Analytical Data
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Gene name
xylF
- Application
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Alternative Names
(HMSH)(2-hydroxymuconic semialdehyde hydrolase)
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Species
Pseudomonas putida
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23106
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Expression Region
1-281aa
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Molecular Weight
38.0 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 the xylF gene, which encodes a key enzyme involved in the anaerobic degradation of xylenes, has garnered significant attention due to its ecological and industrial implications. Xylenes, aromatic hydrocarbons found in various environmental matrices, are of paramount concern due to their toxicity and potential for bioaccumulation. Understanding the xylF gene's function can provide insights into microbial pathways that facilitate the biodegradation of these compounds, offering prospects for bioremediation strategies to mitigate environmental pollution. The recombinant expression of the xylF protein allows for the detailed characterization of its enzymatic properties, substrate specificity, and catalytic mechanisms, advancing our knowledge of xylene metabolism. Additionally, exploring the functionality of xylF in engineered microbial systems could enhance the efficiency of bioprocesses aimed at detoxifying contaminated environments. The increasing prevalence of aromatic pollutants necessitates a deeper understanding of microbial adaptations, thereby emphasizing the importance of xylF research in both environmental microbiology and biotechnology fields.
