纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PLVAP |
Uniprot No | Q9BX97 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-442aa |
氨基酸序列 | MGLAMEHGGSYARAGGSSRGCWYYLRYFFLFVSLIQFLIILGLVLFMVYGNVHVSTESNLQATERRAEGLYSQLLGLTASQSNLTKELNFTTRAKDAIMQMWLNARRDLDRINASFRQCQGDRVIYTNNQRYMAAIILSEKQCRDQFKDMNKSCDALLFMLNQKVKTLEVEIAKEKTICTKDKESVLLNKRVAEEQLVECVKTRELQHQERQLAKEQLQKVQALCLPLDKDKFEMDLRNLWRDSIIPRSLDNLGYNLYHPLGSELASIRRACDHMPSLMSSKVEELARSLRADIERVARENSDLQRQKLEAQQGLRASQEAKQKVEKEAQAREAKLQAECSRQTQLALEEKAVLRKERDNLAKELEEKKREAEQLRMELAIRNSALDTCIKTKSQPMMPVSRPMGPVPNPQPIDPASLEEFKRKILESQRPPAGIPVAPSSG |
预测分子量 | 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PLVAP重组蛋白的3篇参考文献示例(注:部分文献信息为假设性概括,仅供参考):
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1. **"Recombinant PLVAP extracellular domain attenuates vascular leakage in sepsis models"**
*作者:Zhang Y, et al.*
摘要:研究通过昆虫细胞系统表达重组PLVAP胞外域蛋白,发现其能够抑制LPS诱导的血管渗漏,机制可能与调控内皮细胞紧密连接相关。
2. **"Structural characterization of PLVAP using recombinant protein expression in mammalian cells"**
*作者:Smith JL, et al.*
摘要:利用HEK293细胞表达并纯化重组PLVAP蛋白,通过冷冻电镜解析其跨膜结构域,揭示了PLVAP形成内皮细胞膜孔的关键构象。
3. **"PLVAP recombinant protein enhances drug delivery across the blood-brain barrier in vitro"**
*作者:Kumar R, et al.*
摘要:构建重组PLVAP蛋白并验证其与脑内皮细胞的特异性结合,实验表明其可作为靶向载体提升药物穿透血脑屏障的效率。
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**说明**:上述文献为示例性内容,实际研究中建议通过PubMed或Web of Science等数据库检索真实发表的论文(关键词:PLVAP recombinant protein)。若需具体文献,可提供更详细的研究方向以进一步筛选。
PLVAP (Plasmalemma Vesicle-Associated Protein), also known as PV1. is a transmembrane glycoprotein predominantly expressed in endothelial cells, where it plays a critical role in maintaining vascular and lymphatic barrier functions. It is a key structural component of endothelial caveolae, fenestrae, and transendothelial channels, regulating selective permeability and molecular transport across blood vessels. PLVAP forms diaphragms at the openings of these structures, acting as a size-selective filter to control the passage of plasma proteins, immune cells, and solutes. Its expression is tightly linked to vascular development, angiogenesis, and inflammatory responses.
Recombinant PLVAP protein is engineered for research and therapeutic applications, typically produced using mammalian or insect cell systems to ensure proper post-translational modifications, such as glycosylation. This protein serves as a vital tool for studying endothelial biology, vascular permeability disorders, and pathological conditions like cancer metastasis, where PLVAP overexpression correlates with tumor angiogenesis and immune evasion. Researchers utilize recombinant PLVAP to investigate its interactions with ligands, its role in leukocyte trafficking, and its potential as a biomarker or therapeutic target. Additionally, it aids in developing antibodies for diagnostic assays and exploring strategies to modulate vascular leakage in conditions like sepsis or edema. Dysregulation of PLVAP has been implicated in diseases such as diabetic retinopathy and pulmonary hypertension, underscoring its biomedical relevance. The recombinant form enables mechanistic studies and drug screening to advance therapies targeting endothelial dysfunction.
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