Analytical Data
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Gene name
Cathepsin K
- Application
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Alternative Names
CTSKCathepsin K; EC 3.4.22.38
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Species
Cynomolgus
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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
P61276
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Expression Region
115-329aa
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Molecular Weight
27.5 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
EPHX1, or epoxide hydrolase 1, is an important enzyme involved in the metabolism of epoxides, which are reactive compounds formed during the biotransformation of various xenobiotics and endogenous substances. This enzyme plays a crucial role in detoxifying potentially harmful epoxide intermediates, thus protecting cells from oxidative damage and contributing to overall metabolic homeostasis. Recent studies have underscored the significance of EPHX1 in drug metabolism and its association with various diseases, including cancers and cardiovascular disorders. The recombinant expression of EPHX1 protein has emerged as a valuable tool for studying its biochemical properties and functional roles in cellular pathways. By generating large quantities of pure EPHX1, researchers can investigate its substrate specificity, enzymatic activity, and interactions with other proteins. Furthermore, understanding the structure-function relationships of EPHX1 may provide insights into its regulatory mechanisms and potential therapeutic targets. Given its implications in drug development and personalized medicine, ongoing research on EPHX1 recombinant protein is essential for elucidating its role in human health and disease.
