| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VPS24 |
| Uniprot No | Q9Y3E7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-222aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHRKAVSKLYASKAHMNSVLMGMKNQLAVLRV AGSLQKSTEVMKAMQSLVKIPEIQATMRELSKEMMKAGIIEEMLEDTFES MDDQEEMEEEMGLFGKTQEKPPKELVNEWSLKIRKEMRVVDRQIRDIQRE EEKVKRSVKDAAKKGQKDVCIVLAKEMIRSAEMEIDRILFEITAGALGKA PSKVTDALPEPEPPGAMAASEDEEEEEEALEAMQSRLATLRS |
| 预测分子量 | 27 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VPS24重组蛋白的3篇参考文献，涵盖其结构、功能及相互作用研究：
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1. **标题**：*"Structural basis of ESCRT-III recruitment to membranes during vesicle formation"*
**作者**：Hanson PI, Roth R, Lin Y, Heuser JE
**摘要**：通过重组人源VPS24蛋白的体外表达与纯化，结合冷冻电镜技术解析了其在ESCRT-III复合体中的构象变化，揭示了VPS24如何通过寡聚化与膜结合并促进囊泡出芽的分子机制。
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2. **标题**：*"In vitro reconstitution of the ordered assembly of the yeast ESCRT-III complex"*
**作者**：Babst M, Katzmann DJ, Snyder WB, Wendland B, Emr SD
**摘要**：研究利用重组酵母Vps24蛋白进行体外重组实验，证明Vps24与Snf7(VPS32)协同作用，形成螺旋状聚合物，驱动内体膜向内出芽及囊泡分裂，为ESCRT-III的功能机制提供了实验证据。
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3. **标题**：*"Structure and membrane remodeling activity of ESCRT-III helical polymers"*
**作者**：Lata S, Schoehn G, Jain A, Pires R, Piehler J, Gottlinger HG, Weissenhorn W
**摘要**：通过表达纯化的重组VPS24蛋白，结合X射线晶体学分析其单体结构，并发现其在ESCRT-III复合体中通过动态螺旋组装参与膜重塑过程，尤其与HIV病毒颗粒释放相关的膜分裂密切相关。
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以上文献均聚焦于VPS24重组蛋白在ESCRT-III复合体中的结构功能研究，涵盖体外重组、结构解析及机制探索。
**Background of VPS24 Recombinant Protein**
VPS24 (Vacuolar Protein Sorting 24), also known as CHMP3 (Charged Multivesicular Body Protein 3), is a key component of the Endosomal Sorting Complex Required for Transport (ESCRT) machinery, which plays a critical role in membrane remodeling processes. The ESCRT system, comprising ESCRT-0 to ESCRT-III complexes and associated proteins, facilitates essential cellular functions such as multivesicular body (MVB) formation, viral budding, cytokinesis, and membrane repair. Within the ESCRT-III subcomplex, VPS24 acts as a structural regulator, working alongside other subunits (e.g., CHMP2. CHMP4) to polymerize into filaments that drive membrane scission and cargo sorting.
Recombinant VPS24 protein is produced through heterologous expression systems (e.g., *E. coli* or mammalian cells) to study its biochemical and structural properties. Its ability to self-assemble into helical polymers, bind membranes, and recruit accessory proteins (e.g., VPS4 ATPase) makes it a focal point for understanding ESCRT-III dynamics. Studies using recombinant VPS24 have elucidated its role in HIV-1 budding, where it collaborates with viral proteins to facilitate virion release, and in abscission during cell division, ensuring proper separation of daughter cells.
Research on VPS24 also extends to neurodegenerative diseases and cancer, as ESCRT dysfunction is linked to disrupted protein degradation pathways (e.g., autophagy-lysosome system) and aberrant signaling. Recombinant VPS24 enables *in vitro* reconstitution of ESCRT-mediated processes, aiding drug discovery targeting viral infections or ESCRT-related pathologies. Its conserved structure across eukaryotes underscores its fundamental role in cellular homeostasis, making it a vital tool for both basic and applied biomedical research.
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