Analytical Data
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Gene name
apr
- Application
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Alternative Names
subC; apr; Subtilisin Carlsberg; EC 3.4.21.62
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Species
Bacillus licheniformis
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P00780
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Expression Region
106-379aa
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Molecular Weight
42.0 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
The study of reprogrammed proteins, particularly Amidase-Protease Reprogrammed (APR) proteins, has gained significant attention in the field of molecular biology and biotechnology due to their potential applications in various industries, including pharmaceuticals and environmental cleanup. APR proteins are engineered to possess dual functionalities: they can selectively cleave peptide bonds in proteins while simultaneously exhibiting enzymatic properties that allow for the breakdown of harmful substances. This dual capability makes them valuable tools for both therapeutic applications, such as targeted drug delivery and protein degradation in diseases, and bioremediation efforts, where they can help in the detoxification of environmental pollutants. Research in this area focuses on understanding the structural and functional aspects of APR proteins, as well as optimizing their performance through genetic engineering and synthetic biology approaches. Investigations into the mechanisms governing their activity and stability are crucial for enhancing their efficacy in practical applications. As the demand for sustainable and efficient biocatalysts grows, APR proteins represent an innovative solution, bridging the gap between natural and synthetic biology while paving the way for advanced therapeutic and environmental solutions. Thus, the exploration of APR proteins not only contributes to fundamental scientific knowledge but also holds promise for addressing pressing global challenges.
