Analytical Data
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Gene name
EPHX1
- Application
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Alternative Names
EPHX1；EPHX；EPOX;Epoxide hydrolase 1
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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
P07099
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Expression Region
1-455aa
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AA Sequence
MWLEILLTSVLGFAIYWFISRDKEETLPLEDGWWGPGTRSAAREDDSIRP FKVETSDEEIHDLHQRIDKFRFTPPLEDSCFHYGFNSNYLKKVISYWRNE FDWKKQVEILNRYPHFKTKIEGLDIHFIHVKPPQLPAGHTPKPLLMVHGW PGSFYEFYKIIPLLTDPKNHGLSDEHVFEVICPSIPGYGFSEASSKKGFN SVATARIFYKLMLRLGFQEFYIQGGDWGSLICTNMAQLVPSHVKGLHLNM ALVLSNFSTLTLLLGQRFGRFLGLTERDVELLYPVKEKVFYSLMRESGYM HIQCTKPDTVGSALNDSPVGLAAYILEKFSTWTNTEFRYLEDGGLERKFS LDDLLTNVMLYWTTGTIISSQRFYKENLGQGWMTQKHERMKVYVPTGFSA FPFELLHTPEKWVRFKYPKLISYSYMVRGGHFAAFEEPELLAQDIRKFLS VLERQ
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Molecular Weight
76 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
EPHX1, or epoxide hydrolase 1, is a crucial enzyme involved in the metabolism of various endogenous and exogenous epoxides, which are reactive compounds that can induce cellular stress and damage. This enzyme plays a significant role in the detoxification process by converting these harmful epoxides into more water-soluble and less toxic diols, thus facilitating their excretion. Research on EPHX1 has gained attention due to its implications in pharmacology, toxicology, and disease pathology, particularly in cancer, cardiovascular diseases, and inflammatory conditions. Variants in the EPHX1 gene have been associated with altered enzyme activity, influencing individual susceptibility to drug-induced toxicity and the metabolism of environmental pollutants. Understanding the structure and function of EPHX1 through recombinant protein studies can provide insights into its catalytic mechanisms and regulatory processes. This knowledge is essential for developing therapeutic strategies aimed at enhancing detoxification and mitigating the adverse effects of epoxide exposure. Additionally, the production of recombinant EPHX1 proteins enables high-throughput screening endeavors for potential drugs that modulate its functions, thereby offering promising avenues for personalized medicine, especially in individuals with high-risk genotypes. Overall, the exploration of EPHX1 through recombinant technology serves as a vital component in elucidating its biological significance and therapeutic potential in managing various health conditions.
