Analytical Data
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Gene name
Carbonyl reductase
- Application
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Alternative Names
Carbonyl reductase
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Species
Others
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Source
E. coli
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Tag
His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A0A0M1NYQ5
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Expression Region
M1-W235
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Protein Length
Full Length
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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
Carbonyl reductases (CBRs) are a group of NADPH-dependent enzymes that play a crucial role in the reduction of carbonyl compounds, particularly aldehydes and ketones, to their corresponding alcohols. These enzymes are significant in various biological and industrial processes, including the metabolism of drugs and xenobiotics, as well as the synthesis of valuable chiral alcohols used in pharmaceuticals and agrochemicals. The recombinant expression of carbonyl reductase proteins offers an opportunity to enhance their availability and activity, enabling detailed studies of their biochemical properties and potential applications. Recent advancements in genetic engineering and protein expression technologies have facilitated the production of these enzymes in heterologous systems, allowing for the optimization of their catalytic efficiency and stability. Moreover, the engineering of CBRs through site-directed mutagenesis or directed evolution approaches has the potential to create novel variants with improved substrate specificity or altered cofactor requirements. This research not only contributes to the understanding of the structure-function relationship of carbonyl reductases but also paves the way for their application in green chemistry, where biocatalysis can replace traditional chemical processes, leading to more sustainable manufacturing practices. As the demand for eco-friendly synthesis routes in the pharmaceutical industry increases, exploring the full potential of recombinant carbonyl reductases becomes imperative, highlighting their significance in biotechnological applications and the broader field of enzymology.
