Analytical Data
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Gene name
Xylose reductase
- Application
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Alternative Names
xyr-1
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Species
Others
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q7SD67
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Expression Region
M1-G322
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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
Xylose reductase (XR) is an enzyme that plays a crucial role in the bioconversion of xylose, a five-carbon sugar prevalent in lignocellulosic biomass, into xylitol, a sugar alcohol with significant industrial applications, including food and pharmaceutical industries. The increasing demand for renewable energy and bio-based products has spurred research into efficient methods for biomass conversion, making XR a focal point in metabolic engineering and synthetic biology. Traditional sources of XR, such as certain fungi and bacteria, often have limitations related to low yields and enzyme stability. Therefore, recombinant protein technology has emerged as a viable solution to overcome these challenges. By cloning the gene encoding XR from various microorganisms and expressing it in heterologous systems, researchers aim to engineer more efficient versions of the enzyme with enhanced properties. This endeavor not only seeks to improve the efficiency of xylitol production but also to optimize the process by developing enzyme variants with tailored characteristics such as increased thermal stability, pH tolerance, and substrate specificity. As such, the recombinant production of XR offers a promising avenue to facilitate sustainable bioconversion processes and meet the growing demand for xylitol and other valuable sugar alcohols derived from renewable resources.
