Anti-Human OSBPL11 Antibody Pair

Product Description: 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. Protein Function: Plays a role in regulating ADIPOQ and FABP4 levels in differentiating adipocytes and is also involved in regulation of adipocyte triglyceride storage (PubMed:23028956). Weakly binds 25-hydroxycholesterol (PubMed:17428193). Interacts with OSBPL9 to function as lipid transfer proteins (PubMed:39106189). Together they form a heterodimer that localizes at the ER-trans-Golgi membrane contact sites, and exchanges phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine, PS) for phosphatidylinositol-4-phosphate (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate), PI(4)P) between the two organelles, a step that is critical for sphingomyelin synthesis in the Golgi complex (PubMed:39106189) [The Uniprot Consortium]