Analytical Data
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Gene name
aerA
- Application
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Alternative Names
Aerolysin; aerA; Aeromonas hydrophila; Toxin
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Species
Others
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P09167
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Expression Region
A24-Q493
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Protein Length
Full Length of Mature Protein
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Molecular Weight
52.0 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
AerA, a protein that has garnered significant attention in recent years, is a member of the aerotaxis gene family and is associated with bacterial adaptation to varying oxygen levels. Originally identified in *Escherichia coli*, AerA plays a crucial role in sensing oxygen and regulating motility in response to aerobic and anaerobic conditions. Its unique structure, featuring a PAS (Per-ARNT-Sim) domain, allows it to function as a sensor that transduces environmental oxygen signals into cellular responses, thereby influencing cell behavior and survival. Understanding AerA's biochemical properties and its role in bacterial physiology has vital implications, particularly in the context of pathogenic bacteria where oxygen tension varies within host environments. This can inform strategies for developing novel antimicrobial agents or treatments to combat infections. The recombinant expression of AerA has become a focal point for researchers aiming to elucidate its functionality and interactions, providing insights into its potential applications in biotechnology and medicine. By studying the recombinant AerA protein, researchers can explore its structural conformations and elucidate the mechanisms by which it mediates responses to oxygen, thereby enhancing our understanding of microbial ecology and the molecular basis of aerotaxis. This research is essential for developing innovative approaches to manipulate bacterial behavior, which could lead to advancements in synthetic biology and therapeutic interventions. The ongoing exploration of AerA's dynamics promises to contribute significantly to the broader field of microbial biology and environmental adaptation.











