
人 OSBPL11 抗体对
01AB01269
Oxysterol binding protein like 11 (OSBPL11) is a member of the oxysterol-binding protein (OSBP) family, which functions as intracellular lipid receptors. The OSBPL11 protein features an N-terminal pleckstrin homology domain and a conserved C-terminal OSBP-like sterol-binding domain, enabling it to bind sterols and regulate lipid metabolism. It plays a role in regulating adipocyte differentiation by modulating levels of ADIPOQ and FABP4 and is involved in the control of triglyceride storage in adipocytes. OSBPL11 localizes at the Golgi-late endosome interface, where it can dimerize with ORP9, suggesting a role in intracellular lipid trafficking. Disease associations include involvement in cholesterol and glucose metabolism, particularly in obese individuals, and links to splenic manifestations of leukemia.
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技术参数
- 靶点基因名
- OSBPL11
- 基因别名
- ORP11; OSBP12
- 蛋白别名
- oxysterol binding protein like 11; OSBPL11
- UniProt
- Q9BXB4
- 物种
- Human
产品详情
- 靶点名称
- OSBPL11
- 蛋白名称
- oxysterol binding protein like 11
- 蛋白别名
- Oxysterol-binding protein-related protein 11; ORP-11; OSBP-related protein 11
- 靶点基因名
- OSBPL11
- 基因别名
- ORP11; OSBP12
- UniProt
- Q9BXB4
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Oxysterol binding protein like 11 (OSBPL11) is a member of the oxysterol-binding protein (OSBP) family, which functions as intracellular lipid receptors. The OSBPL11 protein features an N-terminal pleckstrin homology domain and a conserved C-terminal OSBP-like sterol-binding domain, enabling it to bind sterols and regulate lipid metabolism. It plays a role in regulating adipocyte differentiation by modulating levels of ADIPOQ and FABP4 and is involved in the control of triglyceride storage in adipocytes. OSBPL11 localizes at the Golgi-late endosome interface, where it can dimerize with ORP9, suggesting a role in intracellular lipid trafficking. Disease associations include involvement in cholesterol and glucose metabolism, particularly in obese individuals, and links to splenic manifestations of leukemia.