| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AQP7 |
| Uniprot No | O14520 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-342aa |
| 氨基酸序列 | MVQASGHRRSTRGSKMVSWSVIAKIQEILQRKMVREFLAEFMSTYVMMVFGLGSVAHMVLNKKYGSYLGVNLGFGFGVTMGVHVAGRISGAHMNAAVTFANCALGRVPWRKFPVYVLGQFLGSFLAAATIYSLFYTAILHFSGGQLMVTGPVATAGIFATYLPDHMTLWRGFLNEAWLTGMLQLCLFAITDQENNPALPGTEALVIGILVVIIGVSLGMNTGYAINPSRDLPPRIFTFIAGWGKQVFSNGENWWWVPVVAPLLGAYLGGIIYLVFIGSTIPREPLKLEDSVAYEDHGITVLPKMGSHEPTISPLTPVSVSPANRSSVHPAPPLHESMALEHF |
| 预测分子量 | 38.6 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AQP7重组蛋白的3篇参考文献示例(文献信息为模拟虚构内容，仅供参考格式)：
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1. **文献名称**：*Cloning and Functional Characterization of Human Aquaporin 7 (AQP7) as a Glycerol Channel*
**作者**：Kondo H, et al.
**摘要**：该研究首次报道了人类AQP7基因的克隆及其重组蛋白在哺乳动物细胞中的表达，证实AQP7在甘油转运中的关键作用，并揭示了其在脂肪代谢中的潜在调控机制。
2. **文献名称**：*Expression and Purification of Recombinant AQP7 in E. coli: Role in Insulin Resistance*
**作者**：Hibuse T, et al.
**摘要**：通过大肠杆菌系统成功表达并纯化AQP7重组蛋白，发现其甘油通透性在胰岛素抵抗模型中显著降低，提示AQP7功能异常可能与2型糖尿病相关。
3. **文献名称**：*AQP7-Deficient Mice Reveal Impaired Lipolysis and Adipocyte Dysfunction*
**作者**：Maeda N, et al.
**摘要**：利用AQP7敲除小鼠模型，结合重组蛋白功能分析，证明AQP7缺失导致脂肪细胞内甘油积累，进而影响脂肪分解和能量代谢平衡。
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注：以上文献为示例，实际引用需查询真实数据库(如PubMed、Web of Science)并核对原文信息。
**Background of AQP7 Recombinant Protein**
Aquaporin-7 (AQP7) is a member of the aquaporin family, a class of transmembrane channel proteins that facilitate the selective transport of water and small solutes across biological membranes. Belonging to the aquaglyceroporin subfamily, AQP7 is uniquely permeable to glycerol in addition to water, playing a critical role in energy metabolism and lipid homeostasis. It is predominantly expressed in adipose tissue, where it regulates glycerol efflux from adipocytes during lipolysis, a process essential for maintaining systemic glucose and lipid balance. AQP7 is also detected in other tissues, including the kidney, testis, and skeletal muscle, suggesting broader physiological relevance.
Dysregulation of AQP7 has been implicated in metabolic disorders such as obesity, insulin resistance, and diabetes. For instance, reduced AQP7 expression in adipose tissue correlates with impaired glycerol release, contributing to hyperglycemia and ectopic lipid accumulation. These associations highlight AQP7 as a potential therapeutic target for metabolic syndrome.
Recombinant AQP7 protein is generated through genetic engineering, typically by cloning the AQP7 gene into expression systems like *E. coli* or mammalian cell lines. This allows large-scale production of the protein for functional and structural studies. The recombinant form retains native channel activity, enabling researchers to investigate its permeability mechanisms, regulatory pathways (e.g., phosphorylation by insulin signaling), and interactions with drugs or inhibitors.
Applications of AQP7 recombinant protein span *in vitro* assays, antibody development, and drug screening. It also aids in elucidating the molecular basis of diseases linked to glycerol metabolism and membrane transport defects. By providing a tool to dissect AQP7’s role in health and disease, recombinant AQP7 advances both basic research and the development of targeted therapies for metabolic conditions.
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