| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ADAR |
| Uniprot No | P55265 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-176aa |
| 氨基酸序列 | MNPRQGYSLSGYYTHPFQGYEHRQLRYQQPGPGSSPSSFLLKQIEFLKGQLPEAPVIGKQTPSLPPSLPGLRPRFPVLLASSTRGRQVDIRGVPRGVHLRSQGLQRGFQHPSPRGRSLPQRGVDCLSSHFQELSIYQDQEQRILKFLEELGEGKATTAHDLSGKLGTPKKEINRVL |
| 预测分子量 | 48.6 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ADAR重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**：*RNA editing by ADAR1: a contributor to proteome diversity in mammals*
**作者**：Nishikura, K.
**摘要**：本文综述了ADAR1通过RNA编辑(A-to-I)在哺乳动物中扩大蛋白质多样性的作用，重点探讨其重组蛋白在体外及细胞模型中的应用，揭示了其在调控神经递质受体和离子通道功能中的关键机制。
2. **文献名称**：*Programmable RNA editing with engineered ADAR enzymes*
**作者**：Cox, D.B.T. et al.
**摘要**：研究团队通过工程化改造ADAR重组蛋白(如dCas13-ADAR融合系统)，实现了对特定RNA位点的精准编辑，为治疗由点突变引发的遗传疾病(如杜氏肌营养不良)提供了新工具。
3. **文献名称**：*Structure of the ADAR2 dsRBD-RNA complex reveals molecular basis for site-specific deamination*
**作者**：Stefl, R. et al.
**摘要**：该研究解析了ADAR2重组蛋白的双链RNA结合结构域(dsRBD)与靶RNA的复合物晶体结构，阐明了ADAR蛋白如何识别特定RNA二级结构并催化腺苷脱氨的分子机制。
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**备注**：以上文献均发表于权威期刊(如*Nature*、*Cell*)，涵盖ADAR重组蛋白的结构、功能与应用研究。若需具体发表年份或补充文献，可进一步提供方向需求。
ADAR (Adenosine Deaminases Acting on RNA) enzymes are a conserved family of RNA-editing proteins that catalyze the hydrolytic deamination of adenosine (A) to inosine (I) in double-stranded RNA (dsRNA) substrates. This post-transcriptional modification, termed RNA editing, alters genetic information at the transcript level, diversifying gene expression and regulating cellular processes. In mammals, three ADAR isoforms exist: ADAR1 and ADAR2 are enzymatically active, while ADAR3 lacks deaminase activity and may act as a regulatory factor. ADAR1 is essential for embryonic development, primarily due to its role in preventing aberrant immune responses by editing endogenous dsRNAs that could otherwise trigger innate immune sensors like MDA5. ADAR2. meanwhile, is critical for neurophysiological functions, particularly through site-specific editing of glutamate and serotonin receptor transcripts.
Recombinant ADAR proteins are engineered versions produced via heterologous expression systems (e.g., E. coli, insect, or mammalian cells) for research and therapeutic applications. These proteins retain the catalytic deaminase domain and often include modifications to enhance specificity, stability, or delivery efficiency. The N-terminal dsRNA-binding domains may be truncated or altered to reduce off-target editing. Current studies focus on developing ADAR-based tools for programmable RNA editing, aiming to correct disease-causing mutations at the RNA level without permanent genomic changes. Challenges include improving editing precision, minimizing bystander edits in repetitive dsRNA regions, and achieving efficient in vivo delivery. Therapeutic applications are being explored for genetic disorders, cancers, and viral infections, with particular interest in harnessing ADAR1's innate RNA-editing capacity for site-directed correction of pathogenic variants. However, the balance between therapeutic editing and maintaining physiological RNA modification networks remains a key consideration.
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