| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | cry1Fb |
| Uniprot No | O66377 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 984-1159aa |
| 氨基酸序列 | VKGHVDVEEQNNHRSVLVVPEWEAEVSQEVRVCPGRGYILRVTAYKEGYGEGCVTIHEVDNNTDELKFSSNCEKEQVYPGNTVACNDYNKNHGANACSSRNGGYDESYESNSSIPADYAPVYEEEAYTDGQRGNPCEFNRGHTPLPAGYVTAELEYFPETDTVWVEIGETEGTFIV |
| 预测分子量 | 22.8 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Cry1Fb重组蛋白的3条参考文献示例(注：内容为模拟生成，仅供参考)：
1. **《Heterologous expression and insecticidal activity of Cry1Fb protein against Spodoptera frugiperda》**
- 作者：Zhang, Y. et al.
- 摘要：本研究在大肠杆菌中成功表达Cry1Fb重组蛋白，证实其对草地贪夜蛾(Spodoptera frugiperda)幼虫具有显著杀虫活性，LC50值为0.25 μg/mL，为转基因作物开发提供潜在候选毒素。
2. **《Binding characterization of Cry1Fb to cadherin-like receptors in Helicoverpa armigera midgut》**
- 作者：Wang, L. et al.
- 摘要：通过配体印迹实验，发现Cry1Fb能与棉铃虫(Helicoverpa armigera)中肠钙黏蛋白特异性结合，揭示其作用机制与细胞膜穿孔模型相关，解释了其对鳞翅目害虫的选择毒性。
3. **《Synergistic effect of Cry1Fb and Vip3Aa proteins on pest resistance management》**
- 作者：Liu, X. et al.
- 摘要：研究证明Cry1Fb与Vip3Aa蛋白联用可延缓亚洲玉米螟(Ostrinia furnacalis)抗性进化，协同增效比达5.3倍，为抗性治理策略提供理论依据。
4. **《Structural analysis of Cry1Fb toxin using cryo-electron microscopy》**
- 作者：Chen, J. et al.
- 摘要：通过冷冻电镜解析Cry1Fb蛋白三维结构(分辨率3.2 Å)，明确其结构域III中关键氨基酸残基与杀虫活性的关联，为理性设计高效突变体奠定基础。
(注：实际文献需通过学术数据库检索确认，以上为模拟内容框架。)
The Cry1Fb recombinant protein is a modified variant derived from the naturally occurring Cry1F insecticidal protein, originally identified in the soil bacterium *Bacillus thuringiensis* (Bt). Bt produces crystal (Cry) proteins during sporulation, which exhibit specific toxicity against insect pests. Cry1F, classified under the three-domain Cry toxin family, targets lepidopteran larvae by binding to midgut receptors, forming pores in cell membranes, and causing osmotic imbalance leading to insect death.
The Cry1Fb variant was engineered through recombinant DNA technology to enhance stability, expression efficiency, or pest resistance management. Such modifications often involve codon optimization for plant expression systems or amino acid substitutions to improve receptor binding affinity or circumvent insect resistance. Recombinant Cry1Fb has been widely utilized in transgenic crops, particularly maize and cotton, to control pests like fall armyworm (*Spodoptera frugiperda*) and European corn borer (*Ostrinia nubilalis*). Its integration into crops reduces reliance on synthetic pesticides, aligning with sustainable agriculture goals.
Safety assessments confirm Cry1Fb’s specificity to target insects, with minimal impact on non-target organisms, including mammals and beneficial insects, due to the absence of compatible gut receptors. Regulatory agencies, including the EPA and EFSA, have approved its use after rigorous evaluation. However, resistance evolution in pest populations remains a concern, prompting strategies like gene pyramiding (combining Cry1Fb with other Bt toxins) or refuge planting to delay resistance.
Ongoing research focuses on optimizing Cry1Fb’s performance under varying environmental conditions and expanding its applicability to other crops. Its development exemplifies the intersection of biotechnology and pest management, offering a targeted, eco-friendly alternative to broad-spectrum insecticides.
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