Analytical Data
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Gene name
Thermostable xylanase
- Application
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Alternative Names
yieL; Uncharacterized protein YieL
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Species
E.coli
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P31471
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Expression Region
M1-K389
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Protein Length
Full Length
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Molecular Weight
44.9 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
Related Products
Protein Description
Thermostable xylanase is an enzyme that plays a crucial role in the degradation of xylan, a major component of hemicellulose found in plant biomass. The increasing demand for environmentally friendly and sustainable technologies in various industries, such as biofuel production, paper manufacturing, and feed processing, has driven research towards enzyme applications. Traditional xylanases often exhibit limited thermal stability, hindering their effectiveness in industrial processes that operate at elevated temperatures. Therefore, the development of thermostable xylanases through recombinant DNA technology represents a significant advancement in enzyme engineering. Recombinant proteins allow for the precise manipulation of xylanase genes, enabling researchers to enhance enzymatic properties such as stability, activity, and substrate specificity. By utilizing thermophilic microorganisms as sources of xylanase genes, scientists have been able to produce enzymes that maintain functionality under extreme conditions. The research surrounding thermostable xylanases not only contributes to improving industrial processes but also supports the broader field of biotechnology by underscoring the potential of enzymes as sustainable catalysts, thereby fostering innovations in renewable energy and green chemistry. As a result, the study of thermostable xylanase recombinant proteins continues to gain momentum, with implications for both environmental sustainability and economic efficiency in various sectors.
