Analytical Data
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Gene name
CarE
- Application
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Alternative Names
/
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Species
Laodelphax striatella
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Source
E. coli
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Tag
C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
E5FQV0
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Expression Region
1-547aa
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Molecular Weight
61.5 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
Related Products
Protein Description
CarE (carboxylesterase) proteins are a group of enzymes that play a crucial role in the hydrolysis of ester bonds in various biological processes, including drug metabolism and lipid metabolism. Their significant involvement in breaking down xenobiotics and prodrug activation has garnered considerable interest within pharmacology and toxicology research. Recent studies have highlighted the diversity and functional variability of CarE isoforms, particularly in relation to their substrate specificity and tissue distribution. This variability is particularly notable in the context of therapeutic interventions, where understanding CarE activity can inform dosing regimens and enhance drug efficacy while minimizing adverse reactions. Additionally, the increasing prevalence of environmental pollutants and their esterified derivatives, alongside the rise of enzyme engineering technologies, has prompted further investigation into the potential for CarE proteins in bioremediation and biotransformation processes. The exploration of CarE's structural biology and its recombinant forms also holds promise for the biotechnological industry, allowing for the design of tailored enzyme solutions for specific applications. Thus, the study of CarE recombinant proteins is not only critical for advancing our knowledge of enzymatic functions but also for addressing practical challenges in health, environmental science, and industrial biotechnology.
