| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | cry1Ac |
| Uniprot No | P05068 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 972-1178aa |
| 氨基酸序列 | LYDARNVIKNGDFNNGLSCWNVKGHVDVEEQNNQRSVLVVPEWEAEVSQEVRVCPGRGYILRVTAYKEGYGEGCVTIHEIENNTDELKFSNCVEEEIYPNNTVTCNDYTVNQEEYGGAYTSRNRGYNEAPSVPADYASVYEEKSYTDGRRENPCEFNRGYRDYTPLPVGYVTKELEYFPETDKVWIEIGETEGTFIVDSVELLLMEE |
| 预测分子量 | 25.8 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Cry1Ac重组蛋白的3篇参考文献摘要概括：
1. **《Expression and insecticidal activity of Cry1Ac toxin from Bacillus thuringiensis in Escherichia coli》**
作者：Adang, M.J. 等
摘要：研究利用大肠杆菌高效表达Cry1Ac蛋白，证实重组蛋白对棉铃虫幼虫具有显著杀虫活性，并优化了蛋白可溶性表达条件。
2. **《Mechanism of Cry1Ac toxin resistance in Helicoverpa armigera》**
作者：Wu, K.M. 等
摘要：分析棉铃虫对Cry1Ac蛋白的抗性机制，发现中肠细胞受体蛋白APN的表达下调导致毒素结合能力下降，揭示了抗性发展的分子基础。
3. **《Improvement of Cry1Ac toxicity by site-directed mutagenesis in a loop region of domain III》**
作者：Hernández-Rodríguez, C.S. 等
摘要：通过定点突变Cry1Ac结构域III的特定环区，增强其与昆虫受体的结合能力，显著提高了重组蛋白的杀虫效果。
**Background of Cry1Ac Recombinant Protein**
Cry1Ac is a recombinant protein derived from the soil bacterium *Bacillus thuringiensis* (Bt), a natural pathogen of insects. It belongs to the Cry (crystal) protein family, specifically the Cry1 class, which exhibits toxicity against certain insect pests. Cry proteins are δ-endotoxins produced during bacterial sporulation, forming crystalline inclusions that target insect midgut cells.
The Cry1Ac protein functions by binding to specific receptors, such as cadherin-like proteins and aminopeptidase N, on the surface of lepidopteran larval midgut epithelial cells. Upon ingestion by susceptible insects, the alkaline environment and proteases in the gut dissolve the crystal structure, releasing the protoxin. This protoxin is then cleaved into an activated toxin, which inserts into the cell membrane, forming pores that disrupt osmotic balance and lead to cell lysis, ultimately causing insect death.
Recombinant Cry1Ac is engineered through genetic modification, where the *cry1Ac* gene is cloned into expression systems (e.g., *E. coli* or yeast) for large-scale production. Its specificity for pests like cotton bollworm (*Helicoverpa armigera*) and pink bollworm (*Pectinophora gossypiella*) has made it a cornerstone of agricultural biotechnology. Since the 1990s, transgenic crops expressing Cry1Ac, such as Bt cotton and Bt maize, have been widely adopted to reduce chemical pesticide use and enhance yield.
However, concerns over insect resistance evolution and potential ecological impacts have driven research into resistance management strategies, including gene stacking (e.g., combining Cry1Ac with Cry2Ab) and refuge policies. Cry1Ac remains a critical tool in integrated pest management, exemplifying the intersection of microbial genetics, biotechnology, and sustainable agriculture.
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