Analytical Data
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Gene name
nahG
- Application
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Alternative Names
(Salicylate 1-monooxygenase)
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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
P23262
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Expression Region
2-434aa
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Molecular Weight
54.3 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 nahG gene, derived from the soil bacterium Pseudomonas putida, encodes a specific enzyme known as catechol 2,3-dioxygenase, which plays a crucial role in the microbial degradation of aromatic compounds, particularly naphthalene. This enzyme facilitates the conversion of catechol, an environmental pollutant, into less harmful products, thereby aiding bioremediation efforts. The study of NahG recombinant protein has gained significant attention due to its potential applications in environmental biotechnology and pollution management. By elucidating the biochemical mechanisms underlying its activity, researchers aim to enhance the efficiency of biodegradation processes, specifically in contaminated soils and water bodies. Furthermore, recombinant NahG can serve as a valuable tool in bioremediation, providing a means to engineer microbial strains with enhanced substrate specificity and degradation capabilities. The production and characterization of NahG have implications not only for environmental protection but also for advancing synthetic biology approaches. By harnessing this enzyme's unique properties, scientists hope to develop innovative strategies for the detoxification of recalcitrant pollutants, promoting sustainable practices in industrial waste management and environmental conservation. Overall, the exploration of nahG recombinant protein underscores the intersection of molecular biology, environmental science, and biotechnology, and highlights the critical importance of such research in addressing contemporary ecological challenges.
