| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | cry3Aa |
| Uniprot No | P0A379 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 58-644aa |
| 氨基酸序列 | DSSTTKDVIQKGISVVGDLLGVVGFPFGGALVSFYTNFLNTIWPSEDPWKAFMEQVEALMDQKIADYAKNKALAELQGLQNNVEDYVSALSSWQKNPVSSRNPHSQGRIRELFSQAESHFRNSMPSFAISGYEVLFLTTYAQAANTHLFLLKDAQIYGEEWGYEKEDIAEFYKRQLKLTQEYTDHCVKWYNVGLDKLRGSSYESWVNFNRYRREMTLTVLDLIALFPLYDVRLYPKEVKTELTRDVLTDPIVGVNNLRGYGTTFSNIENYIRKPHLFDYLHRIQFHTRFQPGYYGNDSFNYWSGNYVSTRPSIGSNDIITSPFYGNKSSEPVQNLEFNGEKVYRAVANTNLAVWPSAVYSGVTKVEFSQYNDQTDEASTQTYDSKRNVGAVSWDSIDQLPPETTDEPLEKGYSHQLNYVMCFLMQGSRGTIPVLTWTHKSVDFFNMIDSKKITQLPLVKAYKLQSGASVVAGPRFTGGDIIQCTENGSAATIYVTPDVSYSQKYRARIHYASTSQITFTLSLDGAPFNQYYFDKTINKGDTLTYNSFNLASFSTPFELSGNNLQIGVTGLSAGDKVYIDKIEFIPVN |
| 预测分子量 | 84.7 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Cry3Aa重组蛋白的3篇代表性文献的简要信息(注：文献为示例性概括，非真实存在)：
1. **文献名称**：*Expression and Insecticidal Activity of Recombinant Cry3Aa Protein in Escherichia coli*
**作者**：Zhang L, Wang Y, et al.
**摘要**：研究利用大肠杆菌表达系统成功表达Cry3Aa重组蛋白，经纯化后证实其对马铃薯甲虫(Leptinotarsa decemlineata)幼虫具有显著杀虫活性，LC50值为15 μg/g，为农业应用提供了潜在生物农药。
2. **文献名称**：*Structural Insights into Cry3Aa Toxin: Crystal Structure and Receptor Binding Analysis*
**作者**：Chen H, Li J, et al.
**摘要**：通过X射线晶体学解析Cry3Aa蛋白的三维结构(分辨率2.5 Å)，揭示了其结构域III中与鞘翅目昆虫中肠刷状缘膜受体互作的关键氨基酸残基，为抗性机制研究提供了分子基础。
3. **文献名称**：*Optimization of Cry3Aa Recombinant Production Using Bacillus subtilis and Toxin Stability Evaluation*
**作者**：Kim S, Park M, et al.
**摘要**：优化枯草芽孢杆菌表达系统生产Cry3Aa的发酵条件，使蛋白产量提高3倍，并证明重组蛋白在碱性环境(pH 9-11)下保持稳定，模拟昆虫中肠环境后仍保留90%以上杀虫活性。
4. **文献名称**：*Synergistic Effect of Cry3Aa and Plant Protease Inhibitors on Colorado Potato Beetle Control*
**作者**：Rodríguez A, Gómez-Ruiz S, et al.
**摘要**：发现Cry3Aa重组蛋白与植物源蛋白酶抑制剂(如大豆胰蛋白酶抑制剂)联用可显著增强对马铃薯甲虫的致死率，表明联合策略可延缓害虫抗性发展。
(注：以上文献信息为基于研究领域常见内容的模拟概括，实际引用请通过PubMed、Web of Science等平台检索真实文献。)
**Background of Cry3Aa Recombinant Protein**
Cry3Aa is a delta-endotoxin protein belonging to the Cry toxin family, produced by the soil bacterium *Bacillus thuringiensis* (Bt). These proteins are widely studied for their insecticidal properties, particularly against coleopteran pests like the Colorado potato beetle (*Leptinotarsa decemlineata*). Cry3Aa specifically targets the larval midgut epithelium, disrupting membrane integrity and causing cell lysis. Its mode of action involves binding to specific receptors on the insect gut lining, followed by pore formation, osmotic imbalance, and eventual death of the pest.
Recombinant Cry3Aa refers to the protein produced via genetic engineering in heterologous expression systems (e.g., *Escherichia coli* or yeast). This approach overcomes limitations of native Bt fermentation, such as low yield or instability. By cloning the *cry3Aa* gene into plasmids and optimizing expression conditions, researchers achieve scalable production. Recombinant technology also allows protein engineering to enhance toxicity, stability, or target specificity. For example, domain-swapping or site-directed mutagenesis can address resistance development in pests.
Cry3Aa has been pivotal in developing biopesticides and transgenic crops. Its specificity reduces non-target organism risks, aligning with sustainable agriculture goals. However, challenges persist, including variable field efficacy and regulatory hurdles for genetically modified organisms (GMOs). Ongoing research focuses on hybrid toxins, fusion proteins, and synergists to improve performance. Additionally, structural studies of Cry3Aa’s three-domain architecture (pore-forming, receptor-binding, and proteolytic domains) provide insights for rational design of next-generation insecticides.
In summary, Cry3Aa recombinant protein exemplifies the intersection of microbial ecology, molecular biology, and agricultural innovation, offering eco-friendly pest control solutions while driving advances in protein engineering and biotechnology.
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