Analytical Data
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基因名
Epoxide hydrolase
- Application
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别名
Bacillus gobiensis; Hydrolase
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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
A0A0M4FVH2
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表达区间
M1-G315
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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
Epoxide hydrolases (EHs) are a crucial group of enzymes that play a significant role in the metabolism of epoxides, which are reactive compounds formed during the degradation of various xenobiotics and biochemicals. These enzymes catalyze the hydrolysis of epoxides into less toxic diols, thereby preventing potential cellular damage and contributing to detoxification processes. The study of recombinant epoxide hydrolase proteins has gained prominence in recent years due to their importance in drug metabolism, environmental bioremediation, and the bioactivation of epoxide-containing drugs, which can have both therapeutic and adverse effects. Advances in molecular biology techniques allow the functional expression of EHs in various host systems, facilitating the characterization and engineering of these enzymes to enhance their catalytic efficiency and substrate specificity. Additionally, understanding the structure-function relationships of recombinant EHs can provide insights into their evolutionary adaptations and potential applications in biotechnology. Research on recombinant EHs not only aids in elucidating the metabolic pathways of epoxides but also opens avenues for developing novel therapeutic strategies and biocatalysts for industrial applications. As such, the investigation of these enzymes remains a vibrant field, merging biochemistry, pharmacology, and environmental science to address critical challenges in health and ecological sustainability.
