| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CLDN5 |
| Uniprot No | O00501 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-218aa |
| 氨基酸序列 | MGSAALEILGLVLCLVGWGGLILACGLPMWQVTAFLDHNIVTAQTTWKGL WMSCVVQSTGHMQCKVYDSVLALSTEVQAARALTVSAVLLAFVALFVTLA GAQCTTCVAPGPAKARVALTGGVLYLFCGLLALVPLCWFANIVVREFYDP SVPVSQKYELGAALYIGWAATALLMVGGCLLCCGAWVCTGRPDLSFPVKY SAPRRPTATGDYDKKNYV |
| 预测分子量 | 50 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CLDN5重组蛋白的3篇代表性文献的简要信息(注：内容基于领域内常见研究方向整合，非真实文献引用)：
1. **文献名称**：**"Recombinant CLDN5 Expression in Mammalian Cells: A Tool for Blood-Brain Barrier Studies"**
**作者**：Smith A, et al.
**摘要**：研究通过哺乳动物表达系统成功制备重组CLDN5蛋白，验证其促进细胞间紧密连接形成的能力，并证明其在体外血脑屏障模型中的功能，为BBB相关药物递送研究提供工具。
2. **文献名称**：**"Structural Insights into Claudin-5 Revealed by Cryo-EM of Recombinant Protein"**
**作者**：Tanaka K, et al.
**摘要**：利用重组CLDN5蛋白进行冷冻电镜结构解析，首次揭示其跨膜区三维构象及关键功能域(如胞外环ECL1)与屏障通透性的关系，为靶向CLDN5的疗法提供结构基础。
3. **文献名称**：**"CLDN5 Recombinant Protein Modulates Endothelial Permeability in Inflammatory Models"**
**作者**：Chen L, et al.
**摘要**：通过原核系统表达纯化重组CLDN5蛋白，发现其外源性添加可减少炎症因子诱导的内皮细胞通透性增加，提示CLDN5可能作为治疗血管渗漏性疾病的潜在靶点。
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**注**：以上文献名为示例性概括，实际研究中建议通过PubMed或Web of Science以“CLDN5 recombinant protein”“Claudin-5 expression”等关键词检索最新论文。
Claudin-5 (CLDN5) is a key component of tight junction complexes, predominantly expressed in endothelial and epithelial cells. As a member of the claudin family, it plays a critical role in maintaining cell polarity and regulating paracellular permeability, particularly in the blood-brain barrier (BBB). Structurally, CLDN5 consists of four transmembrane domains, two extracellular loops, and intracellular N- and C-termini. The extracellular loops mediate homophilic or heterophilic interactions with adjacent claudins, forming selective barriers that control ion and solute transport. Dysregulation of CLDN5 is implicated in neurological disorders (e.g., stroke, Alzheimer’s disease) and cancer metastasis due to BBB leakage or loss of epithelial integrity.
Recombinant CLDN5 protein is produced using expression systems like Escherichia coli or mammalian cells, often tagged with affinity markers (e.g., His-tag) for purification. Its applications span structural studies, antibody development, and functional assays to investigate tight junction dynamics. Researchers use it to model BBB permeability in vitro, screen drugs targeting barrier integrity, or study pathogenic mechanisms of neurotropic viruses that exploit CLDN5 for entry. Notably, CLDN5 overexpression or knockdown models help validate its role in disease progression. However, challenges persist in preserving its native conformation during recombinant production, as post-translational modifications (e.g., phosphorylation) in eukaryotic systems may influence functionality. Despite this, CLDN5 recombinant proteins remain vital tools for advancing vascular biology and therapeutic strategies for barrier-related pathologies.
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