| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TSN |
| Uniprot No | Q15631 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-228aa |
| 氨基酸序列 | MSVSEIFVELQGFLAAEQDIREEIRKVVQSLEQTAREILTLLQGVHQGAG FQDIPKRCLKAREHFGTVKTHLTSLKTKFPAEQYYRFHEHWRFVLQRLVF LAAFVVYLETETLVTREAVTEILGIEPDREKGFHLDVEDYLSGVLILASE LSRLSVNSVTAGDYSRPLHISTFINELDSGFRLLNLKNDSLRKRYDGLKY DVKKVEEVVYDLSIRGFNKETAAACVEK |
| 预测分子量 | 26 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TSN(Tudor Staphylococcal Nuclease)重组蛋白研究的模拟参考文献示例(仅供参考，实际文献请通过学术数据库查询)：
---
1. **标题**：*Recombinant TSN Protein Expression in E. coli and Its Enzymatic Activity Analysis*
**作者**：Zhang L., Wang Y., et al.
**摘要**：本研究成功在大肠杆菌中表达并纯化了重组TSN蛋白，通过优化密码子使用和诱导条件提高了可溶性蛋白产量。酶活性实验表明，重组TSN具有核酸内切酶活性，并在体外RNA降解实验中表现出底物特异性。
2. **标题**：*Structural Insights into TSN’s Role in RNA Binding via Cryo-EM*
**作者**：Smith J.R., Tanaka K., et al.
**摘要**：利用冷冻电镜技术解析了重组人源TSN蛋白的三维结构，揭示了其Tudor结构域与RNA结合的关键位点，为理解TSN在基因沉默和RNA代谢中的功能提供了结构基础。
3. **标题**：*TSN Knockdown and Recombinant Rescue in Cancer Cell Apoptosis*
**作者**：Chen H., Gupta M., et al.
**摘要**：通过RNA干扰技术敲低TSN表达导致癌细胞凋亡增加，而外源性添加重组TSN蛋白可部分恢复细胞存活，表明TSN在肿瘤细胞抗凋亡通路中起重要作用。
4. **标题**：*TSN Interaction with PIWI Proteins: A Recombinant Protein-Based Study*
**作者**：Kim S., Patel R., et al.
**摘要**：采用重组TSN蛋白与PIWI家族蛋白进行体外结合实验，证实TSN通过其SNase结构域直接参与piRNA通路调控，为生殖细胞发育机制提供了新证据。
---
**注意**：以上为模拟生成的参考文献，实际研究中请通过PubMed、Web of Science等平台检索真实文献(关键词：*TSN protein, recombinant TSN, Tudor SNase*)。
TSN recombinant protein, often derived from thioredoxin (Trx) or translin-associated protein (TSN) family members, represents a class of engineered proteins widely utilized in biotechnology and biomedical research. Thioredoxin, a naturally occurring redox-active protein found in organisms ranging from bacteria to humans, plays critical roles in regulating cellular redox homeostasis, protein folding, and antioxidant defense. Its recombinant form is frequently employed as a solubility-enhancing fusion partner due to its stable structure and ability to improve the yield and stability of target proteins during heterologous expression in systems like *E. coli* or mammalian cells.
Translin-associated proteins, on the other hand, are implicated in RNA metabolism, DNA repair, and gametogenesis. Recombinant TSN proteins in this context are studied for their roles in genetic regulation and potential therapeutic applications, such as cancer research or fertility studies. The development of recombinant TSN proteins leverages advanced genetic engineering techniques, including codon optimization, affinity tagging (e.g., His-tag), and host-specific expression optimization, to ensure high purity and functional activity.
These proteins are pivotal in structural biology for crystallization studies, as diagnostic tools in immunoassays, and in drug discovery pipelines. Challenges persist in minimizing aggregation and post-translational modification mismatches across expression platforms. Recent advances in synthetic biology and AI-driven protein design have accelerated the customization of TSN recombinant proteins, expanding their utility in personalized medicine, biocatalysis, and nanotechnology. Their versatility underscores their importance in bridging basic research and industrial applications.
×
