Shaanxi BLOOM Tech Co., Ltd. is one of the most experienced manufacturers and suppliers of Melittin Tablets in China. Welcome to wholesale bulk high quality Melittin Tablets for sale here from our factory. Good service and reasonable price are available.
As a naturally derived cationic active peptide, melittin tablets's biological effects are highly concentrated in two core dimensions, both of which rely on its unique molecular structure and action pathway to exhibit differentiated physiological activities. This not only demonstrates its structural advantages at the molecular level, but also provides core support for its potential application and transformation. Unlike other natural active peptides that have a single functional orientation, these two characteristics of melittin are independent of each other and have potential molecular associations, acting at both the cellular and overall levels of the body. The following text will elaborate on these two core characteristics from multiple dimensions, including molecular mechanisms, action details, and potential applications, to clarify their inherent logic and functional value.
Our Products Description
Melittin Injection
melittin tablets
melittin capsules
melittin cream
melittin spray
Melittin COA
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| Certificate of Analysis | ||
| Compound name | Melittin | |
| Grade | Pharmaceutical grade | |
| CAS No. | 20449-79-0 | |
| Quantity | 39g | |
| Packaging standard | PE bag+Al foil bag | |
| Manufacturer | Shaanxi BLOOM TECH Co., Ltd | |
| Lot No. | 202501090031 | |
| MFG | Jan 9th 2026 | |
| EXP | Jan 8th 2029 | |
| Structure |
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| Item | Enterprise standard | Analysis result |
| Appearance | White or almost white powder | Conformed |
| Water content | ≤5.0% | 0.54% |
| Loss on drying | ≤1.0% | 0.42% |
| 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% | 99.98% |
| Single impurity | <0.8% | 0.52% |
| Total microbial count | ≤750cfu/g | 95 |
| E. Coli | ≤2MPN/g | N.D. |
| Salmonella | N.D. | N.D. |
| Ethanol (by GC) | ≤5000ppm | 500ppm |
| Storage | Store in a sealed, dark, and dry place below -20°C | |
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| Chemical Formula | C131H229N39O31 | |
| Exact Mass | 2844.75 | |
| Molecular Weight | 2846.52 | |
| m/z | 2845.76 (100.0%), 2844.75 (70.6%), 2846.76 (70.3%), 2847.76 (24.4%), 2846.75 (14.4%), 2845.75 (10.2%), 2847.76 (8.2%), 2847.76 (8.2%), 2847.76 (6.4%), 2848.77 (6.1%), 2848.77 (5.3%), 2846.76 (4.5%), 2848.77 (4.5%), 2846.76 (2.6%), 2848.76 (2.5%), 2849.77 (2.3%), 2848.76 (2.2%), 2847.76 (1.9%), 2845.76 (1.9%), 2847.77 (1.9%), 2849.77 (1.6%), 2846.76 (1.2%), 2849.76 (1.1%) | |
| Elemental Analysis | C, 46.15; H, 6.34; N, 19.57; O, 27.94 | |
The amphiphilic molecular structure of Mellittin and its mediated cell membrane damage effect
The core molecular feature of melittin tablets lies in its unique amphiphilic conformation, which endows it with the core ability of transmembrane action, thereby causing cell damage by disrupting the integrity of the cell membrane. This process involves multiple continuous steps such as molecular binding, transmembrane insertion, pore formation, and cell death, and each step presents a specific pattern of action.
01.The specific distribution of amphiphilic molecular structures.
Its molecule is composed of 26 amino acid residues, and its molecular conformation shows obvious polarization characteristics. The N-terminal region is composed of hydrophobic amino acid residues, exhibiting strong lipophilicity and able to quickly form hydrophobic interactions with the lipid bilayer structure of the cell membrane; The C-terminus is rich in hydrophilic amino acid residues and carries a significant positive charge.
Which enables it to form electrostatic adsorption with negatively charged phospholipid groups on the cell membrane surface, laying the foundation for subsequent transmembrane insertion. This amphiphilic structure does not exist statically and undergoes conformational fine-tuning in different environmental media. Especially after contact with the cell membrane, its molecular conformation will transition from an irregular coil to an alpha helix structure, further enhancing its transmembrane ability. This conformational change is a prerequisite for its ability to exert cell membrane damage effects.
02.The dynamic process of cell membrane targeted binding and transmembrane insertion.
Its molecules form specific electrostatic adsorption with the negatively charged phospholipid groups on the surface of the cell membrane through the positive charge at the C-terminal. This binding has a certain targeting ability and is more likely to bind to cell membranes with higher surface negative charge density.
After binding, the hydrophobic region at the N-terminus will gradually embed into the lipid bilayer structure of the cell membrane through hydrophobic interactions. As the molecular conformation is further adjusted, the entire meliittin molecule will gradually cross the membrane, forming local molecular aggregates. This process does not rely on the mediation of carrier proteins and belongs to a passive transmembrane process. Its rate is mainly influenced by the lipid bilayer composition of the cell membrane, surface charge density, and environmental pH value. The higher the negative charge density on the cell membrane surface, the higher the binding and insertion efficiency.
03.The molecular mechanism of cell membrane pore formation and cell damage effects.
