Analytical Data
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Gene name
uxuA
- Application
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Alternative Names
D-mannonate hydro-lyase
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Species
Sorangium cellulosum
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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
A9EVN4
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Expression Region
1-357aa
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Molecular Weight
55.7 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
The study of uxuA recombinant proteins has garnered considerable attention due to their pivotal role in microbial metabolism and potential applications in biotechnology and medicine. The uxuA gene, typically associated with the utilization of uronic acids, encodes an enzyme that is critical for the conversion of these compounds into usable forms of energy for microorganisms. Understanding the structure and function of uxuA proteins can provide insights into metabolic pathways that are crucial for the degradation of plant-derived materials, such as pectin and hemicellulose, thereby presenting opportunities for advancements in bioremediation and biofuel production. In recent years, researchers have focused on recombinant expression systems to produce uxuA proteins in larger quantities and in a more purified form. This approach aids in elucidating the detailed biochemical properties and enzymatic functions of these proteins. Furthermore, exploring the diverse applications of uxuA recombinant proteins in industrial processes, such as waste treatment and the food industry, can lead to innovative solutions for environmental challenges and sustainable practices. The ongoing research into uxuA proteins demonstrates their significance in both fundamental microbiology and applied sciences, making them an attractive subject for further exploration in the context of metabolic engineering and synthetic biology.
