Analytical Data
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基因名
bnk
- Application
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别名
bnk; CG1480; Protein bottleneck
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种属
Drosophila melanogaster
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表达系统
E. coli
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P40794
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表达区间
1-303aa
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分子量
37.6 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
BNK (Bacillus thuringiensis Cry protein) recombinant proteins are an area of significant research due to their potential applications in biotechnology and agriculture. These proteins, originally derived from the bacterium Bacillus thuringiensis, exhibit insecticidal properties that are particularly useful for pest control in agricultural crops. The resurgence of interest in sustainable farming practices and the need for alternatives to chemical pesticides have spurred extensive studies on the genetic engineering of BNK proteins to enhance their efficacy and specificity against target pests while minimizing non-target effects. Recent advancements in synthetic biology and protein engineering techniques have allowed researchers to tailor these proteins to improve their stability, activity, and safety profiles. Consequently, optimizing BNK recombinant proteins can lead to the development of bio-pesticides that are not only effective but also environmentally friendly. Furthermore, understanding the mechanisms of action of these proteins at the molecular level paves the way for innovations in pest management strategies that align with integrated pest management and sustainable agriculture principles. The ongoing research in this domain seeks to unravel the complexities of protein interactions and to harness these insights to create novel agricultural solutions that address the global challenges of food security and environmental sustainability.