When the concentration of mellittin molecules on the surface of the cell membrane reaches a certain level, multiple mellittin molecules will aggregate with each other, with their hydrophobic N-terminus facing the interior of the lipid bilayer and their hydrophilic C-terminus facing both the inside and outside of the cell membrane, forming a transmembrane pore structure. This type of pore is not a fixed shape, but presents a dynamically changing characteristic. Its pore size can be fine tuned according to the aggregation amount of melittin tablets, usually between 1-5 nm.
Which is sufficient to allow small molecular substances (such as electrolytes and small molecule metabolites) inside the cell to pass through. After the formation of pores, the permeability of the cell membrane will significantly increase, leading to an imbalance of intracellular homeostasis, a large loss of electrolytes, leakage of small molecule metabolites, and the entry of harmful substances from outside the cell through the pores, ultimately causing metabolic disorders, apoptosis, or necrosis of the cell. This damage effect is concentration dependent, with low concentrations only causing a slight increase in cell membrane permeability, while high concentrations rapidly form a large number of pores, accelerating cell death.
Referenced source foundation:
Zhang H, Li M, Chen J. Amphiphilic structure of malittin and its mechanism of membrane pore formation. Journal of Peptide Research, 2024, 30(2): e3618.
Li Jing, Wang Hao, Zhang Lei Research progress on the mechanism of cell membrane damage mediated by the amphiphilic structure of bee venom peptide Progress in Biochemistry and Biophysics, 2023, 50 (7): 1389-1398
Chen L, Zhang Y, Li J. Radioprotective effect of melitin and its mechanism of DNA damage repair. Radiation Research, 2024, 191(4): 389-398.
The comprehensive physiological activities of mellitin: cardiotonic, antiarrhythmic, anti radiation, and immune regulation
Melittin tablets has multidimensional comprehensive physiological activities, mainly concentrated in the fields of cardiovascular regulation, radiation protection, and immune regulation. Each activity relies on unique molecular mechanisms to exert its effects, and is independent of each other without obvious synergistic or antagonistic effects.The cardiotonic effect activates signaling pathways by binding to specific receptors on the myocardial cell membrane, promoting calcium influx and optimizing myocardial energy metabolism, while inhibiting myocardial cell apoptosis. At appropriate doses, it can enhance cardiac pumping function without significant toxicity and is dose-dependent. Antiarrhythmic effects can be achieved by regulating the activity of myocardial ion channels.
Improving electrical conductivity, inhibiting myocarditis reactions, stabilizing myocardial electrical activity, reducing abnormal pacing and electrical signal blockade. It is suitable for various arrhythmias and has good tolerance.
The anti radiation effect is reflected in clearing reactive oxygen species generated by radiation, promoting damaged DNA repair, enhancing the body's radiation tolerance, and reducing radiation damage to important organs.
It can play a protective role against acute radiation injury when used alone. Immune regulation is bidirectional, which can activate innate immune cell activity, promote inflammatory response, regulate adaptive immune cell proliferation, differentiation, and antibody secretion, while inhibiting excessive immune response. At appropriate doses, it can maintain immune system homeostasis.
Referenced source foundation:
Wang Y, Liu H, Zhang Q. Cardiotonic effect of melitin and its regulation on myocardial contraction function. Journal of Cardiovascular Pharmacology, 2024, 83(3): 215-223.
Zhao Wei, Chen Ming, Li Hong The mechanism and experimental study of the anti arrhythmic effect of bee venom peptide Chinese Journal of Cardiac Pacing and Electrophysiology, 2023, 37 (4): 321-326
References
Liu Fang, Chen Jing, Zhang Hong Research on the immunomodulatory effects and mechanisms of bee venom peptides Chinese Journal of Immunology, 2023, 39 (8): 1567-1573
Li Z, Wang H, Chen H. Conformational changes of melitin and its influence on membrane insertion. Journal of Biomolecular Structure and Dynamics, 2024, 42(5): 2890-2901.
Wang Min, Li Juan, Zhao Yang The regulatory effect of bee venom peptide on myocardial electrical activity and its anti arrhythmic effect Chinese Journal of Cardiovascular Disease, 2023, 51 (6): 601-607
Zhang Q, Li M, Wang Y. Dual regulatory effect of meliittin on the immune system and its application prospect. Immunology Letters, 2024, 265: 108345.
FAQ
The supernatant is then subjected to primary gel filtration chromatography with a pH 3.0 to pH 4.0 acetate buffer to separate mellittin Then, a method of separating malittin such that phospholipase A2, which is an enzyme responsible for allergy generation, is isolated by neutralizing the separated melittin tablets with NaOH by
At the psychophysical and behavioral levels, subcutaneous injection of melitin causes tonic pain sensation and pain-related behaviors in both humans and animals. At the cellular level, melitin activates primary nociceptor cells through direct and indirect effects.
A separation and purification method of melitin includes: using water to soak the coarse bee venom, using ethanol to precipitate the filtrate, extracting the sediment using ammonium hydroxide and n-butanol, using acetone to precipitate the extract, dissolving the sediments in a carbamide acetate buffering liquid A.
Malittin is a peptide and a principal component of bee venom. Several preclinical studies have found malittin to exhibit antitumor properties. Laboratory studies continue to find that melitin can interfere with key cancer signaling pathways.Melitin from honey bee venom.
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