抗人 RABGAP1L 抗体对
01AB01321
Rab GTPase-activating protein 1-like (RABGAP1L) is a GTPase-activating protein (GAP) that specifically inactivates the small GTPase RAB22A by stimulating its GTP hydrolysis, converting RAB22A-GTP to the inactive RAB22A-GDP form. This activity regulates endocytosis and intracellular protein transport, particularly by modulating trafficking at phosphatidylinositol 3-phosphate (PI3P)-positive early endosomes. RABGAP1L is recruited by ankyrin-2 (ANK2) to these endosomes, facilitating the polarized recycling of fibronectin receptors (ITGA5/ITGB1) to the plasma membrane, which is essential for directional cell migration. Structurally, it contains Rab-GAP-TBC domains and PTB/PI domains, supporting its role in GTPase regulation and protein localization. Disease associations include involvement in cholesteatoma and intrahepatic cholangiocarcinoma, where dysregulation of RABGAP1L-mediated trafficking pathways may contribute to pathological cell migration and tumor progression.
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技术参数
- 靶点基因名
- RABGAP1L
- 基因别名
- HHL; KIAA0471
- 蛋白别名
- Rab GTPase-activating protein 1-like, isoform 10; RABGAP1L
- UniProt
- B7ZAP0
- 物种
- Human
产品详情
- 靶点名称
- RABGAP1L
- 蛋白名称
- Rab GTPase-activating protein 1-like, isoform 10
- 蛋白别名
- Rab GTPase-activating protein 1-like; isoform 10
- 靶点基因名
- RABGAP1L
- 基因别名
- HHL; KIAA0471
- UniProt
- B7ZAP0
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Rab GTPase-activating protein 1-like (RABGAP1L) is a GTPase-activating protein (GAP) that specifically inactivates the small GTPase RAB22A by stimulating its GTP hydrolysis, converting RAB22A-GTP to the inactive RAB22A-GDP form. This activity regulates endocytosis and intracellular protein transport, particularly by modulating trafficking at phosphatidylinositol 3-phosphate (PI3P)-positive early endosomes. RABGAP1L is recruited by ankyrin-2 (ANK2) to these endosomes, facilitating the polarized recycling of fibronectin receptors (ITGA5/ITGB1) to the plasma membrane, which is essential for directional cell migration. Structurally, it contains Rab-GAP-TBC domains and PTB/PI domains, supporting its role in GTPase regulation and protein localization. Disease associations include involvement in cholesteatoma and intrahepatic cholangiocarcinoma, where dysregulation of RABGAP1L-mediated trafficking pathways may contribute to pathological cell migration and tumor progression.