人 ATG3 抗体对
01AB00455
Autophagy related 3 (ATG3) is a ubiquitin-like-conjugating enzyme essential for autophagy, a cellular degradation process. ATG3 catalyzes the conjugation of Atg8/LC3 to phosphatidylethanolamine, crucial for autophagosome formation. It contains an N-terminal domain, a catalytic domain with an active-site cysteine, and a C-terminal domain with a conserved FLKF motif. ATG3 interacts with ATG7 and ATG12-ATG5 complexes to facilitate LC3 lipidation. It also functions as a membrane curvature sensor, promoting LC3/GABARAP lipidation in areas of membrane stress. In disease contexts, ATG3 has been implicated in cancer progression, with its overexpression observed in human osteosarcoma cells enhancing autophagy. Additionally, ATG3 plays a role in neurodegenerative diseases, where its regulation of autophagy contributes to the degradation of accumulated proteins.
| 规格 | 起售价 |
|---|---|
| 登录后可查看 | |
技术参数
- 靶点基因名
- ATG3
- 基因别名
- APG3; APG3L
- 蛋白别名
- autophagy related 3; ATG3
- UniProt
- Q9NT62
- 物种
- Human
产品详情
- 靶点名称
- ATG3
- 蛋白名称
- autophagy related 3
- 蛋白别名
- Ubiquitin-like-conjugating enzyme ATG3; Autophagy-related protein 3; APG3-like; hApg3; Protein PC3-96
- 靶点基因名
- ATG3
- 基因别名
- APG3; APG3L
- UniProt
- Q9NT62
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Autophagy related 3 (ATG3) is a ubiquitin-like-conjugating enzyme essential for autophagy, a cellular degradation process. ATG3 catalyzes the conjugation of Atg8/LC3 to phosphatidylethanolamine, crucial for autophagosome formation. It contains an N-terminal domain, a catalytic domain with an active-site cysteine, and a C-terminal domain with a conserved FLKF motif. ATG3 interacts with ATG7 and ATG12-ATG5 complexes to facilitate LC3 lipidation. It also functions as a membrane curvature sensor, promoting LC3/GABARAP lipidation in areas of membrane stress. In disease contexts, ATG3 has been implicated in cancer progression, with its overexpression observed in human osteosarcoma cells enhancing autophagy. Additionally, ATG3 plays a role in neurodegenerative diseases, where its regulation of autophagy contributes to the degradation of accumulated proteins.