Analytical Data
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Gene name
narG
- Application
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Alternative Names
(Nitrate reductase A subunit alpha)(Quinol-nitrate oxidoreductase subunit alpha)
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Species
Escherichia coli
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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
P09152
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Expression Region
1-110aa
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Molecular Weight
20.5 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
NarG is a key subunit of the nitrate reductase enzyme complex, which plays a crucial role in the process of denitrification, an ecological process that reduces nitrate to nitrogen gas, thereby contributing to the nitrogen cycle and controlling nitrogen levels in the environment. Research on NarG is significant due to its involvement in microbial metabolism, particularly in anaerobic bacteria that thrive in oxygen-deprived conditions. Understanding the structure, function, and regulatory mechanisms of NarG has implications for bioremediation strategies and agricultural practices, as it can influence soil health and fertility. Additionally, the study of NarG and its recombined forms can provide insights into enzyme engineering for biotechnological applications, enhancing the efficiency of nitrate reduction processes in various industrial settings. Recent advances in molecular biology techniques have facilitated the manipulation of NarG to create recombinant proteins, enabling researchers to investigate the enzyme's characteristics in detail. This has opened new avenues for studying its kinetics, substrate specificity, and interaction with other components of the denitrification pathway, ultimately contributing to a better understanding of nutrient cycling in ecosystems and informing efforts to mitigate environmental issues related to nitrogen pollution. The exploration of NarG's role in microbial communities further underscores its importance in maintaining ecological balance, making it a focal point of research in environmental microbiology.
