| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RNASEH1 |
| Uniprot No | O60930 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-286aa |
| 氨基酸序列 | MSWLLFLAHRVALAALPCRRGSRGFGMFYAVRRGRKTGVFLTWNECRAQV DRFPAARFKKFATEDEAWAFVRKSASPEVSEGHENQHGQESEAKASKRLR EPLDGDGHESAEPYAKHMKPSVEPAPPVSRDTFSYMGDFVVVYTDGCCSS NGRRRPRAGIGVYWGPGHPLNVGIRLPGRQTNQRAEIHAACKAIEQAKTQ NINKLVLYTDSMFTINGITNWVQGWKKNGWKTSAGKEVINKEDFVALERL TQGMDIQWMHVPGHSGFIGNEEADRLAREGAKQSED |
| 预测分子量 | 59 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RNASEH1重组蛋白的3篇代表性文献及其摘要概括：
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1. **"Structure of Human RNase H1 Complexed with an RNA/DNA Hybrid"**
*作者：Nowotny M. et al. (2007)*
**摘要**：通过X射线晶体学解析了人源重组RNASEH1蛋白与RNA/DNA杂交链结合的复合物结构，揭示了其底物识别机制及催化活性关键氨基酸残基的作用，为设计靶向RNASEH1的抑制剂提供了结构基础。
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2. **"RNase H1-Deficient Mitochondria Cause Impaired DNA Replication"**
*作者：Cerritelli S.M. et al. (2009)*
**摘要**：研究利用重组RNASEH1蛋白验证其在线粒体DNA复制中的功能，发现RNASEH1缺失会导致DNA复制停滞和异常结构积累，强调了其在维持基因组稳定性中的必要性。
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3. **"Efficient CRISPR/Cas9-Mediated Gene Editing by Reducing Mismatched RNA/DNA Hybrids"**
*作者：Huang L. et al. (2020)*
**摘要**：通过重组RNASEH1蛋白处理CRISPR编辑后的细胞，证明其可降解Cas9蛋白作用后残留的RNA/DNA杂交体，显著提升基因编辑效率并减少脱靶效应，为基因治疗技术优化提供了新策略。
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这些研究分别从结构解析、功能机制和生物技术应用角度探讨了重组RNASEH1蛋白的特性，涵盖基础科学到实际应用的多个层面。如需扩展，可补充疾病模型(如癌症或神经退行性疾病)相关的功能研究文献。
RNASEH1 (Ribonuclease H1) is a conserved endonuclease that specifically degrades the RNA strand in RNA-DNA hybrids, playing a critical role in maintaining genome stability and facilitating essential cellular processes. It is involved in DNA replication, repair, and transcription by resolving R-loops—three-stranded nucleic acid structures formed during transcription—where an RNA molecule remains hybridized to the DNA template strand. Dysregulation of RNASEH1 activity has been linked to genomic instability, neurodegenerative disorders, and cancer, underscoring its biological importance.
The recombinant RNASEH1 protein is engineered for high purity and activity, typically produced in *E. coli* or eukaryotic expression systems. Its structure includes a catalytic domain that binds hybrid substrates via a conserved magnesium-dependent mechanism, ensuring precise cleavage of RNA in duplexes with DNA. Recombinant variants often incorporate affinity tags (e.g., His-tag) for simplified purification and experimental tracking.
In research, recombinant RNASEH1 is widely used to study R-loop dynamics, DNA replication mechanisms, and genome editing technologies. For instance, it enhances the efficiency of CRISPR-Cas9 systems by removing residual RNA-DNA hybrids, improving target specificity. It also serves as a tool to validate RNA interference (RNAi) experiments by distinguishing between RNA-dependent and DNA-dependent effects. Additionally, RNASEH1 is explored therapeutically to mitigate toxic R-loops in diseases like amyotrophic lateral sclerosis (ALS) and cancer, where aberrant hybrid accumulation drives pathology. Its recombinant form offers potential for developing treatments that modulate RNA-DNA hybrid levels, particularly in combination with antisense oligonucleotides or chemotherapeutic agents. Overall, recombinant RNASEH1 is a versatile tool bridging fundamental research and therapeutic innovation.
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