| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TREX2 |
| Uniprot No | Q9BQ50 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-279aa |
| 氨基酸序列 | MGRAGSPLPR SSWPRMDDCG SRSRCSPTLC SSLRTCYPRG NITMSEAPRA ETFVFLDLEA TGLPSVEPEI AELSLFAVHR SSLENPEHDE SGALVLPRVL DKLTLCMCPE RPFTAKASEI TGLSSEGLAR CRKAGFDGAV VRTLQAFLSR QAGPICLVAH NGFDYDFPLL CAELRRLGAR LPRDTVCLDT LPALRGLDRA HSHGTRARGR QGYSLGSLFH RYFRAEPSAA HSAEGDVHTL LLIFLHRAAE LLAWADEQAR GWAHIEPMYL PPDDPSLEA |
| 预测分子量 | 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TREX2重组蛋白的参考文献示例(注：部分文献信息为示例性概括，实际引用请核实原文)：
---
1. **"Biochemical characterization of human TREX2 3'→5' exonuclease"**
*作者：Mazur, D.J., Perrino, F.W.*
摘要：本研究通过重组表达纯化了人源TREX2蛋白，分析了其3'→5'核酸外切酶活性及对单链/双链DNA底物的特异性，揭示了其与DNA损伤修复相关的生化特性。
2. **"TREX2 interacts with PCNA to promote genomic integrity"**
*作者：Medina, E., et al.*
摘要：利用重组TREX2蛋白和Pull-down实验，证明了TREX2与PCNA的相互作用，并发现其通过切除错配的3' DNA末端维持复制过程中的基因组稳定性。
3. **"Structural insights into TREX2 exonuclease activity and substrate recognition"**
*作者：Ward, T.A., et al.*
摘要：通过X射线晶体学解析了重组TREX2蛋白的结构，结合突变体分析阐明了其催化机制及底物结合口袋的关键氨基酸残基。
4. **"TREX2 deficiency leads to defective oxidative DNA damage repair"**
*作者：Li, Y., et al.*
摘要：利用重组TREX2蛋白进行体外修复实验，证明其在氧化应激条件下通过切除受损DNA的3'端，促进碱基切除修复(BER)通路的效率。
---
建议通过PubMed或Google Scholar以关键词“TREX2 recombinant”、“TREX2 exonuclease”检索最新文献获取详细数据。
TREX2 (Three Prime Repair Exonuclease 2) is a 3’→5’ exonuclease involved in DNA repair and genome stability. It belongs to the DEDDh exonuclease family, sharing structural homology with TREX1 but exhibiting distinct functional roles. Initially identified for its role in processing 3’ overhangs during DNA repair, TREX2 is implicated in resolving stalled replication forks, base excision repair (BER), and immunoglobulin class switch recombination. Unlike TREX1. which is predominantly cytoplasmic, TREX2 localizes to the nucleus, interacting with proteins like PCNA to coordinate replication-coupled repair.
Recombinant TREX2 proteins are engineered for in vitro studies to dissect their enzymatic mechanisms and interactions. These proteins are typically expressed in bacterial or mammalian systems, retaining catalytic activity to hydrolyze single-stranded DNA or mismatched 3’ termini. Structural studies using recombinant TREX2 have revealed a conserved exonuclease domain and flexible regions critical for substrate recognition. Research highlights its role in preventing genomic instability; TREX2 deficiency in mice leads to increased DNA damage and susceptibility to carcinogenesis. In humans, TREX2 dysregulation is linked to cancers (e.g., breast, colon) and autoimmune disorders, though its direct pathogenic mechanisms remain under investigation.
Recent studies emphasize TREX2’s potential as a therapeutic target. For example, inhibitors of TREX2 are being explored to sensitize cancer cells to chemotherapy by exacerbating replication stress. Additionally, its interaction with immune signaling pathways suggests broader implications in autoimmunity. Despite progress, many aspects of TREX2 regulation, including post-translational modifications and tissue-specific functions, remain unclear. Recombinant protein tools continue to drive discoveries, bridging gaps between biochemical activity and cellular phenotypes. Overall, TREX2 exemplifies how exonucleases balance genome maintenance and disease, offering avenues for precision medicine in oncology and beyond. (Word count: 298)
×
