Analytical Data
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Gene name
EPHX4
- Application
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Alternative Names
EPHX4；ABHD7；EH4；EPHXRP；Epoxide hydrolase 4
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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
Q8IUS5
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Expression Region
1-362aa
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AA Sequence
MARLRDCLPRLMLTLRSLLFWSLVYCYCGLCASIHLLKLLWSLGKGPAQTFRRPAREHPPACLSDPSLGTHCYVRIKDSGLRFHYVAAGERGKPLMLLLHGFPEFWYSWRYQLREFKSEYRVVALDLRGYGETDAPIHRQNYKLDCLITDIKDILDSLGYSKCVLIGHDWGGMIAWLIAICYPEMVMKLIVINFPHPNVFTEYILRHPAQLLKSSYYYFFQIPWFPEFMFSINDFKVLKHLFTSHSTGIGRKGCQLTTEDLEAYIYVFSQPGALSGPINHYRNIFSCLPLKHHMVTTPTLLLWGENDAFMEVEMAEVTKIYVKNYFRLTILSEASHWLQQDQPDIVNKLIWTFLKEETRKKD
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Molecular Weight
45.2 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
EPHX4, or epoxide hydrolase 4, is an enzyme that plays a significant role in the biotransformation of xenobiotics and endogenous compounds through its ability to hydrolyze epoxides into their corresponding diols. This enzyme is part of the larger family of soluble epoxide hydrolases, which are crucial in the metabolism of fatty acids and the regulation of signaling molecules. Research on EPHX4 has gained attention due to its potential implications in drug metabolism, environmental toxicology, and disease processes, including cancer and cardiovascular disorders. Understanding the structure-function relationship of EPHX4 and its catalytic mechanisms is essential for elucidating its role in metabolic pathways and its impact on human health. Recombinant EPHX4 proteins produced through expression systems allow for the detailed study of this enzyme's kinetics, substrate specificity, and inhibition by various compounds. Furthermore, exploring EPHX4’s interactions with other biomolecules can reveal its involvement in complex biological systems and provide insights into therapeutic targets for diseases associated with disrupted lipid metabolism. Overall, the study of EPHX4 recombinant proteins is crucial for advancing our comprehension of this enzyme's biochemical properties and its potential applications in pharmacology and toxicology.
