纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | AQP5 |
Uniprot No | P55064 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-265aa |
氨基酸序列 | MKKEVCSVAFLKAVFAEFLATLIFVFFGLGSALKWPSALPTILQIALAFG LAIGTLAQALGPVSGGHINPAITLALLVGNQISLLRAFFYVAAQLVGAIA GAGILYGVAPLNARGNLAVNALNNNTTQGQAMVVELILTFQLALCIFAST DSRRTSPVGSPALSIGLSVTLGHLVGIYFTGCSMNPARSFGPAVVMNRFS PAHWVFWVGPIVGAVLAAILYFYLLFPNSLSLSERVAIIKGTYEPDEDWE EQREERKKTMELTTR |
预测分子量 | 31 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AQP5重组蛋白的3篇代表性文献(虚构示例,仅供格式参考):
1. **《Expression and functional characterization of recombinant human AQP5 in insect cells》**
- 作者:Yang, B., et al.
- 摘要:研究通过杆状病毒-昆虫细胞系统成功表达并纯化人源AQP5重组蛋白,证实其水通道活性,为后续功能研究提供工具。
2. **《Cryo-EM structure of AQP5 reveals key residues for water permeability》**
- 作者:Sui, H., et al.
- 摘要:利用冷冻电镜解析AQP5重组蛋白的高分辨率结构,揭示其水分子选择性渗透的分子机制及关键氨基酸位点。
3. **《AQP5-targeted small molecule modulators for treating dry eye syndrome》**
- 作者:de Almeida, A., et al.
- 摘要:基于重组AQP5蛋白筛选小分子化合物,发现两种可增强AQP5活性的候选药物,有望用于干眼症治疗。
4. **《Regulation of AQP5 expression in lung cancer cells via recombinant protein interaction analysis》**
- 作者:Macho, V., et al.
- 摘要:通过重组AQP5蛋白与肺癌细胞互作实验,证明AQP5过表达通过调控EGFR信号通路促进肿瘤迁移。
(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等。)
Aquaporin-5 (AQP5) is a member of the aquaporin family, a class of transmembrane channel proteins that facilitate selective water transport across cell membranes. Primarily expressed in exocrine glands (e.g., salivary, lacrimal, and sweat glands) and epithelial tissues (e.g., lung, cornea, and gastrointestinal tract), AQP5 plays a critical role in maintaining fluid homeostasis, secretion, and hydration. Structurally, it consists of six transmembrane α-helices with two conserved asparagine-proline-alanine (NPA) motifs forming the water-conducting pore. Dysregulation of AQP5 has been implicated in pathologies such as Sjögren’s syndrome, cystic fibrosis, cancer metastasis, and dry eye disease, making it a target for therapeutic research.
Recombinant AQP5 protein is engineered through genetic cloning, typically using prokaryotic (e.g., *E. coli*) or eukaryotic (e.g., mammalian or insect cell) expression systems. These systems allow large-scale production of the protein with post-translational modifications mimicking native forms. Purification methods often involve affinity chromatography, leveraging tags like His or GST for isolation. The recombinant protein serves as a vital tool for studying AQP5’s biophysical properties, regulatory mechanisms, and interactions with drugs or signaling molecules. It also aids in developing antibodies, diagnostic assays, and molecule-targeted therapies. Recent studies focus on modulating AQP5 activity to address fluid secretion disorders or inhibit cancer progression. However, challenges remain in maintaining structural stability during production and ensuring functional accuracy in vitro. Ongoing research aims to optimize expression platforms and explore AQP5’s role in cellular signaling beyond passive water transport.
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