人 SEC24C 抗体对
01AB02284
SEC24 homolog C, COPII component (SEC24C) is a core component of the COPII coat machinery that mediates vesicle formation and selective cargo export from the endoplasmic reticulum (ER) to the Golgi apparatus. It forms a heterodimer with SEC23 and provides specialized cargo-recognition sites for IxM-motif-containing SNAREs and GPI-anchored proteins. SEC24C is essential for neuronal homeostasis; its deficiency leads to ER distension, activation of the unfolded protein response, and neuronal stress. Clinically, SEC24C has been identified as a critical host dependency factor for HIV-1 replication. It binds and stabilizes the HIV-1 capsid lattice via its FG motif, facilitating early post-entry steps of the viral life cycle. Consequently, disruption of SEC24C significantly impairs viral infection, making it a potential therapeutic target.
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技术参数
- 靶点基因名
- SEC24C
- 基因别名
- KIAA0079
- 蛋白别名
- SEC24 homolog C, COPII component; SEC24C
- UniProt
- P53992
- 物种
- Human
产品详情
- 靶点名称
- SEC24C
- 蛋白名称
- SEC24 homolog C, COPII component
- 蛋白别名
- Protein transport protein Sec24C; SEC24-related protein C);SEC24 homolog C; COPII coat complex component
- 靶点基因名
- SEC24C
- 基因别名
- KIAA0079
- UniProt
- P53992
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
SEC24 homolog C, COPII component (SEC24C) is a core component of the COPII coat machinery that mediates vesicle formation and selective cargo export from the endoplasmic reticulum (ER) to the Golgi apparatus. It forms a heterodimer with SEC23 and provides specialized cargo-recognition sites for IxM-motif-containing SNAREs and GPI-anchored proteins. SEC24C is essential for neuronal homeostasis; its deficiency leads to ER distension, activation of the unfolded protein response, and neuronal stress. Clinically, SEC24C has been identified as a critical host dependency factor for HIV-1 replication. It binds and stabilizes the HIV-1 capsid lattice via its FG motif, facilitating early post-entry steps of the viral life cycle. Consequently, disruption of SEC24C significantly impairs viral infection, making it a potential therapeutic target.