Analytical Data
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基因名
aiiA
- Application
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别名
AHL-lactonase AiiA
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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 & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P0CJ63
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表达区间
1-250aa
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分子量
35.7 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
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Protein Description
The study of aiiA, a gene encoding a protein involved in the degradation of N-acyl homoserine lactones (AHLs), has garnered significant attention in recent years due to its potential applications in controlling bacterial communication and quorum sensing. Quorum sensing is a crucial mechanism by which bacteria coordinate their behavior based on population density, influencing processes such as virulence, biofilm formation, and bioluminescence. AiiA, found in certain bacterial species, possesses the ability to hydrolyze AHLs, thereby disrupting these signaling pathways and presenting a novel strategy for combating bacterial infections and biofilm-related issues. The understanding of aiiA's structural and functional properties is essential for its potential engineering and therapeutic applications. Researchers are investigating the recombinant expression of aiiA to produce a purified protein that can be easily studied and applied in various settings, such as in medicine and biotechnology. This research aims to provide insights into aiiA's enzymatic mechanisms and its interactions with different AHL molecules, offering promising avenues for innovative treatments against pathogenic bacteria while minimizing the use of traditional antibiotics. Through detailed biochemical and biophysical studies, scientists seek to optimize aiiA for industrial and medical interventions, highlighting the importance of this protein in the broader context of microbial ecology and therapeutic development.












