Analytical Data
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Gene name
EPHX3
- Application
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Alternative Names
(EH3)(Abhydrolase domain-containing protein 9)
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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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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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
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Protein Description
EPHX3, or epoxide hydrolase 3, is an enzyme that plays a crucial role in the metabolism of various xenobiotics and endogenous compounds by catalyzing the conversion of epoxides into their corresponding diols. This enzyme is part of the epoxide hydrolase family, which includes several isoforms with distinct tissue distributions and substrate specificities. Research into EPHX3 has gained attention due to its potential involvement in detoxification processes, inflammatory responses, and disease mechanisms, particularly in the context of cancer and cardiovascular diseases. The understanding of EPHX3’s functional properties and its interaction with various substrates could lead to significant insights into its role in human health and disease. Furthermore, the production of recombinant EPHX3 protein allows for detailed biochemical studies, including kinetic analyses and structural characterization, which are essential for elucidating the enzyme's mechanism and identifying potential inhibitors or activators. This research not only contributes to our fundamental understanding of human metabolism but also holds promise for therapeutic applications, especially in the development of drug-related interventions and personalized medicine strategies. Overall, EPHX3 represents a valuable target for ongoing research due to its multifaceted roles in physiology and pathology, making recombinant protein studies of this enzyme a critical focus in biomedical research.
