| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VAMP2 |
| Uniprot No | P63027 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-89aa |
| 氨基酸序列 | MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMSA TAATAPPAAP AGEGGPPAPP PNLTSNRRLQ QTQAQVDEVV DIMRVNVDKV LERDQKLSEL DDRADALQAG ASQFETSAAK LKRKYW |
| 预测分子量 | 14 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VAMP2重组蛋白的3篇示例参考文献(内容为模拟概括，仅供参考)：
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1. **文献名称**: "Recombinant VAMP2 purification and functional reconstitution in synaptic vesicle fusion"
**作者**: Südhof TC, et al.
**摘要**: 研究通过大肠杆菌表达系统纯化重组VAMP2蛋白，并利用体外脂质体融合实验验证其与Syntaxin-1A和SNAP-25的相互作用，证明其在SNARE复合体形成中的关键作用。
2. **文献名称**: "Structural analysis of the VAMP2 SNARE motif using recombinant protein crystallography"
**作者**: Sutton RB, et al.
**摘要**: 通过重组VAMP2蛋白的结晶和X射线衍射技术，解析其SNARE结构域的三维结构，揭示了螺旋化过程中关键氨基酸残基的构象变化。
3. **文献名称**: "In vitro reconstitution of VAMP2-mediated neurotransmitter release"
**作者**: Jahn R, et al.
**摘要**: 利用重组VAMP2蛋白与人工膜系统模拟突触囊泡融合过程，证实VAMP2在钙离子触发的神经递质释放中不可或缺。
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如需真实文献，建议通过PubMed、Google Scholar等平台检索关键词：
`VAMP2 recombinant protein expression`、`VAMP2 SNARE complex structure`、`VAMP2 in vitro fusion assay`。
**Background of VAMP2 Recombinant Protein**
Vesicle-associated membrane protein 2 (VAMP2), also known as synaptobrevin-2. is a key component of the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) family, which mediates intracellular membrane fusion events. Predominantly expressed in neurons, VAMP2 resides on synaptic vesicles and plays a critical role in neurotransmitter release by facilitating the fusion of these vesicles with the presynaptic membrane. It interacts with target membrane SNARE proteins (syntaxin-1 and SNAP-25) to form a stable SNARE complex, a process essential for exocytosis.
The interest in VAMP2 extends to its involvement in neurological disorders. Mutations or dysregulation of VAMP2 have been linked to neurodevelopmental conditions, epilepsy, and neurodegenerative diseases. Additionally, VAMP2 is a target for clostridial neurotoxins (e.g., botulinum and tetanus toxins), which cleave SNARE proteins to inhibit neurotransmission, underscoring its functional significance.
Recombinant VAMP2 protein is engineered through heterologous expression systems (e.g., *E. coli* or mammalian cells) to produce purified, functional forms of the protein for research. This tool enables studies on SNARE complex assembly, membrane fusion mechanisms, and synaptic transmission. It also aids in drug discovery, toxin research, and diagnostic assays. By providing a controlled source of VAMP2. recombinant versions help dissect its structural domains (e.g., the SNARE motif and transmembrane region) and post-translational modifications, advancing our understanding of synaptic biology and disease pathology.
In summary, VAMP2 recombinant protein serves as a vital resource for exploring fundamental neurobiological processes and developing therapeutic strategies for synaptic dysfunction-related disorders.
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