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OSBPL1A encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. De plus, nous expédions Oxysterol Binding Protein-Like 1A Anticorps (70) et et beaucoup plus de produits pour cette protéine.
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ORP1L, via its liganding by lipids and the formation of contacts between autophagic vacuoles and the endoplasmic reticulum, governs the last steps in autophagy that lead to the lysosomal degradation of cytosolic material.
This study validated that rs3746444 polymorphism influenced the expression of miR499a, its target gene, osbpl1a, and thereby associated with the HDL level, which makes it a potential factor involved in the mechanism of atherosclerosis.
ORP1L-dependent membrane contacts between late endosomes/lysosomes and the endoplasmic reticulum coordinate cholesterol transfer with the retrograde movement of endo-lysosomal vesicles.
a familial loss-of-function mutation in OSBPL1A affects the first step of the reverse cholesterol transport process and associates with a low HDL-C phenotype
These data suggest that ORP1L is specifically recruited by the bacteria to the Coxiella parasitophorous vacuole, where it influences parasitophorous vacuole membrane dynamics and interactions with the endoplasmic reticulum.
ORP1L-VAP 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, which has a central role in adenovirus pathogenesis and is known to be tightly regulated by cholesterol-rich "lipid rafts."
Data suggest RIDalpha as a model system for understanding physiological egress routes that use ORP1L to activate endosome-to-endoplasmic reticulum (ER) feedback responses involved in lipid droplets (LDs)formation.
ORP1S is a cytoplasmic sterol sensor, which transports sterols to the nucleus and promotes LXR regulated trans-activation of apoE.
The study shows that OSBPL1A binds several oxysterols and cholesterol, and characterize a mutant, OSBPL1A Delta560-563, defective in oxysterol binding.
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, 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 to control Rab7-RILP-p150 Glued 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.
OSBP regulates hepatic TG metabolism and suggest the involvement of OSBP in the insulin 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