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OSBPL1A encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Zusätzlich bieten wir Ihnen Oxysterol Binding Protein-Like 1A Antikörper (69) und und viele weitere Produktgruppen zu diesem Protein an.
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This study validated that rs3746444 polymorphism influenced the expression of miR499a, its target gene, osbpl1a, and thereby associated with the HDL (zeige HSD11B1 Proteine) level, which makes it a potential factor involved in the mechanism of atherosclerosis.
a familial loss-of-function mutation in OSBPL1A affects the first step of the reverse cholesterol transport process and associates with a low HDL (zeige HSD11B1 Proteine)-C phenotype
ORP1L-VAP (zeige F10 Proteine) 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 (zeige TLR4 Proteine), 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 (zeige NR1H3 Proteine) regulated trans-activation of apoE (zeige APOE Proteine).
The study shows that OSBPL1A binds several oxysterols and cholesterol, and characterize a mutant, OSBPL1A Delta560-563, defective in oxysterol bi (zeige APOA1 Proteine)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 (zeige RAB7B Proteine), 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 (zeige F10 Proteine) to control Rab7 (zeige RAB7B Proteine)-RILP (zeige RILP Proteine)-p150 Glued (zeige DCTN1 Proteine) 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 (zeige APOA1 Proteine).
OSBP (zeige OSBP Proteine) regulates hepatic TG metabolism and suggest the involvement of OSBP (zeige OSBP Proteine) in the insulin (zeige INS Proteine) 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