Analytical Data
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基因名
POP7
- Application
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别名
Ribonucleases P/MRP protein subunit POP7 homolog
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种属
Human
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表达系统
E. coli
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标签
N- GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O75817
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表达区间
1-140aa
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分子量
42.7 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
POP7, a key component of the ribonuclease P (RNase P) complex, has garnered significant attention in molecular biology due to its critical role in tRNA processing and maturation in eukaryotic cells. As an essential enzyme, RNase P catalyzes the 5' maturation of precursor tRNA molecules, thereby playing a vital part in protein synthesis and overall cellular function. Research into POP7's recombinant protein has been motivated by its potential implications in various biological processes and diseases, including its involvement in the regulation of RNA metabolism and gene expression. Moreover, understanding POP7 and the RNase P complex could unveil novel therapeutic targets for RNA-related disorders and contribute to advancements in synthetic biology, where engineered RNase P could be utilized for targeted RNA processing applications. The study of POP7’s structure and function through recombinant protein techniques provides insights into enzyme mechanics and interactions within the RNase P complex, ultimately enhancing our understanding of ribonucleoprotein function and its impact on cellular health. As a result, the investigation of POP7 as a recombinant protein has significant implications for both fundamental biology and potential clinical applications.
