Analytical Data
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基因名
aprE
- Application
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别名
aprE; apr; aprA; sprE; BSU10300; Subtilisin E; EC 3.4.21.62
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种属
Bacillus subtilis
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P04189
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表达区间
107-381aa
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分子量
43.7 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
Related Products
Protein Description
The study of aprE recombinant protein centers on the aprE gene, which encodes an extracellular serine protease produced by the bacterium *Bacillus subtilis*. This enzyme plays a significant role in various industrial applications, including food processing, textile, and detergent industries, due to its proteolytic activity and ability to function under a broad range of pH and temperature conditions. The recombinant production of aprE allows for a more efficient and scalable approach to obtain this important enzyme, as traditional methods of extraction from native sources can be labor-intensive and yield limited quantities. Genetic engineering techniques, such as cloning the aprE gene into suitable expression vectors, enable the overexpression of the protein in microorganisms like *E. coli* or *Bacillus* species. Research on aprE recombinant protein not only focuses on improving yield and activity through optimization of cloning and expression conditions but also aims to characterize the enzyme’s properties and enhance its stability and functionality for specific applications. Understanding the structure-function relationship of aprE and its potential modifications further opens avenues for tailored enzyme applications in biotechnological processes, contributing to greener and more efficient industrial practices.












