Analytical Data
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Gene name
nirK
- Application
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Alternative Names
nirK；Copper-containing nitrite reductase
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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
P81445
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Expression Region
1-330aa
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AA Sequence
GLPRVAVDLV APPLVHPHSQ VAAGAPKVVQ FRMSIEEKKM VADDDGTTAQ AMTFNGSVPG PTLVVHEGDY IELTLVNPAT NSMPHNVDFH AATGALGGAG LTQVVPGQEA VLRFKADRSG TFVYHCAPAG MVPWHVVSGM NGALMVLPRD GLRDAAGAAL AYDRVYTIGE SDLYVPKAAD GNYSDYPALA SAYADTVAVM RTLTPSHAVF NGAVGALTGA NALTAAVGES VLIIHSQANR DSRPHLIGGH GDWVWTTGKF ANPPQLNMET WFIPGGSAAA ALYTFKQPGT YAYLSHNLIE AMELGAAAQA SVEGQWDDDL MTSVAAPGPA
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Molecular Weight
34.4 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
NirK is a copper-containing nitrite reductase that plays a crucial role in the denitrification process, converting nitrite (NO2-) to nitric oxide (NO), which is an essential step in the nitrogen cycle. The enzyme is primarily found in various bacteria, including pathogenic strains, where it facilitates anaerobic respiration and contributes to nitrogen removal from the environment. The study of NirK recombinant proteins has gained significant attention due to its potential applications in biotechnology and environmental science. Understanding the structural and functional characteristics of NirK can provide insights into enzyme mechanism, substrate specificity, and its role in microbial ecology. Furthermore, the recombinant expression of NirK allows researchers to produce sufficient quantities of the protein for detailed biochemical assays and structural studies. Recent advancements in protein engineering and purification techniques have enabled the exploration of NirK variants and their catalytic efficiencies. As environmental concerns grow regarding nitrogen pollution, characterizing NirK and similar enzymes could lead to innovative strategies for bioremediation and sustainable agriculture, highlighting their relevance in addressing global environmental challenges. Thus, the research on NirK recombinant proteins not only enhances our understanding of microbial metabolism but also underscores their potential in developing eco-friendly solutions to mitigate nitrogen-related issues.
