| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ftsZ |
| Uniprot No | P0A9A7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-383aa |
| 氨基酸序列 | MFEPMELTNDAVIKVIGVGGGGGNAVEHMVRERIEGVEFFAVNTDAQALR KTAVGQTIQIGSGITKGLGAGANPEVGRNAADEDRDALRAALEGADMVFI AAGMGGGTGTGAAPVVAEVAKDLGILTVAVVTKPFNFEGKKRMAFAEQGI TELSKHVDSLITIPNDKLLKVLGRGISLLDAFGAANDVLKGAVQGIAELI TRPGLMNVDFADVRTVMSEMGYAMMGSGVASGEDRAEEAAEMAISSPLLE DIDLSGARGVLVNITAGFDLRLDEFETVGNTIRAFASDNATVVIGTSLDP DMNDELRVTVVATGIGMDKRPEITLVTNKQVQQPVMDRYQQHGMAPLTQE QKPVAKVVNDNAPQTAKEPDYLDIPAFLRKQAD |
| 预测分子量 | 56 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FtsZ重组蛋白的3-4篇代表性文献的简要整理：
---
1. **文献名称**: *The essential bacterial cell-division protein FtsZ is a GTPase*
**作者**: Dai, K., Lutkenhaus, J.
**摘要**: 该研究首次在大肠杆菌中克隆并体外表达了FtsZ重组蛋白，证明其具有GTP酶活性，并揭示了其在细菌分裂中形成类“Z环”结构的关键作用，为后续研究FtsZ的分子机制奠定了基础。
---
2. **文献名称**: *GTP-dependent polymerization of Escherichia coli FtsZ protein to form tubules*
**作者**: Mukherjee, A., Lutkenhaus, J.
**摘要**: 通过重组FtsZ蛋白的体外实验，发现GTP结合与水解驱动FtsZ聚合成微管样结构，揭示了其动态组装特性，并提出了FtsZ在细菌分裂中收缩的分子模型。
---
3. **文献名称**: *Crystal structure of the bacterial cell-division protein FtsZ*
**作者**: Löwe, J., Amos, L.A., Erickson, H.P.
**摘要**: 该研究解析了来自海洋古菌的FtsZ重组蛋白的晶体结构，揭示了其与真核微管蛋白的相似性，阐明了GTP结合位点和聚合界面的关键氨基酸残基，为设计靶向FtsZ的抑制剂提供了结构基础。
---
4. **文献名称**: *Screening for inhibitors of FtsZ protein dynamics for antibacterial discovery*
**作者**: Boberek, J.M., et al.
**摘要**: 利用重组FtsZ蛋白建立高通量筛选平台，鉴定出多个小分子化合物可通过干扰FtsZ的GTP酶活性或聚合动力学抑制细菌分裂，验证了FtsZ作为新型抗菌靶点的潜力。
---
**说明**：以上文献涵盖FtsZ重组蛋白的早期功能研究(1-2)、结构解析(3)及药物开发应用(4)。如需具体文献来源(期刊、年份等)，可进一步补充作者所属机构或DOI信息。
FtsZ is a highly conserved prokaryotic protein that plays a central role in bacterial cell division. Functionally analogous to eukaryotic tubulin, it assembles into dynamic filamentous structures at the midcell region, forming the Z-ring—a scaffold for cytokinesis machinery. As a GTPase, FtsZ undergoes polymerization and depolymerization cycles, generating mechanical forces to constrict the cell membrane. Its critical role in bacterial proliferation makes it a promising target for novel antimicrobial agents.
Recombinant FtsZ proteins are engineered through molecular cloning, typically expressed in *E. coli* or other heterologous systems. By isolating the *ftsZ* gene from bacterial genomes and inserting it into expression vectors, researchers produce purified, tag-fused FtsZ for *in vitro* studies. This approach enables precise investigation of its biochemical properties, including GTP hydrolysis kinetics, polymerization dynamics, and interaction with regulatory proteins (e.g., ZipA, FtsA).
Studies using recombinant FtsZ have revealed its structural plasticity and sensitivity to ionic conditions, pH, and macromolecular crowding. Notably, certain plant-derived compounds (e.g., berberine) and synthetic molecules have been shown to inhibit FtsZ polymerization, validating its therapeutic potential. Beyond antimicrobial applications, FtsZ serves as a model system for understanding cytoskeletal evolution, given its phylogenetic relationship with tubulin. Recent advances in cryo-EM and single-molecule imaging have further elucidated its conformational changes during filament assembly. However, species-specific variations in FtsZ behavior underscore the need for pathogen-targeted studies when developing inhibitors. As antibiotic resistance escalates, recombinant FtsZ remains a vital tool for mechanistic research and high-throughput drug screening.
×
