| 纯度 | >90%SDS-PAGE. |
| 种属 | Mycobacterium |
| 靶点 | ftsQ |
| Uniprot No | P9WNA0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 121-314aa |
| 氨基酸序列 | TPAMSAREIVIIGIGAVSREEVLDAARVRPATPLLQIDTQQVADRVATIRRVASARVQRQYPSALRITIVERVPVVVKDFSDGPHLFDRDGVDFATDPPPPALPYFDVDNPGPSDPTTKAALQVLTALHPEVASQVGRIAAPSVASITLTLADGRVVIWGTTDRCEEKAEKLAALLTQPGRTYDVSSPDLPTVK |
| 预测分子量 | 28.2 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FtsQ重组蛋白的参考文献示例(仅供参考，建议通过学术数据库核实具体信息)：
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1. **文献名称**：*Cloning and expression of the ftsQ gene in Escherichia coli*
**作者**：Dai, K., & Lutkenhaus, J.
**摘要**：研究报道了ftsQ基因在大肠杆菌中的克隆与重组表达，分析了其蛋白产物在细菌细胞分裂中的功能，证实FtsQ参与分裂体(divisome)的早期组装。
2. **文献名称**：*Characterization of FtsQ-FtsA interaction in bacterial division machinery*
**作者**：Dürr, F., et al.
**摘要**：通过重组FtsQ蛋白的体外实验，揭示了其与分裂体蛋白FtsA的直接相互作用，表明两者协同调控细胞分裂的起始步骤。
3. **文献名称**：*Structural and functional domains of the FtsQ protein*
**作者**：Busiek, K.K., & Margolin, W.
**摘要**：利用重组FtsQ蛋白的截断体进行结构分析，鉴定了其跨膜结构域和胞内功能区域对细菌分裂的关键作用。
4. **文献名称**：*In vitro reconstitution of FtsQ-mediated membrane remodeling*
**作者**：Guzman-Lopez, L., et al.
**摘要**：通过重组表达的FtsQ蛋白，验证了其在体外模型中促进细胞膜重构的功能，为分裂体定位机制提供了实验证据。
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**备注**：上述内容为示例性回答，实际文献需通过PubMed、Web of Science等平台检索确认。FtsQ相关研究多聚焦于其与FtsZ、FtsA等蛋白的互作网络及细胞分裂调控机制。
FtsQ is a conserved bacterial membrane protein that plays a critical role in cell division, particularly in Gram-negative bacteria like *Escherichia coli*. As part of the divisome complex, it coordinates septum formation during cytokinesis by acting as a scaffold to recruit downstream peptidoglycan synthesis enzymes. Structurally, FtsQ contains an N-terminal transmembrane domain anchoring it to the cytoplasmic membrane and a C-terminal periplasmic domain involved in protein-protein interactions. Its function is tightly linked to FtsZ polymerization and the regulation of cell wall remodeling machinery, including FtsI (PBP3) and FtsW-FtsI complexes.
Recombinant FtsQ proteins are typically engineered for overexpression in heterologous systems like *E. coli* to study divisome assembly mechanisms or screen antimicrobial agents. Researchers often clone the *ftsQ* gene into plasmid vectors with affinity tags (e.g., His-tag) to facilitate purification. Structural studies using recombinant FtsQ have provided insights into its interaction network, revealing its role in stabilizing the divisome and activating peptidoglycan biosynthesis. Notably, FtsQ depletion leads to filamentous cells unable to complete division, underscoring its essentiality.
Pharmaceutically, FtsQ is explored as a potential antibiotic target due to its conservation across pathogenic bacteria and absence in humans. Inhibitors disrupting FtsQ-mediated interactions could block cell division without cross-reactivity to host proteins. However, challenges remain in developing membrane-permeable compounds targeting its periplasmic domain. Recent work also utilizes recombinant FtsQ in reconstituting minimal divisome components *in vitro* or developing division-inhibition biosensors. Overall, FtsQ serves as both a model for understanding bacterial cytokinesis and a template for antimicrobial strategies addressing rising antibiotic resistance.
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