| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AQP11 |
| Uniprot No | Q8NBQ7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-271aa |
| 氨基酸序列 | MSPLLGLRSELQDTCTSLGLMLSVVLLMGLARVVARQQLHRPVAHAFVLEFLATFQLCCCTHELQLLSEQHPAHPTWTLTLVYFFSLVHGLTLVGTSSNPCGVMMQMMLGGMSPETGAVRLLAQLVSALCSRYCTSALWSLGLTQYHVSERSFACKNPIRVDLLKAVITEAVCSFLFHSALLHFQEVRTKLRIHLLAALITFLVYAGGSLTGAVFNPALALSLHFMCFDEAFPQFFIVYWLAPSLGILLMILMFSFFLPWLHNNHTINKKE |
| 预测分子量 | 30,2 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AQP11重组蛋白的3篇参考文献示例(内容为模拟，非真实文献)：
1. **文献名称**: "Functional characterization of recombinant AQP11 in cellular osmotic regulation"
**作者**: Tanaka K, et al.
**摘要**: 研究通过大肠杆菌系统表达AQP11重组蛋白，验证其在细胞膜上的水通道功能，发现AQP11对低渗环境中的细胞体积调节起关键作用。
2. **文献名称**: "Crystal structure and ion transport mechanism of human AQP11"
**作者**: Zhang Y, et al.
**摘要**: 利用昆虫细胞表达系统获得高纯度AQP11重组蛋白，解析其晶体结构，揭示其独特的跨膜通道构象及潜在的小分子溶质转运机制。
3. **文献名称**: "AQP11 deficiency-associated nephropathy: Insights from recombinant protein models"
**作者**: Chen L, et al.
**摘要**: 通过哺乳动物细胞表达AQP11重组蛋白，模拟基因敲除模型，证实AQP11缺失导致内质网应激和肾小管细胞凋亡，与多囊肾病相关。
注：以上文献信息为虚构示例，实际引用需查询PubMed/SCI数据库获取真实文献。
Aquaporin 11 (AQP11) is an atypical member of the aquaporin superfamily, a group of membrane channel proteins primarily known for facilitating water transport across cellular membranes. Unlike classical aquaporins (AQP1-10), which exhibit well-characterized water or glycerol permeability, AQP11 and its closest homolog AQP12 are classified as "superaquaporins" due to their divergent structural features and uncertain physiological roles. AQP11 is predicted to adopt a conserved aquaporin fold with six transmembrane domains and two asparagine-proline-alanine (NPA) motifs, but its unique pore architecture suggests distinct substrate selectivity, possibly involving metabolites, ions, or reactive oxygen species rather than bulk water.
Initially identified in 2002. AQP11 is expressed in multiple tissues, including the kidney, liver, brain, and testes. Studies in knockout mice revealed its critical role in embryonic development and organ function. AQP11-deficient mice develop lethal renal cysts and mitochondrial abnormalities, linking the protein to cellular osmoregulation, organelle homeostasis, and stress responses. In humans, AQP11 mutations are associated with congenital kidney defects, implicating its potential role in polycystic kidney disease pathogenesis.
Recombinant AQP11 proteins, typically produced in bacterial or mammalian expression systems, enable structural and functional studies. These engineered proteins often include affinity tags (e.g., His-tag) for purification and tracking. Research using recombinant AQP11 has advanced insights into its subcellular localization (endoplasmic reticulum, mitochondria-associated membranes), pH-sensitive gating mechanisms, and interactions with metabolic enzymes. Current investigations focus on its potential as a therapeutic target for metabolic disorders, neurodegenerative diseases, and cystic pathologies, though its exact transport substrates and regulatory pathways remain incompletely defined.
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