| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TATDN1 |
| Uniprot No | Q6P1N9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-297aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMSRFKFI DIGINLTDPM FRGIYRGVQK HQDDLQDVIG RAVEIGVKKF MITGGNLQDS KDALHLAQTN GMFFSTVGCH PTRCGEFEKN NPDLYLKELL NLAENNKGKV VAIGECGLDF DRLQFCPKDT QLKYFEKQFE LSEQTKLPMF LHCRNSHAEF LDIMKRNRDR CVGGVVHSFD GTKEAAAALI DLDLYIGFNG CSLKTEANLE VLKSIPSEKL MIETDAPWCG VKSTHAGSKY IRTAFPTKKK WESGHCLKDR NEPCHIIQIL EIMSAVRDED PLELANTLYN NTIKVFFPGI |
| 预测分子量 | 36 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TATDN1重组蛋白的模拟参考文献示例(仅供参考，实际文献需通过学术数据库查询)：
1. **文献名称**: *"Functional characterization of recombinant TATDN1 as a Mg²⁺-dependent DNase involved in DNA repair"*
**作者**: Li, X. et al.
**摘要**: 研究报道了TATDN1重组蛋白在大肠杆菌中的高效表达与纯化，证实其具有Mg²⁺依赖的DNA水解酶活性，并可能通过切割单链DNA参与DNA损伤修复通路。
2. **文献名称**: *"Structural insights into the catalytic mechanism of TATDN1 through crystallographic analysis"*
**作者**: Wang, Y. et al.
**摘要**: 通过X射线晶体学解析了TATDN1重组蛋白的三维结构，揭示了其保守的核酸酶催化结构域及底物结合位点，为功能机制研究提供结构基础。
3. **文献名称**: *"TATDN1 knockdown enhances chemosensitivity by promoting apoptosis in colorectal cancer cells"*
**作者**: Zhang, R. et al.
**摘要**: 利用重组TATDN1蛋白进行体外功能实验，发现其通过调控线粒体途径抑制细胞凋亡，提示其在肿瘤耐药性中的潜在作用。
4. **文献名称**: *"Expression optimization and enzymatic activity screening of TATDN1 recombinant protein in eukaryotic systems"*
**作者**: Chen, L. et al.
**摘要**: 比较了昆虫细胞和哺乳动物系统中TATDN1重组蛋白的表达效率，发现其在不同系统中均具有核酸内切酶活性，但底物偏好性存在差异。
**说明**：以上内容为基于TATDN1蛋白已知功能的模拟概括，实际文献需通过PubMed、Web of Science或Google Scholar等平台以“TATDN1 recombinant protein”或“TATDN1 DNase”为关键词检索获取。
**Background of TATDN1 Recombinant Protein**
TATDN1 (TatD DNase domain-containing protein 1) is a conserved eukaryotic protein characterized by its TatD-like DNase domain, which shares homology with bacterial TatD nucleases. Initially identified in *Mycobacterium tuberculosis*, TatD proteins are metal-dependent hydrolytic enzymes implicated in DNA repair, apoptosis, and genome maintenance. In humans, TATDN1 has emerged as a multifunctional protein with roles in nucleic acid metabolism, particularly in resolving RNA-DNA hybrids (R-loops) and processing DNA damage.
Structurally, TATDN1 contains a central catalytic domain that facilitates its endonuclease activity, enabling cleavage of both DNA and RNA substrates. Studies suggest its involvement in maintaining genomic stability by mitigating replication stress and preventing aberrant R-loop accumulation, which can lead to transcription-replication conflicts and chromosomal breaks. Dysregulation of TATDN1 has been linked to cancer progression, where its overexpression correlates with chemotherapy resistance, possibly due to enhanced DNA repair capacity in tumor cells.
Recombinant TATDN1 protein is typically produced using bacterial expression systems (e.g., *E. coli*), enabling large-scale purification for functional studies. Its recombinant form is utilized to dissect enzymatic mechanisms, substrate specificity, and interactions with DNA repair machinery components, such as PARP1. Furthermore, TATDN1’s role in RNA processing, including ribosomal RNA maturation, highlights its versatility in cellular homeostasis.
Research on TATDN1 is expanding, with ongoing investigations into its potential as a therapeutic target in cancers or diseases marked by genomic instability. Its recombinant protein serves as a critical tool for structural analysis (e.g., crystallography) and high-throughput screening for inhibitors or modulators. Despite progress, questions remain regarding its regulatory networks and tissue-specific functions, underscoring the need for further exploration of this enigmatic protein.
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