Analytical Data
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Gene name
Halohydrin epoxidase A
- Application
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Alternative Names
Tistrella mobilis (strain KA081020-065)
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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
I3TGI9
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Expression Region
M1-P248
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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
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.
