Analytical Data
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Gene name
esterase
- Application
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Alternative Names
Arginine esterase; EC 3.4.21.35
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Species
Dog
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P09582
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Expression Region
25-260aa
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Molecular Weight
42 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
Esterases are a group of enzymes that catalyze the hydrolysis of ester bonds, playing vital roles in various biological processes, including metabolism, detoxification, and signal transduction. The study of esterase recombinant proteins has gained significant attention due to their industrial applications, particularly in biocatalysis, pharmaceuticals, and environmental remediation. Advances in molecular biology techniques, such as genetic engineering and synthetic biology, have enabled the production of recombinant esterases with enhanced stability, specificity, and activity. Researchers are increasingly focusing on the characterization of these enzymes, exploring their structure-function relationships to optimize their performance in diverse applications. Additionally, the ability to engineer esterases with tailored properties allows for more efficient and sustainable solutions in fields like biodiesel production, waste management, and the synthesis of chiral intermediates in drug development. As environmental concerns rise, the importance of utilizing biocatalysts, such as recombinant esterases, in green chemistry initiatives continues to grow, making this area of research pivotal for both scientific understanding and practical innovation.
