| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DTD2 |
| Uniprot No | Q96FN9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-168aa |
| 氨基酸序列 | MAEGSRIPQARALLQQCLHARLQIRPADGDVAAQWVEVQRGLVIYVCFFKGADKELLPKMVNTLLNVKLSETENGKHVSILDLPGNILIIPQATLGGRLKGRNMQYHSNSGKEEGFELYSQFVTLCEKEVAANSKCAEARVVVEHGTYGNRQVLKLDTNGPFTHLIEF |
| 预测分子量 | 34.7kDa |
| 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DTD2重组蛋白的示例参考文献(内容为虚构示例，实际文献需通过学术数据库检索验证)：
---
1. **文献名称**: "Structural and functional analysis of DTD2 in tRNA proofreading"
**作者**: Suzuki T., et al.
**摘要**: 本研究通过重组表达纯化了人源DTD2蛋白，解析了其晶体结构，揭示了其特异性识别D-酪氨酸-tRNA的分子机制，并验证了其在翻译质量控制中的去酰基酶活性。
---
2. **文献名称**: "Recombinant DTD2 expression in E. coli and enzymatic characterization"
**作者**: Kobayashi H., et al.
**摘要**: 报道了利用大肠杆菌系统高效表达重组DTD2蛋白的优化方法，通过体外酶活实验证实其对误载的D-氨基酸-tRNA具有高效水解活性，为药物靶点研究提供基础。
---
3. **文献名称**: "DTD2-mediated chiral proofreading in mitochondrial translation"
**作者**: Nureki R., et al.
**摘要**: 通过重组DTD2蛋白的功能研究，阐明了该酶在线粒体翻译过程中防止D-氨基酸错误掺入的分子机制，并探讨了其缺陷与神经退行性疾病的相关性。
---
注：以上为模拟参考文献，实际研究中请通过PubMed、Web of Science等平台检索真实文献。
**Background of DTD2 Recombinant Protein**
DTD2 (D-aminoacyl-tRNA deacylase 2) is an evolutionarily conserved enzyme critical for maintaining translational fidelity in living organisms. It belongs to the DTD family, which specifically hydrolyzes D-amino acids mistakenly attached to tRNA molecules during protein synthesis. This activity prevents the misincorporation of D-amino acids into proteins, ensuring the stereochemical purity of the L-amino acid-based genetic code.
The gene encoding DTD2 is found across diverse species, including bacteria, archaea, and eukaryotes, highlighting its fundamental role in cellular function. Structurally, DTD2 exhibits a compact α/β-hydrolase fold with a conserved catalytic triad (e.g., Ser-His-Asp/Glu) that enables its deacylase activity. Unlike its homolog DTD1. which shows chiral specificity, DTD2 displays broader substrate selectivity, acting on both D-aminoacyl-tRNA and certain non-canonical substrates.
Recombinant DTD2 protein is produced via heterologous expression systems, such as *E. coli* or yeast, enabling large-scale purification for biochemical and structural studies. Its recombinant form retains enzymatic activity, making it valuable for *in vitro* studies on translation quality control mechanisms, enzyme kinetics, and substrate interactions. Additionally, DTD2 has garnered interest in biotechnological applications, including synthetic biology and enzyme engineering, due to its role in minimizing translational errors.
Recent research also explores DTD2's potential in biomedical contexts, such as targeting antibiotic-resistant bacteria (by disrupting their translation fidelity) or understanding neurodegenerative diseases linked to protein misfolding. Overall, DTD2 recombinant protein serves as a vital tool for deciphering the molecular basis of translational accuracy and developing novel therapeutic strategies.
×
