Analytical Data
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Gene name
xylE
- Application
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Alternative Names
CatO2ase Catechol 2,3-dioxygenase
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Species
Pseudomonas putida
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P06622
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Expression Region
1-307aa
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Molecular Weight
55.2 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 xylE gene encodes for a key enzyme in the degradation of aromatic compounds, specifically catechol, within the metabolic pathway of certain bacteria capable of utilizing aromatic compounds as carbon sources. This gene is often studied in the context of bioremediation and environmental microbiology, as its encoded protein plays a crucial role in breaking down toxic pollutants. The reconstruction of xylE protein allows researchers to explore its enzymatic properties, substrate specificity, and potential applications in bioremediation strategies. Given the growing environmental concerns related to aromatic hydrocarbons, such as those found in oil spills and industrial waste, understanding the function and mechanics of xylE becomes essential. Protein engineering and recombinant technology have facilitated the production of xylE protein in model organisms, enabling detailed biochemical characterization. Studying xylE and its recombinant variants enhances our knowledge of bacterial metabolism and can lead to the development of engineered microbial strains with improved capacities for pollutant degradation, thus contributing to sustainable environmental management practices. This research not only highlights the potential of microbial biocatalysts in detoxifying contaminated environments but also underscores the interrelationship between microbial activity and biotechnological advancements in solving environmental challenges.
