Analytical Data
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Gene name
aiiA
- Application
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Alternative Names
AHL-lactonase AiiA
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Species
Bacillus thuringiensis subsp. Kurstaki
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0CJ63
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Expression Region
1-250aa
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Molecular Weight
35.7 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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 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.
