Analytical Data
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Gene name
Epoxide hydrolase
- Application
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Alternative Names
Bacillus gobiensis; Hydrolase
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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
A0A0M4FVH2
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Expression Region
M1-G315
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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
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.
