
抗人 SNX11 抗体对
01AB02766
Sorting nexin 11 (SNX11) is a phosphoinositide-binding protein characterized by a unique extended PX (PXe) domain, which includes additional α-helices essential for its function in intracellular endosomal trafficking and protein sorting. This PX domain specifically binds to phosphatidylinositols found in organelle membranes, facilitating SNX11's recruitment to vesicles and its involvement in membrane trafficking pathways. Structurally, the PXe domain differentiates SNX11 from other sorting nexins by its novel two α-helices at the C-terminus, crucial for modulating vacuolation activity and protein interactions. Functionally, SNX11 assists in trafficking proteins such as the TRPV3 ion channel to lysosomes for degradation, thus playing roles in lysosomal degradation pathways and maintaining protein homeostasis within cells. Its regulatory role in membrane trafficking suggests potential links to neurological and cellular trafficking disorders through disrupted protein sorting and degradation mechanisms.
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|---|---|
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技术参数
- 靶点基因名
- SNX11
- 蛋白别名
- sorting nexin 11; SNX11
- UniProt
- Q9Y5W9
- 物种
- Human
产品详情
- 靶点名称
- SNX11
- 蛋白名称
- sorting nexin 11
- 蛋白别名
- Sorting nexin-11
- 靶点基因名
- SNX11
- UniProt
- Q9Y5W9
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Sorting nexin 11 (SNX11) is a phosphoinositide-binding protein characterized by a unique extended PX (PXe) domain, which includes additional α-helices essential for its function in intracellular endosomal trafficking and protein sorting. This PX domain specifically binds to phosphatidylinositols found in organelle membranes, facilitating SNX11's recruitment to vesicles and its involvement in membrane trafficking pathways. Structurally, the PXe domain differentiates SNX11 from other sorting nexins by its novel two α-helices at the C-terminus, crucial for modulating vacuolation activity and protein interactions. Functionally, SNX11 assists in trafficking proteins such as the TRPV3 ion channel to lysosomes for degradation, thus playing roles in lysosomal degradation pathways and maintaining protein homeostasis within cells. Its regulatory role in membrane trafficking suggests potential links to neurological and cellular trafficking disorders through disrupted protein sorting and degradation mechanisms.