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OSBPL1A encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Additionally we are shipping Oxysterol Binding Protein-Like 1A Antibodies (68) and many more products for this protein.
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a familial loss-of-function mutation in OSBPL1A affects the first step of the reverse cholesterol transport process and associates with a low HDL (show HSD11B1 Proteins)-C phenotype
ORP1L-VAP (show F10 Proteins) complexes also support transport of LDL-derived cholesterol from endosomes to the endoplasmic reticulum when ORP1L was bound to human adenovirus RIDalpha. RIDalpha-induced lipid trafficking also attenuated proinflammatory signaling by Toll-like receptor 4 (show TLR4 Proteins), which has a central role in adenovirus pathogenesis and is known to be tightly regulated by cholesterol-rich "lipid rafts."
ORP1S is a cytoplasmic sterol sensor, which transports sterols to the nucleus and promotes LXR (show NR1H3 Proteins) regulated trans-activation of apoE (show APOE Proteins).
The study shows that OSBPL1A binds several oxysterols and cholesterol, and characterize a mutant, OSBPL1A Delta560-563, defective in oxysterol bi (show APOA1 Proteins)nding.
Results suggest that the two forms of oxysterol binding protein-related protein-1 (ORP1) are functionally distinct and that ORP1L is involved in control of cellular lipid metabolism
binds to Rab7 (show RAB7B Proteins), modifies its functional cycle, and can interfere with lysosome organization and endocytic membrane trafficking.
OSBPL1A was preferentially expressed from the maternal allele
Results describe how ORP1L contacts VAP (show F10 Proteins) to control Rab7 (show RAB7B Proteins)-RILP (show RILP Proteins)-p150 Glued (show DCTN1 Proteins) and late endosome positioning.
Osbpl1a silencing in macrophage foam cells enhances endosome motility and results in inhibition of [(3)H]cholesterol efflux to apolipoprotein A-I (show APOA1 Proteins).
OSBP (show OSBP Proteins) regulates hepatic TG metabolism and suggest the involvement of OSBP (show OSBP Proteins) in the insulin (show INS Proteins) signaling pathways that control hepatic lipogenesis.
This gene encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Most members contain an N-terminal pleckstrin homology domain and a highly conserved C-terminal OSBP-like sterol-binding domain, although some members contain only the sterol-binding domain. Transcript variants derived from alternative promoter usage and/or alternative splicing exist\; they encode different isoforms.
OSBP-related protein 1
, oxysterol binding protein-like 1B
, oxysterol-binding protein-related protein 1
, oxysterol-binding protein-related protein 1 variant 1
, oxysterol-binding protein-related protein 1 variant 2
, oxysterol-binding protein-like 1A
, oxysterol binding protein-like 1A
, oxysterol binding protein-like protein 1A
, oxysterol-binding protein-related protein 1-like