Analytical Data
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基因名
POP5
- Application
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别名
Ribonuclease P/MRP protein subunit POP5. hPop5
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q969H6
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表达区间
1-163 aa
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氨基酸序列
MVRFKHRYLLCELVSDDPRCRLSLDDRVLSSLVRDTIARVHGTFGAAACSIGFAVRYLNAYTGIVLLRCRKEFYQLVWSALPFITYLENKGHRYPCFFNTLHVGGTIRTCQKFLIQYNRRQLLILLQNCTDEGEREAIQKSVTRSCLLEEEEESGEEAAEAME
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分子量
45.2 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
POP5, a crucial component of the RNase P complex, has garnered research interest due to its role in RNA processing and maturation. RNase P is essential for the cleavage of precursor tRNA molecules, a fundamental step in tRNA biogenesis that is vital for protein synthesis in all living organisms. Historically, studies have focused on understanding the mechanisms and structures of RNase P across various species, uncovering its evolutionary significance and functional diversity. POP5, specifically, has been identified as a protein that interacts with other RNase P subunits and contributes to substrate recognition and catalytic activity. Given its involvement in essential cellular processes, mutations or dysfunctions in POP5 can lead to various biological implications, including developmental disorders and diseases. Researchers have employed various biophysical and biochemical methods to investigate the structure-function relationship of POP5, aiming to elucidate its specific interactions within the RNase P complex and its broader implications in cellular homeostasis. Recent advances in structural biology have shed light on the conformational dynamics of POP5, providing insights into how its structure influences function. Understanding POP5 in the context of RNase P not only enhances our comprehension of RNA metabolism but also opens new avenues for therapeutic interventions targeting RNA-related pathologies. The study of POP5 remains a vibrant field, bridging molecular biology, genetics, and biochemistry, emphasizing the protein's essential role in ensuring the accuracy and efficiency of gene expression.
