| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RNASEP |
| Uniprot No | P78346 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-268aa |
| 氨基酸序列 | AVFADLDLR AGSDLKALRG LVETAAHLGY SVVAINHIVD FKEKKQEIEK PVAVSELFTT LPIVQGKSRP IKILTRLTII VSDPSHCNVL RATSSRARLY DVVAVFPKTE KLFHIACTHL DVDLVCITVT EKLPFYFKRP PINVAIDRGL AFELVYSPAI KDSTMRRYTI SSALNLMQIC KGKNVIISSA AERPLEIRGP YDVANLGLLF GLSESDAKAA VSTNCRAALL HGETRKTAFG IISTVKKPRP SEGDEDCLPA SKKAKCEG |
| 预测分子量 | 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RNase P重组蛋白的3篇代表性文献示例(注：文献为假设性概括，实际需根据具体研究补充或核实)：
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1. **文献名称**：*"Recombinant Expression and Functional Analysis of RNase P Protein Subunit in Bacterial Systems"*
**作者**：A. Smith et al.
**摘要**：研究报道了在大肠杆菌中重组表达细菌RNase P的蛋白质亚基(C5蛋白)，通过亲和层析纯化，并验证其在体外与RNA组分协同催化tRNA前体加工的活性，揭示了蛋白质亚基对酶稳定性的关键作用。
2. **文献名称**：*"Structural Insights into Human RNase P by Cryo-EM Using Recombinant Subunits"*
**作者**：B. Chen & L. Wang
**摘要**：通过重组表达人源RNase P的多个蛋白质亚基(如Rpp20、Rpp25)，结合冷冻电镜技术解析其三维结构，阐明了蛋白质与RNA核心的相互作用机制及其在疾病相关突变中的功能缺陷。
3. **文献名称**：*"Engineering Thermostable RNase P Variants via Directed Evolution of Recombinant Protein Components"*
**作者**：K. Tanaka et al.
**摘要**：利用定向进化技术改造古菌RNase P的蛋白质亚基，获得热稳定性增强的重组蛋白，并证明其在高温下仍能有效催化tRNA成熟，为工业酶应用提供潜在工具。
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**备注**：以上文献为示例，实际研究中建议通过PubMed或Web of Science检索关键词(如“recombinant RNase P protein”“RNASEP expression”)获取真实文献。
Ribonuclease P (RNase P) is a conserved endoribonuclease primarily involved in processing precursor transfer RNA (tRNA) molecules by cleaving their 5' leader sequences. Initially characterized as a ribonucleoprotein complex, RNase P consists of a catalytic RNA subunit and a variable number of protein cofactors depending on the organism. In bacteria, the RNA component alone can catalyze tRNA maturation in vitro, while eukaryotic RNase P requires protein subunits for stability and activity. Recombinant RNase P proteins are engineered versions produced through genetic engineering, often expressed in heterologous systems like *E. coli* or yeast for functional studies or therapeutic applications.
The development of recombinant RNase P proteins has advanced research into RNA processing mechanisms and enzyme evolution. These proteins are crucial for reconstituting functional RNase P complexes in vitro, enabling structural and mechanistic studies. For example, human RNase P subunits expressed recombinantly have helped elucidate their roles in substrate recognition and catalysis. Additionally, recombinant RNase P has therapeutic potential, particularly in targeting RNA viruses or cleaving disease-associated RNAs. Engineered variants, such as RNase P coupled with guide RNAs, have been explored for gene-silencing technologies.
Challenges in producing recombinant RNase P include maintaining proper folding and post-translational modifications, especially for eukaryotic subunits. Recent advances in protein engineering and expression systems have improved yields and activity. Recombinant RNase P proteins also serve as tools in synthetic biology, enabling customized RNA processing in engineered organisms. Their study continues to bridge gaps in understanding RNA-protein interactions and the development of RNA-targeted therapies.
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