纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | NPC1 |
Uniprot No | O15118 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 151-250aa |
氨基酸序列 | GFANAMYNACRDVEAPSSNDKALGLLCGKDADACNATNWIEYMFNKDNGQ APFTITPVFSDFPVHGMEPMNNATKGCDESVDEVTAPCSCQDCSIVCGPK |
预测分子量 | 37 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NPC1重组蛋白的3篇代表性文献及其摘要概括:
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1. **文献名称**:*Structural basis for human NPC1-mediated cholesterol transport*
**作者**:Qian, H., Wu, X., Du, X., Yao, X., Zhao, X., Lee, D., ... & Yan, N.
**摘要**:通过冷冻电镜解析人源NPC1蛋白的原子结构,揭示其胆固醇结合域构象及跨膜通道特征,阐明了NPC1介导细胞内胆固醇转运的分子机制,为尼曼-匹克病C型的病理机制提供结构生物学依据。
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2. **文献名称**:*A small molecule inhibitor of the NPC1 protein attenuates Ebola virus infection*
**作者**:Côté, M., Misasi, J., Ren, T., Bruchez, A., Lee, K., & Chandran, K.
**摘要**:研究发现重组NPC1蛋白是埃博拉病毒入侵宿主细胞的关键宿主因子,通过高通量筛选鉴定出靶向NPC1的小分子抑制剂,证实其可通过阻断病毒糖蛋白与NPC1结合抑制病毒感染,为抗病毒药物开发提供新靶点。
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3. **文献名称**:*Niemann-Pick C1 protein regulates cholesterol transport to the trans-Golgi network and plasma membrane caveolae*
**作者**:Watari, H., Blanchette-Mackie, E.J., Dwyer, N.K., & Pentchev, P.G.
**摘要**:利用重组NPC1蛋白表达系统,证明NPC1通过调控溶酶体胆固醇向反式高尔基体及质膜穴样结构的定向转运,维持细胞胆固醇稳态,其功能缺失导致胆固醇异常堆积并引发神经退行性病变。
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**领域关联性**:上述文献涵盖NPC1的结构解析、疾病机制及治疗应用,涉及分子生物学、病毒学和药理学领域,可作为相关研究的核心参考文献。
**Background of NPC1 Recombinant Protein**
The Niemann-Pick type C1 (NPC1) protein is a critical transmembrane glycoprotein encoded by the *NPC1* gene, located in the endosomal/lysosomal system. It plays a central role in intracellular cholesterol trafficking, facilitating the efflux of cholesterol and other lipids from lysosomes to cellular compartments. Mutations in *NPC1* cause Niemann-Pick disease type C (NPC), a rare lysosomal storage disorder characterized by progressive neurodegeneration, hepatosplenomegaly, and premature death.
NPC1 comprises 13 transmembrane domains, cytoplasmic N-terminal domains, and a sterol-sensing region. Its dysfunction disrupts lipid homeostasis, leading to lysosomal accumulation of unesterified cholesterol and glycosphingolipids. Studying NPC1’s structure-function relationship is essential for understanding NPC pathogenesis and developing therapies.
Recombinant NPC1 protein, produced via heterologous expression systems (e.g., mammalian CHO cells or *E. coli*), enables in vitro studies of its biochemical properties and interactions. Purified NPC1 is used to investigate cholesterol-binding mechanisms, screen small-molecule correctors (e.g., cyclodextrins), and evaluate gene therapy vectors. Recent advances include engineered NPC1 variants to enhance stability or delivery efficiency in preclinical models.
Research on NPC1 recombinant protein also explores its potential as a therapeutic agent, such as enzyme replacement therapy or nanoparticle-mediated delivery. Despite challenges in protein folding and lysosomal targeting, ongoing studies aim to translate these insights into treatments for NPC and related lipid metabolism disorders.
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