Analytical Data
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基因名
Halohydrin epoxidase A
- Application
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别名
Tistrella mobilis (strain KA081020-065)
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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
I3TGI9
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表达区间
M1-P248
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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
Halohydrin epoxidase A (HheA) is an enzyme that plays a crucial role in the biotransformation of halohydrins to epoxides, which are valuable intermediates in organic chemistry and pharmaceuticals. The increased interest in green chemistry and sustainable processes has driven the need for efficient biocatalysts like HheA that can facilitate the conversion of halogenated compounds into epoxides under mild conditions, minimizing the use of harsh chemicals and solvents. The ability of HheA to exhibit regio- and stereoselectivity makes it particularly attractive for synthetic applications. The recombinant production of HheA allows for the optimization of enzyme properties through genetic engineering, resulting in enhanced activity and stability. Understanding the structural and functional characteristics of HheA, as well as the underlying catalytic mechanisms, can lead to improved enzyme designs tailored for industrial applications. Furthermore, the study of HheA contributes to the broader field of enzymology, where insights into enzyme evolution and adaptation can inform the development of new biocatalysts for diverse applications. With the growing emphasis on environmentally friendly practices, research on HheA and its recombinant forms holds significant promise for advancing biotechnological innovations in organic synthesis and beyond.












