| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TMPRSS2 |
| Uniprot No | O15393 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 383-492aa |
| 氨基酸序列 | GWGATEEKGKTSEVLNAAKVLLIETQRCNSRYVYDNLITPAMICAGFLQG NVDSCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTD WIYRQMRADG |
| 预测分子量 | 38 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3篇关于TMPRSS2重组蛋白研究的参考文献，涵盖不同研究方向：
---
1. **文献名称**: *Expression and purification of recombinant TMPRSS2 serine protease in E. coli for biochemical characterization*
**作者**: Kim, J.H., et al.
**摘要**: 该研究成功在大肠杆菌中表达并纯化可溶性TMPRSS2重组蛋白，通过优化表达条件(如诱导温度、IPTG浓度)和亲和层析技术获得高纯度蛋白。酶活性实验表明重组蛋白具有切割荧光底物的能力，为后续抑制剂筛选提供了基础。
2. **文献名称**: *Structural insights into TMPRSS2 through recombinant expression in insect cells using baculovirus system*
**作者**: Smith, T.R., et al.
**摘要**: 利用杆状病毒-昆虫细胞系统表达TMPRSS2胞外域重组蛋白，通过冷冻电镜解析其三维结构。研究发现其催化三联体结构与已知丝氨酸蛋白酶高度相似，并揭示了底物结合口袋的关键氨基酸残基，为靶向药物设计提供依据。
3. **文献名称**: *Functional characterization of human TMPRSS2 expressed in HEK293 cells: Role in SARS-CoV-2 spike protein activation*
**作者**: Laporte, M., et al.
**摘要**: 在HEK293细胞中重组表达TMPRSS2.证明其能够切割SARS-CoV-2刺突蛋白的S1/S2位点，增强病毒与宿主膜融合。通过抑制剂卡莫司他(Camostat)验证其蛋白酶活性，提示靶向TMPRSS2的抗病毒治疗潜力。
---
**注**：上述文献为示例，实际引用时需根据具体研究内容检索PubMed或Web of Science获取真实文献(如搜索关键词：TMPRSS2 recombinant expression/purification/structural analysis)。近年研究多聚焦于TMPRSS2与病毒感染机制的关联。
TMPRSS2 (Transmembrane Serine Protease 2) is a type II transmembrane protein belonging to the serine protease family, encoded by the *TMPRSS2* gene on human chromosome 21. It plays a critical role in proteolytic activation of various substrates, including viral glycoproteins and cellular receptors. Structurally, it consists of an N-terminal cytoplasmic domain, a transmembrane region, and an extracellular serine protease domain. The protease domain contains a catalytic triad (His, Asp, Ser) essential for enzymatic activity.
TMPRSS2 is predominantly expressed in epithelial tissues, notably in the prostate, respiratory tract, and gastrointestinal system. Its physiological functions include regulating epithelial sodium channels, modulating inflammation, and processing hormones like matriptase. However, it gained significant attention during the COVID-19 pandemic due to its role in cleaving the SARS-CoV-2 spike protein, enabling viral entry into host cells. This mechanism highlighted TMPRSS2 as a potential therapeutic target for antiviral interventions.
Recombinant TMPRSS2 protein is produced using expression systems (e.g., mammalian, insect, or bacterial cells) to study its biochemical properties, substrate specificity, and interactions with inhibitors. It serves as a tool for *in vitro* research on viral pathogenesis, host-pathogen interactions, and drug screening. Additionally, TMPRSS2 is implicated in cancer progression, particularly in prostate cancer, where gene fusions (e.g., *TMPRSS2-ERG*) drive oncogenic signaling.
Despite its biomedical relevance, challenges remain in understanding tissue-specific regulation and off-target effects of TMPRSS2 inhibition. Recombinant TMPRSS2 continues to be vital for developing targeted therapies and diagnostics for infectious diseases and cancers.
×
