Analytical Data
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Gene name
aprA
- Application
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Alternative Names
(Alkaline metalloproteinase)(AP)
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Species
Pseudomonas aeruginosa
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q03023
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Expression Region
37-479aa
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Molecular Weight
50.6 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
AprA, a member of the subtilisin-like serine protease family, has garnered significant research interest due to its potential applications in biotechnology and medicine. This enzyme, originally derived from the bacterium Bacillus, plays a crucial role in protein degradation and processing, which is vital for various biological functions. Understanding the structure and function of AprA can lead to applications in food industry processes, pharmaceutical developments, and environmental biotechnology, where proteases are fundamental for breaking down organic materials. Researchers have been particularly focused on recombinantly expressing AprA to study its enzymatic properties, stability, and substrate specificity. The recombinant protein can be produced in larger quantities and with more consistent quality compared to its native counterpart. Additionally, engineering AprA through mutations or fusions can enhance its activity and optimize its performance for specific industrial applications. Recent developments using techniques such as site-directed mutagenesis and protein engineering have further elucidated its mechanistic aspects, paving the way for novel applications. By exploring its biochemical characteristics and catalytic mechanisms, these studies aim to harness AprA's potential in diverse fields including biocatalysis, where sustainable and efficient enzymatic processes are sought after. The ongoing research into AprA not only enhances our understanding of serine proteases but also contributes to the broader goal of developing green technologies through biocatalysis and enzymatic processes.
