Analytical Data
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Gene name
nirS
- Application
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Alternative Names
(Cytochrome cd1)(Cytochrome oxidase)(Hydroxylamine reductase)
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Species
Pseudomonas stutzeri
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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
P24040
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Expression Region
127-560aa
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Molecular Weight
56.0 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
NirS, or nitrite reductase, is an enzyme found in various microorganisms that plays a crucial role in the denitrification process, which is vital for the nitrogen cycle and environmental sustainability. This enzyme catalyzes the reduction of nitrite (NO₂⁻) to nitric oxide (NO), a key step in the conversion of nitrogen oxides to nitrogen gas (N₂). The research on NirS recombinant proteins has gained prominence due to their potential applications in bioremediation and agricultural practices, addressing issues like soil fertility and water quality. Understanding the structure and function of NirS is essential for developing effective biocatalysts that can promote denitrification in specific environments. Advances in molecular cloning and expression systems have enabled the production of NirS as a recombinant protein, allowing detailed studies of its enzymatic activity, regulation, and interaction with other cellular components. Additionally, characterizing NirS at the molecular level can provide insights into the evolutionary adaptations of microorganisms in diverse habitats. As concerns about nitrogen pollution and environmental health intensify, further research into NirS and its recombinant forms holds promise for innovative solutions to mitigate the negative impacts of excess nitrogen in ecosystems.
