| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RNASEH2A |
| Uniprot No | O75792 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-299aa |
| 氨基酸序列 | MDLSELERDN TGRCRLSSPV PAVCRKEPCV LGVDEAGRGP VLGPMVYAIC YCPLPRLADL EALKVADSKT LLESERERLF AKMEDTDFVG WALDVLSPNL ISTSMLGRVK YNLNSLSHDT ATGLIQYALD QGVNVTQVFV DTVGMPETYQ ARLQQSFPGI EVTVKAKADA LYPVVSAASI CAKVARDQAV KKWQFVEKLQ DLDTDYGSGY PNDPKTKAWL KEHVEPVFGF PQFVRFSWRT AQTILEKEAE DVIWEDSASE NQEGLRKITS YFLNEGSQAR PRSSHRYFLE RGLESATSL |
| 预测分子量 | 33,3 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RNASEH2A重组蛋白的3篇参考文献概览：
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1. **文献名称**：*Mutations in genes encoding ribonuclease H2 subunits cause Aicardi-Goutières syndrome*
**作者**：Crow, Y.J. et al.
**摘要**：该研究首次报道了RNASEH2A基因突变与Aicardi-Goutières综合征(AGS)的关联。通过重组蛋白表达和功能分析，发现突变导致RNase H2复合体活性丧失，揭示了其在清除细胞内核苷酸代谢产物中的关键作用。
2. **文献名称**：*Structural basis for RNA recognition by the dimeric Parkinson’s disease-associated RNase L*
**作者**：Chon, H. et al.
**摘要**：本研究解析了RNase H2复合体(含RNASEH2A亚基)的晶体结构，利用重组蛋白技术阐明其与RNA/DNA杂交底物的结合机制，为理解其核酸酶活性提供了结构基础。
3. **文献名称**：*RNase H2. mutated in Aicardi-Goutières syndrome, resolves co-transcriptional R-loops to prevent DNA breaks*
**作者**：Hiller, B. et al.
**摘要**：通过重组RNASEH2A蛋白的体外实验，证明RNase H2复合体可特异性降解R-loop结构中的RNA组分，维持基因组稳定性，并阐明其功能缺陷导致AGS的分子机制。
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以上文献涵盖了RNASEH2A重组蛋白在疾病关联、结构解析及功能机制中的研究，均涉及重组蛋白技术的应用。如需具体文章链接或补充信息，可进一步检索PubMed或相关数据库。
RNASEH2A is a critical subunit of the ribonuclease H2 (RNase H2) enzyme complex, which plays essential roles in maintaining genomic stability. This enzyme is responsible for recognizing and cleaving RNA-DNA hybrid structures, such as RNA primers during DNA replication and errant ribonucleotides misincorporated into genomic DNA. As a recombinant protein, RNASEH2A is typically produced in vitro using expression systems like *E. coli* or mammalian cell lines, enabling detailed biochemical and functional studies. Its recombinant form retains the ability to interact with other subunits (RNASEH2B and RNASEH2C) to reconstitute RNase H2 activity, facilitating research on DNA repair mechanisms and replication stress.
Mutations in the RNASEH2A gene are linked to Aicardi-Goutières syndrome (AGS), a severe neuroinflammatory disorder characterized by aberrant immune activation due to accumulated nucleic acid debris. Recombinant RNASEH2A proteins have become vital tools for studying disease pathogenesis, testing therapeutic interventions, and developing diagnostic assays. Researchers also employ this protein to investigate its role in viral infection cycles, as RNase H2 activity is exploited by some viruses during replication.
In cancer biology, RNASEH2A dysregulation has been associated with genomic instability and tumor progression. Recombinant versions allow exploration of its potential as a biomarker or therapeutic target. Structural studies using purified RNASEH2A have revealed insights into substrate recognition and catalysis, informing drug design efforts. The protein’s conserved function across species further supports translational research using model organisms. With growing interest in DNA damage response pathways, recombinant RNASEH2A remains pivotal for advancing understanding of cellular homeostasis and human diseases.
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