Analytical Data
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Gene name
nfsA
- Application
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Alternative Names
nfsA；mda18；mdaA；ybjB；Oxygen-insensitive NADPH nitroreductase
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P17117
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Expression Region
1-240aa
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AA Sequence
MTPTIELICGHRSIRHFTDEPISEAQREAIINSARATSSSSFLQCSSIIRITDKALREELVTLTGGQKHVAQAAEFWVFCADFNRHLQICPDAQLGLAEQLLLGVVDTAMMAQNALIAAESLGLGGVYIGGLRNNIEAVTKLLKLPQHVLPLFGLCLGWPADNPDLKPRLPASILVHENSYQPLDKGALAQYDEQLAEYYLTRGSNNRRDTWSDHIRRTIIKESRPFILDYLHKQGWATR
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Molecular Weight
28.8 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
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Protein Description
NfsA, a member of the nitroreductase family, has garnered significant attention in recent years due to its potential applications in bioremediation and pharmaceuticals. The enzyme is known for its ability to reduce nitro groups in various compounds, thereby transforming potentially toxic pollutants into less harmful substances. Research has highlighted its significance in the metabolism of nitro-containing drugs, where it plays a crucial role in drug activation and detoxification processes. Despite its biological relevance, the structural and functional characterization of NfsA remains underexplored, limiting our understanding of its catalytic mechanisms and substrate specificity. Advances in recombinant DNA technology have facilitated the expression and purification of NfsA, enabling detailed studies of its properties and functions. Furthermore, the enzyme's potential in biotechnological applications, such as in the development of biosensors and targeted drug delivery systems, underscores the importance of understanding its functional dynamics. Ongoing research aims to elucidate the enzyme's structure-function relationships, enhancing its application prospects in environmental and medicinal chemistry. By investigating NfsA's mechanisms of action and interaction with various substrates, scientists seek to unlock its full potential and harness its capabilities for innovative solutions to complex biochemical challenges.
