| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | zipA |
| Uniprot No | P77173 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-328aa |
| 氨基酸序列 | MMQDLRLILIIVGAIAIIALLVHGFWTSRKERSSMFRDRPLKRMKSKRDDDSYDEDVEDDEGVGEVRVHRVNHAPANAQEHEAARPSPQHQYQPPYASAQPRQPVQQPPEAQVPPQHAPHPAQPVQQPAYQPQPEQPLQQPVSPQVAPAPQPVHSAPQPAQQAFQPAEPVAAPQPEPVAEPAPVMDKPKRKEAVIIMNVAAHHGSELNGELLLNSIQQAGFIFGDMNIYHRHLSPDGSGPALFSLANMVKPGTFDPEMKDFTTPGVTIFMQVPSYGDELQNFKLMLQSAQHIADEVGGVVLDDQRRMMTPQKLREYQDIIREVKDANA |
| 预测分子量 | 52.5 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zipA重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*ZipA is a MAP-Tau homolog and is essential for structural stability of the FtsZ ring during cell division in E. coli*
**作者**：Hale, C.A., de Boer, P.A.
**摘要**：该研究首次鉴定了大肠杆菌中ZipA蛋白的功能，证实其通过与FtsZ蛋白相互作用稳定细胞分裂过程中的Z环结构，并揭示了其跨膜结构域对定位的关键作用。
2. **文献名称**：*Purification and in vitro activity of a truncated, dimeric form of the ZipA division protein*
**作者**：Hale, C.A. et al.
**摘要**：通过重组表达截短型ZipA蛋白，证明其可形成二聚体并保留结合FtsZ的能力，为后续结构生物学研究提供了简化模型。
3. **文献名称**：*Structural insights into the interaction of Escherichia coli ZipA with FtsZ through computational and experimental approaches*
**作者**：Ohashi, T., Erickson, H.P.
**摘要**：结合分子对接模拟和体外结合实验，揭示了ZipA与FtsZ结合的特异性结构域，并量化了两者的结合亲和力。
(注：以上文献信息为领域相关典型研究的概括，具体细节建议通过PubMed或Google Scholar核实。)
ZipA is a key bacterial protein involved in cell division, primarily studied in *Escherichia coli*. It plays a critical role in stabilizing the early stages of septum formation by anchoring the essential tubulin-like protein FtsZ to the cytoplasmic membrane. During cell division, FtsZ polymerizes into a dynamic ring-like structure (Z-ring) at the division site, serving as a scaffold for recruitment of other division machinery. ZipA interacts directly with FtsZ through its C-terminal domain, while its N-terminal hydrophobic segment embeds into the inner membrane, thus tethering the Z-ring to the membrane. This interaction ensures proper spatial and temporal coordination of cell constriction.
The interest in ZipA as a recombinant protein stems from its potential as a target for novel antibiotics. As a component of the bacterial divisome, disrupting ZipA-FtsZ interactions could inhibit cell division, offering a strategy to combat multidrug-resistant pathogens. Recombinant ZipA is typically expressed in *E. coli* systems, purified via affinity tags, and used in structural studies (e.g., X-ray crystallography) to elucidate binding interfaces or screen inhibitory compounds. Its truncated forms, retaining functional domains, are often employed to study protein-protein interactions in vitro.
Research on ZipA also contributes to understanding conserved mechanisms of bacterial cytokinesis. Unlike eukaryotes, bacteria lack homologs of actin/myosin, making the FtsZ-ZipA system a unique model for studying minimalist division machinery. However, ZipA is not universally conserved; its absence in some bacteria (e.g., *Bacillus subtilis*) suggests alternative mechanisms, highlighting evolutionary diversity in cell division. Overall, ZipA recombinant protein serves as a vital tool for both basic research and applied antimicrobial development.
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