人 SNAP23 抗体对
01AB01844
Synaptosome associated protein 23 (SNAP23) is a ubiquitously expressed Qbc-SNARE protein that serves as the primary non-neuronal homolog of SNAP25. It is anchored to the plasma membrane and intracellular membranes via a palmitoylated cysteine-rich region. SNAP23 forms ternary SNARE complexes with syntaxins and VAMP proteins to mediate regulated vesicle docking and fusion. This mechanism is essential for diverse cellular processes, including exocytosis, endomembrane trafficking, GLUT4 translocation, and exosome release. Pathophysiologically, SNAP23 is involved in several disease processes; it promotes cancer progression by facilitating the delivery of matrix metalloproteinases and exosome secretion. It also modulates inflammatory responses through regulated degranulation in immune cells and influences thrombosis by mediating the exocytosis of von Willebrand factor from endothelial cells.
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技术参数
- 靶点基因名
- SNAP23
- 蛋白别名
- synaptosome associated protein 23; SNAP23
- UniProt
- O00161
- 物种
- Human
产品详情
- 靶点名称
- SNAP23
- 蛋白名称
- synaptosome associated protein 23
- 蛋白别名
- Synaptosomal-associated protein 23; SNAP-23; Vesicle-membrane fusion protein SNAP-23
- 靶点基因名
- SNAP23
- UniProt
- O00161
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Synaptosome associated protein 23 (SNAP23) is a ubiquitously expressed Qbc-SNARE protein that serves as the primary non-neuronal homolog of SNAP25. It is anchored to the plasma membrane and intracellular membranes via a palmitoylated cysteine-rich region. SNAP23 forms ternary SNARE complexes with syntaxins and VAMP proteins to mediate regulated vesicle docking and fusion. This mechanism is essential for diverse cellular processes, including exocytosis, endomembrane trafficking, GLUT4 translocation, and exosome release. Pathophysiologically, SNAP23 is involved in several disease processes; it promotes cancer progression by facilitating the delivery of matrix metalloproteinases and exosome secretion. It also modulates inflammatory responses through regulated degranulation in immune cells and influences thrombosis by mediating the exocytosis of von Willebrand factor from endothelial cells.