Analytical Data
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Gene name
Carboxylesterase
- Application
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Alternative Names
Carboxylesterase; Thermobifida fusca; Thermomonospora fusca; Hydrolase; Serine esterase; 3.1.1.1
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Species
Others
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Source
E. coli
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Tag
His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P86325
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Expression Region
M1-L497
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Protein Length
Full Length
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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
Carboxylesterases (CEs) are a group of enzymes that play a crucial role in the hydrolysis of ester bonds in various substrates, including drugs, xenobiotics, and endogenous compounds. These enzymes are significant in pharmacology and toxicology due to their ability to metabolize a wide range of drugs, influencing drug efficacy and safety. Recent studies have highlighted the role of CEs in drug resistance and the metabolic activation of prodrugs, making them a focal point in drug development and personalized medicine. With advancements in recombinant DNA technology, researchers have begun to produce and manipulate carboxylesterase proteins to better understand their structure-function relationships and catalytic mechanisms. The ability to generate recombinant CEs allows for in-depth studies into their substrate specificity, enzymatic activity, and potential applications in bioremediation and biotransformation processes. Furthermore, the exploration of genetically engineered variants of carboxylesterases holds promise for enhancing their catalytic efficiency and stability, providing valuable tools in pharmaceutical applications. Overall, the growing interest in carboxylesterases as therapeutic targets and biocatalysts underscores their importance in biochemical research, making them a key focus for future investigations in enzymology and drug metabolism.
