| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TPP2 |
| Uniprot No | P29144 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 44-264aa |
| 氨基酸序列 | DTGVDPGAPGMQVTTDGKPKIVDIIDTTGSGDVNTATEVEPKDGEIVGLSGRVLKIPASWTNPSGKYHIGIKNGYDFYPKALKERIQKERKEKIWDPVHRVALAEACRKQEEFDVANNGSSQANKLIKEELQSQVELLNSFEKKYSDPGPVYDCLVWHDGEVWRACIDSNEDGDLSKSTVLRNYKEAQEYGSFGTAEMLNYSVNIYDDGNLLSIVTSGGAH |
| 预测分子量 | 31.8 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TPP2重组蛋白的模拟参考文献示例(仅供研究参考，非真实文献)：
1. **《Expression and Purification of Recombinant Human TPP2 in Escherichia coli》**
- 作者：Zhang L, et al.
- 摘要：研究通过大肠杆菌表达系统成功表达并纯化具有酶活性的重组人源TPP2蛋白，优化了诱导条件与纯化步骤，为后续功能研究提供基础。
2. **《Structural Characterization of TPP2 Reveals a Novel Protease Mechanism》**
- 作者：Johnson R, et al.
- 摘要：利用X射线晶体学解析了重组TPP2的三维结构，揭示了其底物结合位点和催化机制，为设计靶向抑制剂奠定结构基础。
3. **《TPP2 Knockdown Enhances Chemotherapy Sensitivity in Cancer Cells》**
- 作者：Wang Y, et al.
- 摘要：通过重组TPP2蛋白体外实验及细胞模型，发现TPP2通过调控蛋白酶体活性影响肿瘤细胞耐药性，提示其作为潜在治疗靶点。
4. **《Functional Analysis of Recombinant TPP2 in Immune Regulation》**
- 作者：Müller S, et al.
- 摘要：在哺乳动物细胞(HEK293)中表达重组TPP2.证明其通过降解特定免疫调节肽影响T细胞功能，为自身免疫疾病机制研究提供新方向。
(注：以上为模拟内容，建议通过PubMed、Web of Science等平台搜索真实文献。)
**Background of Recombinant TPP2 Protein**
Tripeptidyl-peptidase II (TPP2), also known as Tripeptidyl-peptidase II, is a large, multifunctional serine protease belonging to the SC clan of peptidases. It plays a critical role in intracellular protein degradation by cleaving tripeptides from the N-terminus of polypeptides, functioning both as an exopeptidase and endopeptidase. TPP2 is structurally unique, forming a massive 4.5-6 MDa complex composed of two stacked, spiral-shaped homodimers, making it one of the largest known eukaryotic enzymes. This assembly enables its involvement in diverse cellular processes, including proteasome-mediated protein turnover, antigen processing for MHC class I presentation, and regulation of apoptosis.
Recombinant TPP2 protein is engineered using molecular cloning techniques, where the *TPP2* gene is expressed in heterologous systems like *E. coli*, insect cells, or mammalian cell lines. This allows large-scale production of purified, active TPP2 for biochemical and functional studies. Researchers leverage recombinant TPP2 to investigate its enzymatic mechanisms, substrate specificity, and interactions with inhibitors or regulatory molecules. Its role in diseases, such as cancer (via apoptosis evasion), neurodegenerative disorders (e.g., Alzheimer’s-linked protein aggregation), and immune dysregulation, has spurred interest in TPP2 as a therapeutic target. Inhibitors of TPP2 are being explored for cancer therapy and immune modulation.
Additionally, recombinant TPP2 is utilized in structural biology (e.g., cryo-EM studies) to elucidate its complex architecture and dynamic conformational changes. Its applications extend to biomarker research, given its dysregulation in pathological conditions. Despite progress, challenges remain in understanding its precise regulatory networks and context-dependent functions, driving ongoing research to harness its potential in medicine and biotechnology.
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