Anti-OSBPL9 antibody [EPR9333]

Supplementary info

Activity summary

OSBPL9 also referred to as oxysterol-binding protein-like 9 is a member of the oxysterol-binding protein (OSBP)-related protein family. This protein family involves intracellular lipid transport. OSBPL9 has a molecular weight of approximately 89 kDa. It is expressed in various tissues with high levels in brain pancreas and intestine. The protein possesses a pleckstrin homology domain and a conserved OSBP-related domain which play roles in binding to lipids and facilitating their transport within cells.

Biological function summary

OSBPL9 participates in lipid metabolism and cellular lipid homeostasis. It binds to phosphoinositides and sterols regulating lipid distribution and signaling. Studies indicate that OSBPL9 forms part of a complex involved in the transfer of lipids at the membrane contact sites between organelles such as the endoplasmic reticulum and the Golgi apparatus. These interactions highlight its integral role in maintaining lipid equilibrium across cellular compartments.

Pathways

A deeper understanding of OSBPL9 shows its involvement in signaling pathways alongside other lipid-binding proteins. It plays a significant role within the sterol regulatory element-binding protein (SREBP) signaling pathway and potentially the PI3K-Akt signaling pathway. These pathways are essential in lipid synthesis and cellular growth. OSBPL9 shares functional interactions with proteins like OSBP and other OSBP-related proteins emphasizing its collaborative involvement in these pathways.

Associated diseases and disorders

OSBPL9 association with dyslipidemia and metabolic disorders has been observed due to its influence on lipid homeostasis. Alterations in OSBPL9 function may contribute to abnormal lipid levels impacting conditions like atherosclerosis. The protein's connection to metabolic pathways suggests a linkage with proteins such as OSBPL10 further indicating its potential involvement in the pathogenesis of these metabolic disorders. Researchers continue to study OSBPL9 to better understand its role in these diseases.