Analytical Data
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Gene name
EPHX3
- Application
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Alternative Names
EPHX3；ABHD9；Epoxide hydrolase 3
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H6B9
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Expression Region
43-360aa
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AA Sequence
ALTHVLCRPRRGCCGRRRSASPACLSDPSLGEHGFLNLKSSGLRLHYVSAGRGNGPLMLFLHGFPENWFSWRYQLREFQSRFHVVAVDLRGYGPSDAPRDVDCYTIDLLLVDIKDVILGLGYSKCILVAHDWGALLAWHFSIYYPSLVERMVVVSGAPMSVYQDYSLHHISQFFRSHYMFLFQLPWLPEKLLSMSDFQILKTTLTHRKTGIPCLTPSELEAFLYNFSQPGGLTGPLNYYRNLFRNFPLEPQELTTPTLLLWGEKDTYLELGLVEAIGSRFVPGRLEAHILPGIGHWIPQSNPQEMHQYMWAFLQDLLD
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Molecular Weight
43.9 kDa
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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
EPHX3 (epoxide hydrolase 3) is an important enzyme involved in the metabolism of xenobiotics and endogenous compounds, specifically in the hydrolysis of epoxides to diols. This enzymatic activity plays a critical role in detoxifying various carcinogenic substances and contributes to the regulation of lipid metabolism. Research into EPHX3 is particularly significant due to its potential implications in drug metabolism, environmental toxicology, and the development of therapeutic strategies for diseases linked to oxidative stress and inflammation. As an enzyme that influences the bioavailability and toxicity of multiple compounds, understanding its structure, function, and regulation can pave the way for advancements in pharmacology and toxicology. Recent studies have focused on characterizing recombinant forms of EPHX3 to explore its kinetic properties and substrate specificity, facilitating a deeper understanding of its role in various metabolic pathways. Moreover, investigating the polymorphisms in the EPHX3 gene can reveal correlations with individual susceptibilities to diseases and adverse drug reactions, underscoring the relevance of personalized medicine. Thus, the exploration of EPHX3 recombinant proteins holds promise for enhancing our comprehension of cellular detoxification processes and may contribute to innovations in treating conditions associated with epoxide exposure and related metabolic disorders.
