| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | rnhA |
| Uniprot No | Q9HSF6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-199aa |
| 氨基酸序列 | MPVVECDIQTARAALADAGASFSDGNSEHELWHADLGDAHAVAYADKLVVQGGSPTDITAVVQPDRGGRVHAYFDGASRGNPGPAAVGWVLVSGDGGIVAEGGDTIGRATNNQAEYDALIAALEAAADFGFDDIELRGDSQLVEKQLTGAWDTNDPDLRRKRVRARELLTGFDDWSITHVPRATNERADALANEALDDA |
| 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3篇关于rnhA重组蛋白的参考文献概览：
1. **"Cloning, expression, and characterization of recombinant RNase H from Escherichia coli"**
- 作者：Kanaya, S., et al.
- 摘要：该研究报道了在大肠杆菌中克隆并高效表达rnhA基因，纯化获得重组RNase H蛋白，并验证其水解RNA-DNA杂交链的活性，为后续酶学性质研究奠定基础。
2. **"Crystal structure of RNase H from Bacillus subtilis: Insights into substrate recognition"**
- 作者：Haruki, M., et al.
- 摘要：通过X射线晶体学解析枯草芽孢杆菌重组RNase H的三维结构，揭示其与RNA-DNA复合物结合的关键氨基酸残基，阐明底物特异性机制。
3. **"Functional analysis of thermostable RNase H variants for PCR applications"**
- 作者：Hogrefe, H.H., et al.
- 摘要：研究利用定点突变技术构建耐高温重组RNase H突变体，证明其在PCR中有效消除引物二聚体，提升扩增效率，拓展了rnhA工程化改造的应用潜力。
注：以上文献为示例性概括，实际引用时需核实原文准确性。若需具体文献，建议通过PubMed或Web of Science以“rnhA recombinant protein”等关键词检索。
**Background of RnhA Recombinant Protein**
RNase H (Ribonuclease H) enzymes are endonucleases that specifically hydrolyze the RNA strand in RNA-DNA hybrids, playing critical roles in DNA replication, repair, and transcription. Among bacterial RNase H enzymes, RnhA (encoded by the *rnhA* gene) is a well-studied member, primarily found in *Escherichia coli*. Unlike RNase HII, which cleaves at single ribonucleotides in DNA, RnhA functions as a class I RNase H, requiring a divalent metal ion (Mg²⁺ or Mn²⁺) to degrade longer RNA segments within hybrid duplexes.
The recombinant RnhA protein is produced via heterologous expression, where the *rnhA* gene is cloned into an expression vector (e.g., plasmid) and introduced into a host system (commonly *E. coli*). This allows large-scale production of the enzyme, which is then purified using affinity chromatography or other biochemical methods. Recombinant RnhA retains the enzymatic activity of its native counterpart, making it a valuable tool in molecular biology.
Applications of recombinant RnhA include studying RNA-DNA hybrid dynamics (e.g., R-loops) in genomic stability, optimizing reverse transcription processes by removing RNA templates, and aiding in structural studies of RNase H mechanisms. It also serves as a model for understanding bacterial DNA repair pathways and has potential biotechnological uses, such as in antisense oligonucleotide therapies or CRISPR-based technologies where RNA-DNA hybrid resolution is required.
Research on RnhA has expanded insights into cellular responses to replication stress and transcriptional errors, highlighting its significance in both basic science and applied research. Its recombinant form ensures accessibility for high-throughput studies, bridging gaps between biochemical characterization and functional genomics.
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