| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Mel |
| Uniprot No | P61006 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-207aa |
| 氨基酸序列 | MAKTYDYLFKLLLIGDSGVGKTCVLFRFSEDAFNSTFISTIGIDFKIRTIELDGKRIKLQIWDTAGQERFRTITTAYYRGAMGIMLVYDITNEKSFDNIRNWIRNIEEHASADVEKMILGNKCDVNDKRQVSKERGEKLALDYGIKFMETSAKANINVENAFFTLARDIKAKMDKKLEGNSPQGSNQGVKITPDQQKRSSFFRCVLL |
| 预测分子量 | 23,6 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于Mel重组蛋白的示例性参考文献(注：部分信息为模拟示例，实际文献需通过学术数据库查询确认)：
1. **《Recombinant expression and functional characterization of Melittin as a potential anticancer agent》**
- 作者：Zhang, Y. et al. (2020)
- 摘要：研究通过大肠杆菌系统重组表达蜂毒肽(Melittin)，验证其诱导肿瘤细胞凋亡的能力及对正常细胞的低毒性，为抗癌药物开发提供依据。
2. **《Engineered Melittin-derived peptides with enhanced antimicrobial activity against multidrug-resistant bacteria》**
- 作者：Li, X. et al. (2018)
- 摘要：通过基因工程改造Melittin序列，提高其对耐药菌的穿透性和抗菌效果，同时降低溶血副作用，展示其在感染治疗中的潜力。
3. **《Optimization of recombinant Melittin production in Pichia pastoris and its application in drug delivery systems》**
- 作者：Wang, Q. et al. (2021)
- 摘要：利用毕赤酵母高效表达重组Melittin，并开发基于纳米颗粒的靶向递送系统，提升其稳定性和肿瘤靶向性。
4. **《Structural and mechanistic insights into Melittin-lipid interactions for membrane disruption》**
- 作者：Chen, L. et al. (2019)
- 摘要：通过分子动力学模拟和实验分析，揭示重组Melittin与细胞膜相互作用的分子机制，解释其选择性破坏癌细胞膜的分子基础。
**建议**：实际研究中请通过PubMed、Web of Science等平台，以“recombinant Melittin”、“Melanin recombinant protein”等关键词检索最新文献，或结合具体研究方向(如抗肿瘤、抗菌)筛选。
**Background of Recombinant Melittin (Mel) Protein**
Melittin, a major bioactive component of honeybee (*Apis mellifera*) venom, has garnered significant attention for its diverse biological properties, including antimicrobial, antiviral, and anticancer activities. Traditionally extracted directly from bee venom, melittin’s clinical application has been limited due to challenges in obtaining sufficient quantities, potential immunogenicity, and hemolytic toxicity. To overcome these hurdles, recombinant DNA technology has been employed to produce melittin as a recombinant protein (recombinant Mel), enabling scalable and controlled synthesis in heterologous expression systems such as *E. coli* or yeast.
Structurally, melittin is a 26-amino acid amphipathic peptide with a cationic N-terminal and hydrophobic C-terminal, allowing it to interact with cell membranes. This interaction underpins its ability to disrupt lipid bilayers, making it a potent lytic agent. However, its nonspecific cytotoxicity has driven research into engineered variants or delivery systems (e.g., nanoparticle encapsulation, fusion proteins) to enhance target specificity and reduce off-target effects.
Recent studies highlight recombinant Mel’s potential in oncology, where it induces apoptosis in cancer cells by activating caspases and disrupting mitochondrial membranes. It also exhibits synergism with conventional chemotherapeutics. Additionally, its antimicrobial properties are being explored against drug-resistant pathogens, while its anti-inflammatory effects are investigated for autoimmune diseases.
Despite promising applications, challenges remain in optimizing recombinant Mel’s stability, bioavailability, and safety profile. Ongoing research focuses on structural modifications, such as site-directed mutagenesis or PEGylation, to mitigate toxicity while preserving therapeutic efficacy. As a multifunctional peptide, recombinant Mel represents a compelling candidate for bridging natural venom-derived compounds with modern biopharmaceutical innovation.
×
