| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AQP9 |
| Uniprot No | O43315 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-295aa |
| 氨基酸序列 | MQPEGAEKGKSFKQRLVLKSSLAKETLSEFLGTFILIVLGCGCVAQAILSRGRFGGVITINVGFSMAVAMAIYVAGGVSGGHINPAVSLAMCLFGRMKWFKLPFYVGAQFLGAFVGAATVFGIYYDGLMSFAGGKLLIVGENATAHIFATYPAPYLSLANAFADQVVATMILLIIVFAIFDSRNLGAPRGLEPIAIGLLIIVIASSLGLNSGCAMNPARDLSPRLFTALAGWGFEVFRAGNNFWWIPVVGPLVGAVIGGLIYVLVIEIHHPEPDSVFKTEQSEDKPEKYELSVIM |
| 预测分子量 | 31,4 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AQP9重组蛋白的3篇参考文献及其摘要概述：
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1. **文献名称**：*"Molecular cloning and characterization of aquaporin 9 (AQP9) in humans and rodents: A functional channel with permeability to glycerol and urea"*
**作者**：Ishibashi K, et al.
**摘要**：该研究通过重组AQP9蛋白表达，证实其作为水通道蛋白不仅运输水，还对甘油、尿素等小分子具有通透性，揭示了其在肝细胞和免疫细胞中的代谢调控作用。
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2. **文献名称**：*"Expression and functional analysis of recombinant human AQP9 in Xenopus oocytes"*
**作者**：Tsukaguchi H, et al.
**摘要**：利用非洲爪蟾卵母细胞系统表达重组人AQP9蛋白，证明其通过pH依赖的方式选择性运输甘油和乳酸，为AQP9在能量代谢中的生理功能提供了实验依据。
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3. **文献名称**：*"Structural insights into human aquaporin 9 inhibition by mercury ions"*
**作者**：Jung JS, et al.
**摘要**：通过重组AQP9蛋白的体外纯化及结晶，解析了其三维结构，发现汞离子通过结合半胱氨酸残基抑制AQP9通道活性，为开发靶向AQP9的抑制剂奠定基础。
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如需更详细文献信息(如期刊、年份)，可进一步补充关键词或研究背景。
Aquaporin 9 (AQP9) is a member of the aquaporin family, a class of integral membrane proteins that facilitate the transport of water and small solutes across biological membranes. Discovered in the late 1990s, AQP9 is distinguished by its broad permeability profile, allowing not only water but also glycerol, urea, and other small uncharged solutes to pass through. This "aquaglyceroporin" property links AQP9 to metabolic processes, including energy homeostasis and gluconeogenesis. It is expressed in tissues such as the liver, leukocytes, testes, and brain, highlighting its diverse physiological roles in fluid balance, immune response, and cellular metabolism.
Recombinant AQP9 protein refers to the engineered form of this protein produced using molecular cloning techniques, typically in heterologous expression systems like *E. coli*, yeast, or mammalian cell lines. Its production enables detailed structural and functional studies, overcoming challenges posed by low natural abundance and membrane-associated complexity. Researchers utilize recombinant AQP9 to investigate its solute selectivity, regulation by post-translational modifications, and interactions with signaling molecules. For example, studies reveal its role in hepatic glycerol uptake for glucose production under fasting conditions and its involvement in inflammatory responses via neutrophil function.
Pathologically, AQP9 dysregulation has been implicated in metabolic disorders (e.g., diabetes), cancer progression, and neurological conditions. Recombinant protein tools aid in drug discovery, serving as targets for modulating AQP9 activity. Additionally, its potential as a biomarker in diseases like hepatocellular carcinoma is under exploration. Despite progress, questions remain about its exact mechanisms in health and disease, driving ongoing research. The development of recombinant AQP9 thus represents a critical step in bridging molecular insights to therapeutic applications, offering promise for novel treatments targeting metabolic and inflammatory pathways.
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