Analytical Data
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基因名
rnhB
- Application
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别名
RNase HII
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种属
TNT-Thermus thermophilus
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表达系统
E. coli
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q5SLU5
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表达区间
1-203aa
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分子量
23.9 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 rnhB gene, which encodes the enzyme ribonuclease H (RNase H), plays a crucial role in the degradation of RNA-DNA hybrids generated during various cellular processes, including DNA replication and repair. RNase H enzymes are essential for maintaining genomic stability by eliminating these hybrids, which, if accumulated, can lead to genomic instability and contribute to various diseases, including cancer. Research on rnhB recombinant protein has gained traction due to its potential applications in biotechnology and medicine. By understanding the structure and function of the rnhB-encoded RNase H, scientists aim to utilize this enzyme in therapeutic settings, such as targeting RNA viruses or enhancing gene therapy strategies. Additionally, the production of rnhB as a recombinant protein allows for the detailed study of its enzymatic properties and mechanisms, providing insights that could lead to the development of novel inhibitors for therapeutic intervention. Current studies are focused on optimizing expression and purification techniques to obtain high-yield, functional RNase H proteins for experimental use, paving the way for future innovations in disease treatment and genetic engineering.
