Analytical Data
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基因名
NIT2
- Application
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别名
NIT2;Omega-amidase NIT2
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种属
Human
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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
Q9NQR4
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表达区间
1-276aa
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氨基酸序列
MGSSHHHHHHSSGLVPRGSHMGSMTSFRLALIQLQISSIKSDNVTRACSF IREAATQGAKIVSLPECFNSPYGAKYFPEYAEKIPGESTQKLSEVAKECS IYLIGGSIPEEDAGKLYNTCAVFGPDGTLLAKYRKIHLFDIDVPGKITFQ ESKTLSPGDSFSTFDTPYCRVGLGICYDMRFAELAQIYAQRGCQLLVYPG AFNLTTGPAHWELLQRSRAVDNQVYVATASPARDDKASYVAWGHSTVVNP WGEVLAKAGTEEAIVYSDIDLKKLAEIRQQIPVFRQKRSDLYAVEMKKP
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分子量
33 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
NIT2, a member of the transition metal-dependent nitroreductase family, has garnered significant interest in recent years due to its potential applications in bioremediation and biotechnology. This enzyme is known for its ability to catalyze the reduction of nitro compounds, which are prevalent environmental pollutants arising from industrial activities and agricultural runoff. In bacterial systems, NIT2 plays a critical role in the metabolism of these compounds, necessitating a deeper understanding of its biochemical properties and mechanisms of action. Research into NIT2 has aimed to elucidate its structure-function relationship, thereby providing insights into its catalytic activity and substrate specificity. Advances in techniques such as recombinant DNA technology have facilitated the production of NIT2 as a recombinant protein, allowing for more detailed studies using various biophysical and biochemical methods. Moreover, as environmental concerns regarding nitro compound pollution continue to rise, NIT2's potential applications offer promising avenues for developing bioremediation strategies. By harnessing the unique properties of this enzyme, researchers aspire to create bio-based solutions that can effectively mitigate the adverse effects of nitro pollutants, contributing to a cleaner and more sustainable environment. This area of research highlights the intersection of protein engineering, environmental science, and biotechnology, making NIT2 a focal point in the quest for effective biodegradation technologies. As studies progress, the findings may lead to novel applications that extend beyond environmental remediation, potentially impacting areas such as pharmaceuticals and industrial processes.












