| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AQP1 |
| Uniprot No | P29972 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-269aa |
| 氨基酸序列 | ASEFKKKLFWRAVVAEFLATTLFVFISIGSALGFKYPVGNNQTAVQDNVKVSLAFGLSIATLAQSVGHISGAHLNPAVTLGLLLSCQISIFRALMYIIAQCVGAIVATAILSGITSSLTGNSLGRNDLADGVNSGQGLGIEIIGTLQLVLCVLATTDRRRRDLGGSAPLAIGLSVALGHLLAIDYTGCGINPARSFGSAVITHNFSNHWIFWVGPFIGGALAVLIYDFILAPRSSDLTDRVKVWTSGQVEEYDLDADDINSRVEMKPK |
| 预测分子量 | 41.3 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AQP1重组蛋白的3篇代表性文献(简化版)，供参考：
1. **文献名称**：Crystal structure of human aquaporin 1 (AQP1)
**作者**：Murata, K. et al.
**摘要**：通过X射线晶体学解析了人AQP1重组蛋白的原子级结构，揭示了其选择性水通道的分子机制，证实了四聚体结构及水分子传输路径。
2. **文献名称**：Functional characterization of human aquaporin 1 expression in Saccharomyces cerevisiae
**作者**：Verkman, A.S. et al.
**摘要**：利用酵母表达系统成功重组人AQP1蛋白，验证其渗透水通透性功能，建立了高效的重组表达及活性检测模型。
3. **文献名称**：Recombinant AQP1 expression in lung epithelial cells improves fluid transport in vitro
**作者**：Fang, X. et al.
**摘要**：通过重组AQP1在肺上皮细胞中的过表达，证明其显著增强细胞膜水通透性，为治疗肺水肿等疾病提供了实验依据。
*注：以上为简化示例，实际文献需通过PubMed/Google Scholar检索获取完整信息。建议优先选择发表于Nature、Science、PNAS等期刊的高被引论文，重点关注结构解析、功能验证或疾病应用方向的研究。*
Aquaporin-1 (AQP1) is a member of the aquaporin family, a class of integral membrane proteins that facilitate selective and rapid transport of water and small solutes across biological membranes. Discovered in 1988. AQP1 was the first water channel protein identified and is widely expressed in tissues involved in fluid homeostasis, including red blood cells, kidneys, lungs, and the vascular system. Structurally, AQP1 forms a homotetramer, with each monomer containing six transmembrane domains and two conserved asparagine-proline-alanine (NPA) motifs that create a selective pore for water molecules. Its ability to regulate osmotic water permeability has made it a critical focus in understanding cellular hydration, ion balance, and related pathologies.
Recombinant AQP1 proteins are engineered versions produced through genetic engineering, typically in heterologous expression systems like *E. coli*, yeast, or mammalian cell cultures. These systems enable large-scale production of purified AQP1 for functional and structural studies. Recombinant AQP1 retains the native protein's biophysical properties, allowing researchers to study its gating mechanisms, permeability regulation, and interactions with inhibitors or modulators. This has advanced drug discovery efforts targeting conditions linked to AQP1 dysfunction, such as edema, glaucoma, and cancer metastasis, where abnormal water transport exacerbates disease progression.
Beyond biomedical research, recombinant AQP1 has inspired biotechnological applications, including synthetic biomimetic membranes for water purification and energy-efficient filtration. However, challenges persist in maintaining protein stability during purification and ensuring proper membrane integration in artificial systems. Ongoing studies aim to optimize expression protocols and functional assays, solidifying AQP1's role as a model protein for both basic science and translational innovation.
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