| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VAMP8 |
| Uniprot No | Q9BV40 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-100aa |
| 氨基酸序列 | MEEASEGGGNDRVRNLQSEVEGVKNIMTQNVERILARGENLEHLRNKTEDLEATSEHFKTTSQKVARKFWWKNVKMIVLICVIVFIIILFIVLFATGAFS |
| 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VAMP8重组蛋白的3篇参考文献示例(文献信息为模拟概括，非真实存在)：
1. **文献名称**：*VAMP8重组蛋白在血小板分泌中的功能研究*
**作者**：Duan, X. et al.
**摘要**：该研究通过表达纯化VAMP8重组蛋白，结合体外囊泡融合实验，揭示了其在血小板颗粒分泌中的关键调控作用，并证明其与特定SNARE复合物的相互作用。
2. **文献名称**：*重组VAMP8的结构解析及其与Syntaxin7的互作机制*
**作者**：Fasshauer, D. & Bruns, D.
**摘要**：利用重组VAMP8蛋白进行X射线晶体学分析，阐明了其螺旋结构域与Syntaxin7的结合位点，为溶酶体膜融合的分子机制提供结构基础。
3. **文献名称**：*VAMP8重组蛋白在自噬体-溶酶体融合中的动态调控*
**作者**：Zhao, Y.G. et al.
**摘要**：通过体外重建实验证明，重组VAMP8蛋白可与HOPS复合体协同介导自噬体与溶酶体的膜融合，并揭示磷酸化修饰对其功能的调节。
(注：以上文献为示例性概括，实际文献需通过PubMed/Google Scholar等平台以关键词“VAMP8 recombinant protein”或“VAMP8 ectopic expression”检索。)
**Background of VAMP8 Recombinant Protein**
VAMP8 (vesicle-associated membrane protein 8), also known as endobrevin, is a member of the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family. It plays a critical role in intracellular membrane fusion events, particularly in secretory pathways and lysosome-related processes. As an R-SNARE protein, VAMP8 mediates the docking and fusion of vesicles with target membranes by forming a stable SNARE complex with Q-SNARE partners like syntaxin and SNAP-25. This interaction is essential for processes such as endocytosis, autophagy, and the release of secretory granules in platelets and other cell types.
Structurally, VAMP8 contains a conserved SNARE domain, a transmembrane region, and short N- and C-terminal tails. Its involvement in lysosomal fusion and endosomal trafficking highlights its importance in maintaining cellular homeostasis. Dysregulation of VAMP8 has been linked to pathologies, including cancer, neurodegenerative disorders, and immune dysfunctions, making it a target for therapeutic research.
Recombinant VAMP8 protein is produced using heterologous expression systems (e.g., *E. coli* or mammalian cell lines) to study its biochemical interactions, structural features, and functional mechanisms *in vitro*. Purified recombinant VAMP8 enables researchers to investigate SNARE complex assembly, membrane fusion kinetics, and the impact of mutations or inhibitors. It is also utilized in drug discovery to screen molecules that modulate vesicle trafficking, potentially addressing diseases with impaired membrane dynamics.
Overall, VAMP8 recombinant protein serves as a vital tool for dissecting the molecular basis of intracellular transport and developing strategies to target SNARE-mediated processes in human health and disease.
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