| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 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. |
以下是关于aqpZ重组蛋白的3篇参考文献及其摘要概括：
1. **"Molecular cloning and characterization of aqpZ, a water channel gene from Escherichia coli"**
- **作者**: Calamita, G., et al.
- **摘要**: 该研究首次报道了大肠杆菌水通道蛋白基因aqpZ的克隆与功能验证。通过重组表达aqpZ蛋白，证实其显著提升细胞膜的水通透性，并通过渗透实验证明其选择性水转运特性。
2. **"Crystal structure of AqpZ tetramer reveals two distinct water-conducting pathways"**
- **作者**: Savage, D.F., et al.
- **摘要**: 通过X射线晶体学解析了重组aqpZ蛋白的四聚体结构，揭示了两种独立的水分子传输通道，为理解水通道蛋白的分子机制提供了结构基础。
3. **"Functional reconstitution and molecular dynamics of Escherichia coli aquaporin Z"**
- **作者**: de Groot, B.L., et al.
- **摘要**: 将重组aqpZ蛋白嵌入脂质体进行功能重建，结合分子动力学模拟，阐明其高效水转运的分子机制，并验证其对甘油等分子的通透屏障作用。
4. **"Site-directed mutagenesis of AqpZ: Role of conserved residues in water permeability"**
- **作者**: Jung, J.S., et al.
- **摘要**: 通过定点突变技术研究重组aqpZ蛋白中保守氨基酸残基(如Arg189)对水通道功能的影响，发现关键残基通过静电作用调控水分子选择性通过。
这些研究涵盖了aqpZ重组蛋白的基因克隆、结构解析、功能模拟及关键位点分析，提供了从分子机制到应用基础的全方位见解。
Aquaporin Z (AqpZ), a member of the aquaporin family, is a transmembrane protein primarily found in *Escherichia coli* and other Gram-negative bacteria. It functions as a selective water channel, facilitating rapid passive transport of water molecules across cell membranes while excluding ions and other solutes. This permeability is critical for bacterial osmoregulation, enabling cells to maintain osmotic balance under varying environmental conditions. AqpZ is structurally characterized by six transmembrane α-helices and two shorter helices forming a narrow pore, with conserved asparagine-proline-alanine (NPA) motifs critical for water selectivity.
Recombinant AqpZ refers to the protein produced through genetic engineering, typically by cloning the *aqpZ* gene into expression vectors (e.g., plasmid systems) and expressing it in heterologous hosts like *E. coli* or yeast. The recombinant protein is often tagged (e.g., His-tag) for simplified purification via affinity chromatography. Studies on recombinant AqpZ have advanced understanding of aquaporin mechanics, including how pore architecture dictates selectivity and how structural dynamics regulate water flux. Its stability and simplicity make it a model for investigating aquaporin-related pathologies in humans, such as edema or neurological disorders linked to water channel dysfunction.
Biotechnologically, recombinant AqpZ has potential applications in biomimetic membranes for water purification, biosensors, or synthetic biology systems requiring precise water transport control. Research also explores its role in bacterial survival mechanisms, aiding antimicrobial strategies targeting osmotic regulation. Despite its prokaryotic origin, AqpZ shares functional and structural homology with eukaryotic aquaporins, making it a valuable tool for comparative studies. Overall, recombinant AqpZ bridges fundamental microbial physiology and applied bioengineering, offering insights into both cellular water dynamics and novel biotechnological solutions.
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