Analytical Data
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基因名
cry1Ia
- Application
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别名
81 kDa crystal protein;Crystaline entomocidal protoxin;Insecticidal delta-endotoxin CryII(a)
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种属
Bacillus thuringiensis subsp. Kurstaki
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表达系统
E. coli
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标签
N- His-KSI
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q45752
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表达区间
97-180aa
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分子量
24.9 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Cry1Ia is a member of the Cry protein family produced by the bacterium *Bacillus thuringiensis* (Bt), which is widely recognized for its insecticidal properties, particularly against certain lepidopteran pests. This protein exhibits a structure that is conducive to binding specific receptors in the midgut of target insects, leading to cell lysis and ultimately the death of the insect. The research on Cry1Ia recombinant proteins has gained significant attention due to their potential application in biotechnology and agriculture as natural insecticides, offering an environmentally friendly alternative to chemical pesticides. Specifically, studies aim to characterize the efficacy, specificity, and mode of action of Cry1Ia against various agricultural pests. Understanding the molecular mechanisms underlying its insecticidal activity can facilitate the development of genetically modified crops that express Cry1Ia, enhancing pest resistance while minimizing ecological impact. Furthermore, exploring the resistance mechanisms in target pests can inform strategies to delay or prevent the emergence of resistance, ensuring the long-term effectiveness of Bt-based biopesticides. As agricultural practices increasingly lean towards sustainable solutions, the investigation of Cry1Ia recombinant proteins not only contributes to pest management strategies but also aligns with global efforts to promote environmentally sustainable agricultural practices. Hence, ongoing research is focused on optimizing expression systems, improving protein stability, and enhancing insecticidal activity, which collectively highlight the significance of Cry1Ia in the context of both fundamental research and practical agricultural applications.
