关键信息
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基因名
nirK
- 应用
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别名
nirK；Copper-containing nitrite reductase
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种属
E.coli
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P81445
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表达区间
1-330aa
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氨基酸序列
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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分子量
34.4 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.
质检流程
相关产品
背景信息
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.
