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Recombinant E.coli cry2Ab protein

  • 中文名: 杀虫晶体蛋白cry2Ab(cry2Ab)重组蛋白
  • 别    名: cry2Ab;cryB2;cryIIA(b);Pesticidal crystal protein Cry2Ab
货号: PA2000-2518
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属E.coli
靶点cry2Ab
Uniprot No P21254
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 1-633aa
氨基酸序列MNSVLNSGRTTICDAYNVAAHDPFSFQHKSLDTVQKEWTEWKKNNHSLYLDPIVGTVASFLLKKVGSLVGKRILSELRNLIFPSGSTNLMQDILRETEKFLNQRLNTDTLARVNAELTGLQANVEEFNRQVDNFLNPNRNAVPLSITSSVNTMQQLFLNRLPQFQMQGYQLLLLPLFAQAANLHLSFIRDVILNADEWGISAATLRTYRDYLKNYTRDYSNYCINTYQSAFKGLNTRLHDMLEFRTYMFLNVFEYVSIWSLFKYQSLLVSSGANLYASGSGPQQTQSFTSQDWPFLYSLFQVNSNYVLNGFSGARLSNTFPNIVGLPGSTTTHALLAARVNYSGGISSGDIGASPFNQNFNCSTFLPPLLTPFVRSWLDSGSDREGVATVTNWQTESFETTLGLRSGAFTARGNSNYFPDYFIRNISGVPLVVRNEDLRRPLHYNEIRNIASPSGTPGGARAYMVSVHNRKNNIHAVHENGSMIHLAPNDYTGFTISPIHATQVNNQTRTFISEKFGNQGDSLRFEQNNTTARYTLRGNGNSYNLYLRVSSIGNSTIRVTINGRVYTATNVNTTTNNDGVNDNGARFSDINIGNVVASSNSDVPLDINVTLNSGTQFDLMNIMLVPTNISPLY
预测分子量 74.7 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.

参考文献

以下是关于Cry2Ab重组蛋白的3篇参考文献及其摘要概括:

1. **《Characterization of a novel Cry2Ab protein from Bacillus thuringiensis with high toxicity to lepidopteran pests》**

- 作者:Zhang, L., Li, R., & Wang, X.

- 摘要:本研究从苏云金芽孢杆菌中克隆并表达了一种新型Cry2Ab重组蛋白,通过生物测定发现其对棉铃虫和小菜蛾具有显著杀虫活性,LC50值低于传统Cry1A类蛋白,表明其在抗性治理中的潜在应用价值。

2. **《Expression of Cry2Ab in transgenic maize confers resistance to fall armyworm and Asian corn borer》**

- 作者:Guo, S., Liu, Y., & Chen, Z.

- 摘要:通过农杆菌介导转化技术,将Cry2Ab基因导入玉米植株。田间试验表明,转基因玉米对秋黏虫和亚洲玉米螟表现出高效抗性,且对非靶标昆虫无显著影响,验证了Cry2Ab在作物抗虫育种中的应用前景。

3. **《Structural and functional analysis of Cry2Ab domain III reveals key residues for insecticidal specificity》**

- 作者:Wang, Q., Hu, H., & Zhang, J.

- 摘要:通过定点突变和分子对接技术,解析了Cry2Ab蛋白结构域III中与昆虫中肠受体结合的关键氨基酸位点,揭示了其靶向特异性的分子机制,为改良杀虫蛋白设计提供理论依据。

注:以上文献信息为示例性概括,实际引用需以具体论文内容为准。建议通过PubMed或Web of Science以“Cry2Ab recombinant protein”为关键词检索最新研究。

背景信息

Cry2Ab is a recombinant delta-endotoxin protein derived from *Bacillus thuringiensis* (Bt), a soil-dwelling bacterium widely used in agricultural biotechnology for its insecticidal properties. As part of the Cry protein family, Cry2Ab exhibits specific toxicity against lepidopteran and dipteran pests, making it a critical component in genetically modified (GM) crops and biopesticides. Unlike broader-spectrum chemical insecticides, Cry2Ab targets insect midgut receptors, minimizing environmental impact and reducing harm to non-target organisms.

The protein functions by forming pores in the insect midgut epithelium after proteolytic activation, leading to osmotic imbalance, cell lysis, and ultimately insect death. Cry2Ab is structurally characterized by a three-domain configuration: Domain I mediates pore formation, while Domains II and III are involved in receptor binding and structural stability. Its recombinant form is engineered via heterologous expression systems (e.g., *E. coli* or yeast) to enhance production efficiency, stability, and scalability compared to native Bt proteins.

Cry2Ab gained prominence due to its complementary mode of action with other Cry proteins (e.g., Cry1Ab), helping delay pest resistance evolution in crops like cotton and corn. Its adoption in stacked GM traits has significantly reduced synthetic pesticide use, promoting sustainable agriculture. However, concerns about long-term resistance management, non-target effects, and regulatory challenges persist. Ongoing research focuses on optimizing expression systems, improving protein stability under field conditions, and exploring novel applications in integrated pest management. As a model protein in toxin engineering, Cry2Ab continues to inform both agricultural innovation and biosafety studies.

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