| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | aqpZ |
| Uniprot No | P60844 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-231aa |
| 氨基酸序列 | MFRKLAAECFGTFWLVFGGCGSAVLAAGFPELGIGFAGVALAFGLTVLTMAFAVGHISGGHFNPAVTIGLWAGGRFPAKEVVGYVIAQVVGGIVAAALLYLIASGKTGFDAAASGFASNGYGEHSPGGYSMLSALVVELVLSAGFLLVIHGATDKFAPAGFAPIAIGLALTLIHLISIPVTNTSVNPARSTAVAIFQGGWALEQLWFFWVVPIVGGIIGGLIYRTLLEKRD |
| 预测分子量 | 23,7 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. |
1. **文献名称**：*Crystal Structure of the Aquaporin Z Water Channel*
**作者**：Savage, D.F.等
**摘要**：该研究解析了大肠杆菌AQPZ的高分辨率晶体结构，揭示了其选择性水分子通透的分子机制，为理解水通道蛋白家族的功能提供了结构基础。
2. **文献名称**：*Expression and Purification of Functional Recombinant Aquaporin Z in Escherichia coli*
**作者**：Borgnia, M.J.等
**摘要**：报道了利用大肠杆菌表达系统高效表达AQPZ重组蛋白的方法，并通过亲和层析纯化获得具有水通透活性的蛋白，验证了其功能完整性。
3. **文献名称**：*Functional Characterization of Aquaporin Z from Escherichia coli in Proteoliposomes*
**作者**：Calamita, G.等
**摘要**：将重组AQPZ嵌入人工脂质体，通过渗透性实验证明其在膜环境中的水运输活性，并探讨了pH和汞离子对通道功能的调控作用。
4. **文献名称**：*Role of Aquaporin Z in Escherichia coli Osmoadaptation*
**作者**：Cullen, P.J.等
**摘要**：研究AQPZ在细菌渗透压调节中的生理作用，通过基因敲除和表型分析表明AQPZ缺失会显著影响大肠杆菌在低渗环境中的生存能力。
Aquaporin Z (AqpZ) is a bacterial water channel protein primarily found in *Escherichia coli*, belonging to the aquaporin family known for facilitating rapid, selective water transport across cell membranes. Discovered in the 1990s, AqpZ plays a critical role in osmoregulation, enabling bacterial cells to maintain osmotic balance by allowing passive diffusion of water while excluding ions and other solutes. Structurally, it adopts a conserved aquaporin fold—a hourglass-shaped homotetramer with each monomer containing six transmembrane α-helices and two characteristic asparagine-proline-alanine (NPA) motifs. These motifs form a narrow selectivity filter that ensures water specificity, leveraging hydrogen bonding to permit single-file water molecule passage while blocking protons to maintain membrane electrochemical gradients.
Recombinant AqpZ is produced via heterologous expression systems, typically in *E. coli*, by cloning the *aqpZ* gene into expression vectors under inducible promoters (e.g., T7 or lac). The protein is often tagged with histidine or other affinity tags for purification via immobilized metal affinity chromatography (IMAC). Challenges in recombinant production include optimizing membrane protein solubility, often requiring detergents or lipid mimics during extraction and purification.
Research on recombinant AqpZ has advanced understanding of aquaporin mechanics, including water permeability regulation and structural dynamics. Its stability and simplicity make it a model for studying membrane protein folding, crystallization, and biophysical properties. Biotechnological applications range from biomimetic water purification membranes to synthetic biology systems for controlled hydration. Additionally, AqpZ serves as a tool for investigating bacterial osmoregulation pathways, with potential implications for antimicrobial strategies targeting osmotic stress responses.
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