Analytical Data
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Gene name
EPHX1
- Application
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Alternative Names
Epoxide hydratase Microsomal epoxide hydrolase EPHX, EPOX
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Species
Human
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Source
E. coli
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Tag
N- His
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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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Molecular Weight
56.9 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
Prolyl Endopeptidase (PREP), an enzyme primarily found in the cytoplasm, plays a crucial role in the regulation of various physiological processes by hydrolyzing proline-containing peptides. Its significance is underscored by its involvement in the metabolism of neuropeptides and its potential implications in neurodegenerative disorders, including Alzheimer's disease and schizophrenia. Research into PREP has gained momentum due to its unique substrate specificity, which distinguishes it from other proteolytic enzymes. Recombinant PREP protein has become a valuable tool for studying its enzymatic activity, structure-function relationships, and interactions with its substrates. The production of recombinant PREP allows for more controlled investigations into its kinetics, inhibition, and potential as a therapeutic target. Furthermore, advances in molecular cloning and expression systems have facilitated the generation of sufficient quantities of this enzyme, making it easier to dissect its mechanisms of action and explore its roles in cellular signaling pathways. As researchers continue to uncover the multifaceted roles of PREP in health and disease, the recombinant protein stands at the forefront of studies aiming to develop targeted therapies for conditions associated with dysregulation of proline metabolism. Overall, the investigation of recombinant Prolyl Endopeptidase not only enhances our understanding of its biological functions but also paves the way for innovative approaches in the treatment of various diseases.
