Analytical Data
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基因名
POP4
- Application
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别名
POP4; RPP29; Ribonuclease P protein subunit p29; hPOP4; EC 3.1.26.5
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种属
Human
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O95707
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表达区间
1-220aa
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分子量
41.4 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 POP4, a crucial component of the ribonuclease P (RNase P) complex, has garnered significant interest in molecular biology due to its essential role in RNA metabolism and processing. RNase P is responsible for the maturation of pre-transfer RNA (tRNA) molecules by cleaving their 5' leader sequences, a process vital for proper protein synthesis and cellular function. POP4, being a pivotal subunit of the RNase P complex, contributes to the structural integrity and enzymatic activity of the ribonucleoprotein complex. Research on POP4 has expanded the understanding of ribonucleoprotein interactions and the regulation of RNA processing pathways. Additionally, studies investigating the functional consequences of POP4 deficiency or mutations have shed light on various cellular processes and potential links to human diseases. Understanding the molecular mechanisms involving POP4 may pave the way for therapeutic strategies targeting RNA processing disorders, enhancing the recognition of its role not just in basic biology but also in disease pathology. The continued exploration of POP4 and its interactions within the RNase P complex remains crucial for elucidating RNA biogenesis and improving our knowledge of the fundamental mechanisms guiding cellular homeostasis.
