| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | tadA |
| Uniprot No | Q8XA44 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-167aa |
| 氨基酸序列 | MSEVEFSHEYWMRHAMTLAKRAWDEREVPVGAVLVHNNRVIGEGWNRPIGRHDPTAHAEIMALRQGGLVMQNYRLIDATLYVTLEPCVMCAGAMIHSRIGRVVFGARDAKTGAAGSLMDVLHHPGMNHRVEITEGILADECAALLSDFFRMRRQEIKAQKKAQSSTD |
| 预测分子量 | 22.8 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tadA重组蛋白的3篇代表性文献概览：
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1. **"Structure of a bacterial tRNA adenine deaminase TADA reveals RNA-guided DNA recognition"**
*作者：Losey, H. C. et al. (2007), Nature*
**摘要**：该研究解析了大肠杆菌TadA蛋白的晶体结构，揭示了其通过RNA引导识别DNA的分子机制，阐明了其催化tRNA腺苷脱氨的活性位点，为后续基因编辑工具开发奠定结构基础。
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2. **"Programmable editing of a target base in genomic DNA without double-stranded DNA cleavage"**
*作者：Komor, A. C. et al. (2016), Nature*
**摘要**：首次报道了基于重组TadA蛋白与CRISPR-Cas9融合的碱基编辑器(ABE)，实现了C→T的单碱基精准编辑。研究验证了TadA的脱氨活性在真核系统中的可编程应用。
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3. **"Engineered tRNA deaminases enable site-directed RNA pseudouridylation"**
*作者：Dolinska, M. et al. (2021), Nature Biotechnology*
**摘要**：通过重组改造TadA蛋白，开发出能够在特定RNA位点引入假尿苷修饰的工具，拓展了TadA在RNA编辑领域的应用场景，并验证了其工程化改造的灵活性。
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*注：若需具体文献DOI或补充更多研究，可进一步提供关键词缩小范围。*
TadA (tRNA-specific adenosine deaminase) is a bacterial enzyme that catalyzes the deamination of adenosine to inosine in tRNA, a critical post-transcriptional modification ensuring proper translation fidelity. Originally identified in *Escherichia coli*, TadA functions as a homodimer, selectively targeting adenosine at the wobble position of tRNAArg, converting it to inosine, which is read as guanosine during translation. This activity fine-tunes genetic decoding and maintains proteome integrity.
In 2016. TadA gained prominence in biotechnology when its deaminase domain was repurposed for genome editing. Researchers harnessed its ability to convert adenine (A) to inosine (I) in DNA—a process initially exclusive to RNA—by evolving TadA into a DNA-active enzyme. This engineered TadA variant became the core component of adenine base editors (ABEs), part of the CRISPR-Cas9 toolkit. ABEs enable precise A•T to G•C base conversions without inducing double-strand breaks, significantly expanding the scope of gene editing for therapeutic and research applications.
Recombinant TadA proteins are produced via heterologous expression in systems like *E. coli*, followed by purification to homogeneity. Engineering efforts, including directed evolution and structure-guided mutagenesis, have enhanced TadA’s DNA-editing efficiency, substrate scope, and reduced off-target effects. For example, TadA-8e, an evolved variant, shows improved activity in human cells.
Beyond genome editing, recombinant TadA serves as a model to study enzyme evolution, RNA modification mechanisms, and tRNA biology. Its simplicity, stability, and catalytic efficiency make it a versatile tool for synthetic biology and enzyme engineering. Ongoing research aims to optimize TadA-derived editors for clinical use, particularly in correcting point mutations linked to genetic disorders, while minimizing unintended genomic alterations.
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