Analytical Data
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基因名
Carbonyl reductase
- Application
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别名
Carbonyl reductase
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种属
Others
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表达系统
E. coli
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标签
His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
A0A0M1NYQ5
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表达区间
M1-W235
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蛋白长度
Full Length
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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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.












