纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | STX17 |
Uniprot No | P56962 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-229aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMSEDEEK VKLRRLEPAI QKFIKIVIPT DLERLRKHQI NIEKYQRCRI WDKLHEEHIN AGRTVQQLRS NIREIEKLCL KVRKDDLVLL KRMIDPVKEE ASAATAEFLQ LHLESVEELK KQFNDEETLL QPPLTRSMTV GGAFHTTEAE ASSQSLTQIY ALPEIPQDQN AAESWETLEA DLIELSQLVT DFSLLVNSQQ EKIDSIADHV NSAAVNVEEG TKNLGKAAKY KL |
预测分子量 | 29 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STX17重组蛋白的3篇代表性文献示例(注:文献信息为假设性概括,建议通过数据库核实具体内容):
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1. **文献名称**: *STX17 mediates the fusion of autophagosomes with lysosomes*
**作者**: Tamura, N. et al.
**摘要**: 本研究利用重组STX17蛋白,揭示了其在自噬体-溶酶体融合中的关键作用。实验表明,STX17通过C端跨膜结构域锚定在自噬体膜上,并与SNAP29/VAMP8形成SNARE复合物,调控自噬通量的完成。重组STX17的体外实验进一步验证了其与LC3蛋白的相互作用机制。
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2. **文献名称**: *Recombinant STX17 facilitates membrane repair via ESCRT pathway*
**作者**: Zhang, Y. et al.
**摘要**: 通过表达纯化STX17重组蛋白,研究者发现STX17在细胞膜损伤修复中与ESCRT-III复合物协作。体外膜重组实验显示,STX17通过促进膜曲率形成和脂质重塑,增强细胞对机械应激的耐受性,为治疗膜损伤相关疾病提供新靶点。
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3. **文献名称**: *Structural insights into STX17 function in mitochondrial dynamics*
**作者**: Nakamura, S. et al.
**摘要**: 本研究解析了重组STX17蛋白的晶体结构,发现其N端结构域与线粒体分裂蛋白DRP1特异性结合。功能实验表明,STX17通过调控线粒体膜融合-分裂平衡影响细胞代谢,为线粒体疾病机制研究提供了分子基础。
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**提示**:以上内容为模拟概括,实际文献需通过PubMed、Google Scholar等平台以“STX17 recombinant protein”或“Syntaxin 17”为关键词检索。近年研究多聚焦于STX17在自噬、细胞器动态及癌症中的功能,建议结合具体研究方向筛选文献。
**Background of STX17 Recombinant Protein**
Syntaxin 17 (STX17), a member of the SNARE protein family, plays a critical role in intracellular membrane fusion events, particularly in autophagy and organelle dynamics. It is a transmembrane protein localized to the endoplasmic reticulum (ER), Golgi apparatus, and autophagosomal membranes. STX17 gained prominence for its essential function in autophagosome-lysosome fusion, a key step in autophagy. During this process, STX17 partners with SNAP29 and VAMP8 to form a ternary SNARE complex, mediating membrane docking and fusion. Its unique C-terminal hairpin-like transmembrane domain enables selective recruitment to mature autophagosomes, ensuring spatial and temporal regulation of autophagy.
Beyond autophagy, STX17 is implicated in mitochondrial dynamics, lipid droplet metabolism, and secretory pathways. Dysregulation of STX17 has been linked to neurodegenerative diseases, cancer, and metabolic disorders, underscoring its therapeutic relevance.
Recombinant STX17 protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cells) to produce purified, functional protein for *in vitro* studies. This tool enables researchers to dissect STX17’s structural domains, binding partners, and biochemical mechanisms. Applications include studying SNARE complex assembly, screening autophagy-modulating compounds, and exploring disease-related mutations. Its availability accelerates drug discovery and mechanistic insights into membrane trafficking disorders.
Recent studies also highlight STX17’s role in unconventional secretion and cellular stress responses, broadening its biological significance. As research advances, STX17 recombinant protein remains vital for unraveling its multifaceted roles in cellular homeostasis and pathology.
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