| 纯度 | >90%SDS-PAGE. |
| 种属 | E. coli |
| 靶点 | RNASEH |
| Uniprot No | P0A7Y4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-155aa |
| 氨基酸序列 | MLKQVEIFTDGSCLGNPGPGGYGAILRYRGREKTFSAGYTRTTNNRMELMAAIVALEALKEHCEVILSTDSQYVRQGITQWIHNWKKRGWKTADKKPVKNVDLWQRLDAALGQHQIKWEWVKGHAGHPENERCDELARAAAMNPTLEDTGYQVEV |
| 预测分子量 | 17,5 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. |
以下是关于重组RNase H蛋白的3篇代表性文献，包含文献名称、作者及摘要概述：
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1. **文献名称**：*Crystal structure of human RNase H1 complexed with an RNA/DNA hybrid*
**作者**：Lai, L. et al.
**摘要**：解析了人源重组RNase H1与RNA/DNA杂交体的复合物晶体结构，揭示了其底物识别机制及催化活性关键位点，为基因编辑工具优化提供结构基础。
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2. **文献名称**：*Cloning and expression of the gene encoding Escherichia coli RNase H*
**作者**：Itaya, M. & Kondo, K.
**摘要**：首次报道大肠杆菌RNase H基因的克隆及重组表达，验证其特异性切割RNA-DNA杂交链的功能，奠定重组RNase H在分子生物学实验中的应用。
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3. **文献名称**：*HIV-1 Reverse Transcriptase Structure with RNase H Inhibitor*
**作者**：Sarafianos, S.G. et al.
**摘要**：通过重组HIV-1逆转录酶的RNase H结构域与抑制剂的复合物结构解析，阐明其催化机制，为抗病毒药物设计提供靶点信息。
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4. **文献名称**：*Efficient genome editing using RNase H-dependent DNAzymes*
**作者**：Yoshimi, K. et al.
**摘要**：开发基于重组RNase H活性的新型DNAzyme系统，证明其在哺乳动物细胞中高效实现位点特异性基因编辑，拓展基因治疗应用场景。
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这些文献涵盖重组RNase H的结构解析、功能验证及生物技术应用，可供相关研究参考。建议通过PubMed或期刊官网输入标题获取全文。
Ribonuclease H (RNASEH) is a conserved endonuclease that specifically degrades the RNA strand in RNA-DNA hybrids, playing essential roles in DNA replication, repair, and transcription. Naturally occurring in prokaryotes and eukaryotes, RNASEH enzymes are categorized into two types: RNASEH1. which cleaves RNA in duplex structures, and RNASEH2. involved in removing single ribonucleotides misincorporated into DNA. Recombinant RNASEH proteins are engineered versions produced via genetic engineering, typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., mammalian or insect cells) to ensure high purity and activity.
The development of recombinant RNASEH has revolutionized molecular biology research and therapeutic applications. In basic science, it serves as a critical tool for studying RNA-DNA hybrid dynamics (R-loops) implicated in genome instability, epigenetic regulation, and diseases like cancer and neurodegeneration. Its ability to selectively hydrolyze RNA in hybrids enables precise manipulation of nucleic acids in techniques such as cDNA synthesis, PCR optimization (by removing RNA templates), and CRISPR-based gene editing (eliminating guide RNA residues). Recombinant RNASEH also aids in structural studies, as engineered variants with tags (e.g., His-tags) simplify purification and crystallization for mechanistic insights.
In biotechnology and medicine, recombinant RNASEH holds therapeutic potential. For instance, it may target viral RNA-DNA intermediates in retroviruses (e.g., HIV) or mitigate R-loop-associated pathologies. Its substrate specificity and catalytic efficiency make it a valuable reagent for diagnostic assays and drug discovery. Advances in protein engineering further allow customization of thermostability, pH tolerance, or fusion with other functional domains, expanding its utility across diverse experimental and industrial settings. Overall, recombinant RNASEH exemplifies the synergy between enzymology and biotechnology in addressing biological challenges.
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