Analytical Data
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基因名
nirS
- Application
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别名
(Cytochrome cd1)(Cytochrome oxidase)(Hydroxylamine reductase)
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种属
Pseudomonas stutzeri
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P24040
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表达区间
127-560aa
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分子量
56.0 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.
