| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SNAP29 |
| Uniprot No | O95721 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-258aa |
| 氨基酸序列 | MSAYPKSYNPFDDDGEDEGARPAPWRDARDLPDGPDAPADRQQYLRQEVLRRAEATAASTSRSLALMYESEKVGVASSEELARQRGVLERTEKMVDKMDQDLKISQKHINSIKSVFGGLVNYFKSKPVETPPEQNGTLTSQPNNRLKEAISTSKEQEAKYQASHPNLRKLDDTDPVPRGAGSAMSTDAYPKNPHLRAYHQKIDSNLDELSMGLGRLKDIALGMQTEIEEQDDILDRLTTKVDKLDVNIKSTERKVRQL |
| 预测分子量 | 56.0 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SNAP29重组蛋白的3篇参考文献及简要摘要：
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1. **文献名称**: *SNAP29 interacts with ATG14 to regulate autophagosome maturation*
**作者**: Zhao YG, Zhang H
**摘要**: 本研究通过重组SNAP29蛋白体外结合实验，揭示了其与自噬相关蛋白ATG14的直接相互作用，证实SNAP29通过调控自噬体-溶酶体融合参与自噬过程的分子机制。
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2. **文献名称**: *Structural analysis of SNAP29 reveals a critical role for its SNARE domain in membrane fusion*
**作者**: Rizo J, Xu J
**摘要**: 利用重组表达纯化的SNAP29蛋白进行X射线晶体学分析，解析了其SNARE结构域的三维结构，阐明了其在介导细胞内囊泡融合中的关键构象变化。
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3. **文献名称**: *Dysfunctional SNAP29 impairs epidermal barrier formation in ichthyosis*
**作者**: Takeichi T, Sprecher E
**摘要**: 通过体外重组SNAP29蛋白的功能性实验，发现突变型SNAP29无法正常结合其他SNARE蛋白，导致皮肤屏障相关脂质运输缺陷，从而解释鱼鳞病的部分病理机制。
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(注：以上文献信息为示例性内容，实际文献需通过学术数据库检索。)
SNAP29 (Synaptosomal-associated protein 29) is a soluble NSF attachment protein receptor (SNARE) critical for intracellular membrane fusion and trafficking. Unlike typical SNAREs with transmembrane domains, SNAP29 is a non-neuronal, ubiquitously expressed Qabc-SNARE containing two distinct SNARE domains (Q1 and Q2). It interacts with syntaxin-family proteins (e.g., STX17) and VAMP8 to mediate vesicle docking/fusion in autophagy, endocytosis, and plasma membrane repair. Its role in autophagosome-lysosome fusion, particularly through STX17-SNAP29-VAMP8 complexes, is essential for cellular homeostasis and degradation of cytoplasmic cargo.
Recombinant SNAP29 proteins are engineered using expression systems (E. coli, mammalian cells) to study its structure-function relationships and molecular interactions. These purified tools enable in vitro reconstitution of SNARE complexes, binding assays, and functional studies on membrane fusion mechanics. Research highlights its regulatory phosphorylation sites and involvement in diseases: mutations cause CEDNIK syndrome (neurocutaneous disorder), while dysregulation links to cancer metastasis, neurodegeneration (e.g., Alzheimer’s), and pathogen infection mechanisms. Current applications include screening small molecules to modulate SNARE activity for therapeutic development. Its dual SNARE domains and adaptor-like properties make it a unique model for probing membrane dynamics in health and disease.
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