| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | botA |
| Uniprot No | P0DPI0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-436aa |
| 氨基酸序列 | MPFVNKQFNYKDPVNGVDIAYIKIPNVGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLKNFTGLFEFYKLLCVRGIIT |
| 预测分子量 | 52.0 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botA重组蛋白的虚构参考文献示例(仅供格式参考，非真实文献)：
1. **《重组botA蛋白在大肠杆菌中的高效表达及纯化》**
作者：Zhang L. et al.
摘要：本研究构建了botA毒素Hc结构域的重组表达载体，利用大肠杆菌BL21系统实现可溶性表达，通过镍柱亲和层析获得高纯度蛋白，为疫苗开发提供基础。
2. **《BotA重组蛋白的晶体结构解析与功能域研究》**
作者：Smith J.R., Patel K.
摘要：通过X射线衍射解析了重组botA蛋白的晶体结构(分辨率2.1Å)，揭示了其受体结合域的关键氨基酸位点，为毒素抑制剂的分子设计提供依据。
3. **《基于重组botA的神经毒素中和抗体筛选》**
作者：Wang Y. et al.
摘要：利用重组botA蛋白构建体外中和模型，筛选出3种单克隆抗体，动物实验显示其可显著降低毒素引起的肌肉麻痹效应。
4. **《定向进化改良重组botA蛋白的稳定性》**
作者：Kim S., Müller T.
摘要：采用易错PCR技术对重组botA进行定向进化，获得热稳定性提高的突变体(Tm值提升8℃)，拓展了其在高温环境下的工业应用潜力。
注：以上内容为模拟文献，实际研究中请通过PubMed、Web of Science等平台检索真实数据。
BotA recombinant protein refers to a genetically engineered form of the botulinum neurotoxin type A (BoNT/A), a potent toxin produced by the bacterium *Clostridium botulinum*. BoNT/A is a zinc-dependent protease that inhibits acetylcholine release at neuromuscular junctions, leading to muscle paralysis. While native BoNT/A is a dangerous neurotoxin responsible for botulism, its recombinant derivatives have been extensively studied and repurposed for therapeutic and cosmetic applications due to their targeted neuro-modulatory effects.
The recombinant BotA protein is typically produced by expressing specific domains of the toxin (e.g., the light chain or binding domain) in bacterial or eukaryotic expression systems like *E. coli* or CHO cells. These systems enable scalable production while eliminating the toxin’s inherent toxicity through domain truncation or mutagenesis. Researchers often focus on the light chain (LC) domain, which retains proteolytic activity but lacks the native toxin’s cellular entry machinery, making it safer for experimental use.
BotA recombinant proteins are pivotal in neuroscience research, particularly for studying synaptic vesicle exocytosis and neuronal signaling. They also serve as tools for developing anti-botulism therapeutics, including vaccines and neutralizing antibodies. In clinical settings, modified BoNT/A derivatives (e.g., Botox) are FDA-approved for treating conditions like chronic migraines, muscle spasticity, and aesthetic wrinkle reduction. Ongoing research explores engineered BotA variants with enhanced specificity, reduced immunogenicity, or extended duration of action. Additionally, recombinant BotA fragments are used in diagnostics to detect botulism or assess toxin-neutralizing antibody responses. The development of these proteins exemplifies the intersection of toxin biology, protein engineering, and translational medicine.
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