| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VAMP5 |
| Uniprot No | O95183 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-116aa |
| 氨基酸序列 | MAGIELERCQQQANEVTEIMRNNFGKVLERGVKLAELQQRSDQLLDMSSTFNKTTQNLAQKKCWENIRYRICVGLVVVGVLLIILIVLLVVFLPQSSDSSSAPRTQDAGIASGPGN |
| 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VAMP5重组蛋白的3篇示例参考文献(注：以下内容为虚构示例，实际文献需通过学术数据库查询)：
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1. **文献名称**: *"Recombinant VAMP5 Expression and Its Role in SNARE-Mediated Membrane Fusion"*
**作者**: Müller A, et al.
**摘要**: 研究通过原核系统表达并纯化重组VAMP5蛋白，验证其与Syntaxin-4和SNAP-23形成功能性SNARE复合体的能力，揭示了VAMP5在非神经元细胞膜融合中的作用机制。
2. **文献名称**: *"Structural Characterization of Recombinant VAMP5 Using Cryo-Electron Microscopy"*
**作者**: Chen H, et al.
**摘要**: 利用冷冻电镜解析重组VAMP5的分子结构，发现其N端结构域对靶膜锚定至关重要，为理解其与疾病相关突变的功能异常提供了结构基础。
3. **文献名称**: *"VAMP5 Knockdown and Recombinant Rescue in Epithelial Cell Polarization"*
**作者**: Gupta R, et al.
**摘要**: 通过重组VAMP5蛋白回补实验，证明VAMP5在细胞极性建立中调控囊泡运输的关键作用，并发现其与Rab11的协同功能。
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如需真实文献，建议通过PubMed或Google Scholar检索关键词“VAMP5 recombinant protein”或“VAMP5 SNARE function”获取最新研究。
**Background of VAMP5 Recombinant Protein**
VAMP5 (Vesicle-Associated Membrane Protein 5), a member of the VAMP/synaptobrevin family, is a key player in intracellular membrane fusion processes. These proteins are integral to SNARE (Soluble NSF Attachment Protein Receptor) complexes, which mediate vesicle trafficking and fusion with target membranes. Unlike its neuronal homologs VAMP1/2. VAMP5 is broadly expressed in non-neuronal tissues, including endothelial cells, smooth muscle, and secretory epithelia, suggesting roles in constitutive exocytosis and cellular homeostasis.
Structurally, VAMP5 contains a conserved SNARE motif and a transmembrane domain, enabling its interaction with syntaxin and SNAP-25 homologs to drive membrane fusion. Its unique N-terminal extension may regulate compartment-specific trafficking. Dysregulation of VAMP5 has been linked to pathological conditions, such as cardiovascular diseases and cancer metastasis, highlighting its biomedical relevance.
Recombinant VAMP5 proteins are engineered for research applications, typically produced in *E. coli* or mammalian expression systems. These proteins retain functional domains and are often tagged (e.g., His, GST) for purification and detection. They serve as critical tools for studying SNARE assembly kinetics, membrane fusion mechanisms, and intracellular transport pathways. Additionally, recombinant VAMP5 aids in screening therapeutic agents targeting exocytosis-related disorders.
In summary, VAMP5 recombinant protein bridges fundamental cell biology with translational research, offering insights into vesicle dynamics and potential therapeutic strategies. Its production and application continue to advance our understanding of cellular communication and disease mechanisms.
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