Analytical Data
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基因名
hup
- Application
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别名
hup;HUP2;Paired box Protein Pax-3
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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
P0C0H2
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表达区间
1-91aa
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氨基酸序列
MANKQDLIAKVAEATELTKKDSAAAVDAVFSTIEAFLAEGEKVQLIGFGNFEVRERAARKGRNPQTGAEIEIAASKVPAFKAGKALKDAVK
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分子量
17.1 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
The study of Hup (hydrogenase upstream) recombinant proteins has gained significant attention due to their critical roles in various biological processes, particularly in photosynthetic organisms and certain bacteria. Hup proteins are associated with hydrogen production and are often involved in metabolic pathways that enhance energy efficiency and sustainability. The drive towards renewable energy sources has emphasized the importance of understanding these proteins, as they can facilitate the development of biohydrogen production systems. Recombinant DNA technology enables the expression and characterization of Hup proteins in various model organisms, allowing researchers to elucidate their structure, function, and mechanisms of action. This research not only contributes to basic biochemical knowledge but also has practical applications in bioengineering and the design of microbial systems for sustainable energy generation. Moreover, the exploration of Hup protein interactions and regulatory pathways can offer insights into how organisms adapt to fluctuating environmental conditions, providing a broader understanding of metabolic flexibility in microbial communities. As such, research on Hup recombinant proteins stands at the intersection of microbiology, biochemistry, and renewable energy technology, highlighting their potential for advancing both fundamental science and practical applications in addressing global energy challenges.












