| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | POP7 |
| Uniprot No | O75817 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-140aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSEFMAENREPRGAVEAELDPVEYTLRKR LPSRLPRRPNDIYVNMKTDFKAQLARCQKLLDGGARGQNACSEIYIHGLG LAINRAINIALQLQAGSFGSLQVAANTSTVELVDELEPETDTREPLTRIR NNSAIHIRVFRVTPK |
| 预测分子量 | 18 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于POP7重组蛋白的3篇代表性文献的简要信息(部分内容基于模拟文献示例)：
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1. **文献名称**: *Recombinant Expression and Functional Characterization of Human RNase P Protein POP7*
**作者**: Zhang L, et al.
**摘要**: 本研究利用大肠杆菌系统成功表达并纯化重组人源POP7蛋白，通过体外酶活实验证实其与RNAse P其他亚基协同催化tRNA前体加工的能力，为解析RNAse P组装机制提供基础。
2. **文献名称**: *Structural Insights into POP7 Subunit in Archaeal RNase P Complex*
**作者**: Tanaka N, et al.
**摘要**: 通过重组表达古菌来源的POP7蛋白，结合X射线晶体学解析其三维结构，揭示其与RNA组分相互作用的关键结构域，阐明其在RNAse P复合体中的构象变化机制。
3. **文献名称**: *Optimization of POP7 Protein Production in Yeast for Therapeutic Screening*
**作者**: Gupta R, et al.
**摘要**: 开发了基于毕赤酵母的重组POP7高效表达系统，优化发酵条件使蛋白产量提升5倍，并验证其在基于RNAse P的基因治疗药物筛选中的应用潜力。
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注：以上文献为示例性内容，实际研究中请通过学术数据库(如PubMed、Web of Science)检索最新文献。若需具体文献，可提供更详细的研究方向或应用场景。
POP7. also known as RPP25 or RPP25L, is a conserved protein component of two essential ribonucleoprotein (RNP) complexes: RNase P and RNase MRP. These complexes play critical roles in RNA processing, particularly in the maturation of precursor transfer RNA (tRNA) and ribosomal RNA (rRNA). RNase P is responsible for cleaving the 5′ leader sequence of precursor tRNA molecules, while RNase MRP participates in rRNA processing and mitochondrial DNA replication. POP7 functions as a structural and catalytic cofactor within these complexes, stabilizing their architecture and enhancing enzymatic activity through interactions with RNA subunits and other protein partners.
Structurally, POP7 belongs to the oligonucleotide/oligosaccharide-binding (OB)-fold protein family, characterized by a β-barrel motif that facilitates nucleic acid binding. Its recombinant form is engineered for research and therapeutic applications, typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems to ensure proper folding and post-translational modifications. Recombinant POP7 production enables controlled studies of RNase P/MRP mechanisms, which are implicated in diseases like cancer, neurodegenerative disorders, and mitochondrial dysfunction.
The development of recombinant POP7 addresses challenges in isolating native proteins from cellular sources, offering higher purity, scalability, and reduced batch variability. It has become a vital tool for structural studies (e.g., X-ray crystallography, cryo-EM), enzymatic assays, and drug discovery targeting RNA-processing pathways. Recent studies also explore its potential as a biomarker for certain cancers, where dysregulated RNA processing correlates with tumor progression. Despite progress, questions remain about POP7’s dynamic roles in tissue-specific RNP variants and its interactions with noncoding RNAs, driving ongoing research into its molecular functions.
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