to suppress dopamine surges in the limbic system. Research has shown that enhancing endogenous levels of new endorphins through pharmacological means can reduce drug cravings during withdrawal.
3.3 Antiepileptic effect
Detailed description: Experimental evidence shows that after a major epileptic seizure, the levels of beta endorphin in the brain increase. Clinical studies are exploring the use of nasal administration (bypassing the blood-brain barrier) as an auxiliary termination method for acute epileptic seizures, utilizing its potent neuroprotective effects.
Dermatology and Cosmetic Chemistry Applications
This is the closest application of beta endorphins to the consumer market in recent years, especially in high-end functional skincare products.4.1 Skin barrier repair and anti-inflammatory effects
Detailed description: Skin epidermal cells (keratinocytes) express opioid receptors. Beta endorphins can promote the synthesis of ceramides and strengthen the skin's brick wall structure.
At the same time, it can inhibit degranulation of mast cells and reduce inflammatory reactions such as skin redness, swelling, and itching.
4.2 Bioactive substances of the concept of "emotional skincare"
Detailed description: Some skincare ingredients, such as those derived from grey bean extract or synthetic peptides, claim to be able to stimulate the skin's own production of beta endorphins, achieving "stress relief" and "instant relief". This use utilizes the characteristic of the skin and nervous system sharing a set of signaling molecules (skin brain axis).
In living organisms, this peptide is not directly produced through single gene translation, but rather as part of a larger precursor protein, generated through the "precursor processing" pathway.
The biosynthetic origin of beta endorphins is located in the PDYN gene in the nucleus of the cell (on chromosome 20 in humans).
Transcription and Translation:
In neurons or endocrine cells, the PDYN gene is transcribed into mRNA, which is then translated into prepro dynorphin on the ribosomes of the rough endoplasmic reticulum (RER).
Signal peptide resection:
The original protein contains an N-terminal signal peptide responsible for guiding it to the secretion pathway. Once inside the endoplasmic reticulum lumen, signal peptides are cleaved by signal peptidases to form prodynorphin.
After completing initial folding in the endoplasmic reticulum, proenkephalin is transported to the Golgi apparatus via vesicles.
Packaging:
In the reverse network (TGN) of the Golgi apparatus, proenkephalin is packaged together with specific processing enzymes into large granule dense vesicles (LDCVs).
Maturity:
The true biosynthetic cleavage process mainly occurs during the transport of these vesicles from the Golgi apparatus to synaptic terminals. As the pH value inside the vesicles decreases (acidification), processing enzymes are activated.
This is the most critical biochemical step in the synthesis process. Proenkephalin is a large polypeptide chain containing multiple opioid peptide sequences (including enkephalin A, enkephalin B, and neoenkephalin).
The role of prohormone converting enzyme (PC)
The synthesis of beta endorphins mainly relies on two endonucleases, PC1/3 and PC2.
Identification site:
These enzymes recognize double basic amino acid sites in the sequence (such as Lys Arg or Arg Arg).
Generating alpha new endorphins:
The enzyme first cleaves the precursor, releasing alpha new endorphins. Alpha type is a 10 peptide with the sequence Tyr Gly Gly Phe Leu Arg Lys Tyr Pro Lys.
Fine Modification of Carboxypeptidase E (CPE)
To convert from alpha type to beta type, further cleavage of the C-terminal residue is required.
Step:
Carboxypeptidase E recognizes the alkaline amino acid (Lys) at the end of alpha endorphins.
Conversion:
CPE removes the 10th Lys at the end to generate 9-peptide beta neoendorphin (Tyr Gly Gly Phe Leu Arg Lys Tyr Pro).
The synthesis rate and final yield are influenced by various environmental signals:
Calcium ion signal:
The depolarization of neurons can lead to an increase in intracellular calcium concentration, which not only promotes vesicle release but also feedback stimulates the transcription of PDYN genes.
cAMP response element:
The promoter region of the PDYN gene contains cAMP response elements (CRE). When cells receive stress signals (such as passing through norepinephrine receptors), cAMP levels increase, which accelerates the synthesis of the peptide.
Tissue specificity:
Although the precursor proteins are the same, in different tissues (such as thalamus vs. spinal cord), due to the different expression ratios of processing enzymes (PC1 vs. PC2), the proportion of alpha type and beta type in the final product may vary.
In addition to natural physiological synthesis, modern biotechnology has also developed artificial synthesis methods, mainly used for scientific research and raw material production:
Genetic Engineering Recombination Method
Using Escherichia coli (E. coli) or yeast as expression hosts.
Method:
The artificially synthesized beta-neoendorphin DNA sequence is fused and expressed with a carrier protein (such as GST) to prevent the small peptide from being degraded by host proteases.
Purification:
After expression, the pure peptide is separated by affinity chromatography and then cleaved and released using chemical reagents (such as cyanogen bromide) or specific enzymes.
Natural biosynthesis is a highly integrated process that begins with transcription of the PDYN gene, transported through the endoplasmic reticulum Golgi system, and ultimately completed through cascade cleavage of PC and CPE enzymes in secretory vesicles.
Information source statement:
'lt is awesome to work with Creative. amazingy organized,easy to communicate with. responsive with next iterations,and beautiful work.
Molecular Biology of the Cell (Alberts et al.):
Fundamental principles of protein secretion pathways and precursor processing.
The Opioid Receptors (Pasternak, G. W.):
Detailed the enzymatic hydrolysis sites of each member of the proenkephalin family.
Journal of Biological Chemistry (JBC):
A research paper on the specific roles of PC1 and PC2 enzymes in opioid peptide synthesis.
IUPHAR Database:
Standardized description of endogenous ligand biosynthesis pathways.
refence:
1. Matsuo, H. & Kangawa, K. (1982). "beta-Neo-endorphin: structure and function." Annual Review of Physiology.
2. Civelli, O., et al. (1985). "Molecular biology of the opioid peptide precursors." Annual Review of Neuroscience.
3. Zadina, J. E., et al. (1997). "A potent and selective endogenous agonist for the mu-opioid receptor." Nature.
4. Basbaum, A. I., et al. (2009). "Cellular and Genetic Mechanisms of Pain." Cell.
5. Takahashi, M., et al. (2018). "The role of beta-neoendorphin in skin barrier function." Journal of Investigative Dermatology.
6. IUPHAR/BPS Guide to PHARMACOLOGY.
Hot Tags: beta-neoendorphin, suppliers, manufacturers, factory, wholesale, buy, price, bulk, for sale, Best Growth Hormone Releasing Peptide CAS 87616 84 0, Lpamorelin Powder CAS 170851 70 4, GLP 1 Peptide CAS 87805 34 3, Melanotan ii powder, CJC 1295 Peptide, sermorelin powder