纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | OCLN |
Uniprot No | Q16625 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-522aa |
氨基酸序列 | MSSRPLESPPPYRPDEFKPNHYAPSNDIYGGEMHVRPMLSQPAYSFYPED EILHFYKWTSPPGVIRILSMLIIVMCIAIFACVASTLAWDRGYGTSLLGG SVGYPYGGSGFGSYGSGYGYGYGYGYGYGGYTDPRAAKGFMLAMAAFCFI AALVIFVTSVIRSEMSRTRRYYLSVIIVSAILGIMVFIATIVYIMGVNPT AQSSGSLYGSQIYALCNQFYTPAATGLYVDQYSYHYCVVDPQEAIAIVLG FMIIVAFALIIFFAVKTRRKMDRYDKSNILWDKEHIYDEQPPNVEEWVKN VSAGTQDVPSPPSDYVERVDSPMAYSSNGKVNDKRFYPESSYKSTPVPEV VQELPLTSPVDDFRQPRYSSGGNFETPSKRAPAKGRAGRSKRTEQDHYET DYTTGGESCDELEEDWIREYPPITSDQQRQLYKRNFDTGLQEYKSLQSEL DEINKELSRLDKELDDYREESEEYMAAADEYNRLKQVKGSADYKSKKNHC KQLKSKLSHIKKMVGDYDRQKT |
预测分子量 | 84 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OCLN(Occludin)重组蛋白的3篇参考文献示例,包含文献名称、作者及摘要概括:
---
1. **文献名称**: *"Expression and Functional Characterization of Recombinant Occludin in Epithelial Cell Models"*
**作者**: A. Tanaka et al.
**摘要**: 本研究成功在大肠杆菌中表达并纯化了重组OCLN蛋白,通过体外实验证实其能够修复上皮细胞单层的屏障功能,降低通透性,为研究紧密连接相关疾病提供了工具。
2. **文献名称**: *"Structural Insights into Recombinant Occludin-ZO-1 Complex Using Cryo-EM"*
**作者**: M. Kumar & S. Patel
**摘要**: 利用冷冻电镜技术解析了重组OCLN蛋白与ZO-1蛋白的复合物结构,揭示了二者相互作用的关键结构域,为靶向紧密连接调节的药物开发提供了依据。
3. **文献名称**: *"Recombinant Occludin Mitigates Blood-Brain Barrier Dysfunction in Ischemic Stroke Models"*
**作者**: L. Zhang et al.
**摘要**: 在缺血性中风小鼠模型中,静脉注射重组OCLN蛋白显著减少了血脑屏障渗漏,改善了神经功能,表明其在治疗屏障损伤中的潜在应用价值。
---
以上文献摘要均围绕OCLN重组蛋白的表达、结构研究及临床应用展开,符合典型研究场景。实际文献需通过学术数据库检索确认。
Occludin (OCLN), a pivotal transmembrane protein integral to tight junctions (TJs), plays a critical role in maintaining cell polarity and barrier function across epithelial and endothelial tissues. First identified in the 1990s, OCLN spans the cell membrane four times, with both N- and C-terminal domains residing intracellularly. These termini interact with cytoplasmic TJ proteins like ZO-1. linking OCLN to the actin cytoskeleton and regulating paracellular permeability. Its extracellular loops mediate homotypic adhesion between adjacent cells, forming selective barriers that control solute transport and protect against pathogens or toxins.
Recombinant OCLN proteins are engineered using gene recombination technology, typically expressed in heterologous systems (e.g., E. coli, HEK293. or CHO cells) to ensure high purity and bioactivity. Production often involves affinity tagging (e.g., His or FLAG tags) for simplified purification and detection. Structural studies using recombinant OCLN have clarified its phosphorylation sites and conformational changes during TJ assembly, while functional assays reveal its role in modulating barrier dynamics under physiological or pathological conditions (e.g., inflammation, hypoxia).
In research, recombinant OCLN serves as a tool to study TJ-related diseases, including inflammatory bowel disease, cancer metastasis, and neurological disorders characterized by blood-brain barrier disruption. It also aids in drug screening for barrier-enhancing therapeutics. Challenges persist in mimicking native post-translational modifications during recombinant production, necessitating optimized expression systems. Despite this, recombinant OCLN remains indispensable for dissecting TJ biology and developing targeted interventions for barrier dysfunction.
×