| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OSBP |
| Uniprot No | P22059 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 324-407aa |
| 氨基酸序列 | GATVLPANTPGNVGSGKDQCCSGKGDMSDEDDENEFFDAPEIITMPENLG HKRTGSNISGASSDISLDEQYKHQLEETKKEKRT |
| 预测分子量 | 35 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OSBP(Oxysterol-binding Protein)重组蛋白的3篇代表性文献的简要列举：
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1. **标题**：Crystal structure of the yeast OSBP homolog Osh4 bound to a sterol derivative
**作者**：Im, Y.J., Raychaudhuri, S., Prinz, W.A., & Hurley, J.H.
**摘要**：该研究解析了酵母OSBP同源蛋白Osh4与胆固醇类似物复合物的晶体结构，揭示了OSBP通过疏水口袋结合固醇分子的机制，并提出了其在细胞内脂质运输中的构象变化模型。
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2. **标题**：Characterization of the sterol-binding domain of oxysterol-binding protein (OSBP)
**作者**：Lehto, M., Laitinen, S., Chinetti, G., et al.
**摘要**：通过重组表达OSBP的功能域，作者鉴定了其固醇结合的关键氨基酸残基，并证明OSBP的PH结构域和FFAT基序分别介导了细胞膜和内质网的靶向定位。
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3. **标题**：OSBP is a cholesterol-regulated scaffolding protein in control of ER-Golgi transport
**作者**：Ridgway, N.D., Zhao, K., & Prinz, W.A.
**摘要**：研究利用重组OSBP蛋白发现其通过胆固醇依赖的方式招募下游效应蛋白，调控内质网-高尔基体间的膜接触及脂质转运，揭示了OSBP在维持细胞胆固醇稳态中的作用。
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如需扩展，可补充OSBP与疾病相关的研究文献(如病毒利用OSBP机制的论文)。
**Background of OSBP Recombinant Protein**
Oxysterol-binding protein (OSBP), first identified in yeast, belongs to a conserved family of lipid-binding proteins involved in intracellular lipid transport, signaling, and membrane trafficking. OSBP and its homologs (OSBP-related proteins, ORPs) are characterized by a modular structure featuring an N-terminal pleckstrin homology (PH) domain for membrane anchoring, a central FFAT motif for endoplasmic reticulum (ER) interactions, and a C-terminal ligand-binding domain that recognizes oxysterols, cholesterol, and phospholipids. These structural elements enable OSBP to shuttle between the ER and Golgi apparatus, mediating non-vesicular lipid transfer and regulating cellular lipid homeostasis.
Recombinant OSBP proteins are engineered versions produced via heterologous expression systems (e.g., *E. coli*, mammalian cells) for functional and structural studies. Their production allows researchers to investigate OSBP’s role in cholesterol trafficking, sphingolipid metabolism, and its interplay with viral pathogens—notably, OSBP is exploited by certain viruses, including enteroviruses and SARS-CoV-2. to facilitate viral replication by hijacking lipid membranes.
Studies using recombinant OSBP have elucidated its dual function as a lipid sensor and transporter, as well as its involvement in diseases like atherosclerosis, cancer, and neurodegenerative disorders. Additionally, OSBP inhibitors are being explored as antiviral therapeutics. The development of high-purity, bioactive recombinant OSBP has been pivotal in screening such inhibitors and dissecting OSBP’s molecular mechanisms, underscoring its significance in both basic research and drug discovery.
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