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Oxysterol binding protein is an intracellular protein that is believed to transport sterols from lysosomes to the nucleus where the sterol down-regulates the genes for the LDL receptor, HMG-CoA reductase, and HMG synthetase [provided by RefSeq, Jul 2008]. Zusätzlich bieten wir Ihnen Oxysterol Binding Protein Antikörper (61) und Oxysterol Binding Protein Proteine (5) und viele weitere Produktgruppen zu diesem Protein an.
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Study identified an OSBP- and FAN (zeige NSMAF ELISA Kits)-mediated sterol requirement in Drosophila spermatogenesis
Cholesterol transfer, PI4P consumption, and control of membrane lipid order by endogenous OSBP have been described.
Data suggest that OSBP shifts the distribution of phosphatidylinositol 4-phosphate upon localization to endoplasmic reticulum-Golgi contact sites.
Our results identify OspB as a regulator of mTORC1 and mTORC1-dependent cell proliferation early during S. flexneri infection and establish a role for IQGAP1 (zeige IQGAP1 ELISA Kits) in mTORC1 signaling
These results suggest that poliovirus proteins modulate PI4KB (zeige PI4KB ELISA Kits) activity and provide PI4P for recruitment of OSBP to accumulate unesterified cholesterol on virus-induced membrane structure for formation of a virus replication complex.
OSBP-mediated back transfer of phosphatidylinositol 4-phosphate might coordinate the transfer of other lipid species at the endoplasmic reticulum-Golgi interface.
OSBP is required for efficient replication of intracellular S. Typhimurium.
Data indicate that phosphorylation on two serine-rich motifs, S381-S391 (site 1) and S192, S195, S200 (site 2), specifically controls oxysterol-binding protein (OSBP) activity at the endoplasmic reticulum (ER).
PKD (zeige PRKD1 ELISA Kits) negatively regulates HCV secretion/release by attenuating OSBP and CERT (zeige COL4A3BP ELISA Kits) functions by phosphorylation inhibition. This study identifies the key role of the Golgi components in the HCV maturation process.
Results identify a novel substrate of protein kinase D (zeige PRKD1 ELISA Kits) at the Golgi, the oxysterol-binding protein OSBP.
This review summarizes recent evidence of sterol transfer activity by OSBP, suggesting seemingly disparate functions that could be the result of alterations in membrane sterol distribution or ancillary to this primary activity.
Partitioning of Osbp between the endoplasmic reticulum and the Golgi apparatus is regulated by Vapa (zeige VAPA ELISA Kits).
OSBP opposes the activity of LXR (zeige NR1H3 ELISA Kits) by negatively regulating ABCA1 (zeige ABCA1 ELISA Kits) activity in the cytoplasm by sterol-binding domain-dependent protein destabilization
Oxysterol-binding protein is required for the perinuclear localization of intra-Golgi v-SNAREs.
Oxysterol binding protein is an intracellular protein that is believed to transport sterols from lysosomes to the nucleus where the sterol down-regulates the genes for the LDL receptor, HMG-CoA reductase, and HMG synthetase
, oxysterol binding protein
, oxysterol-binding protein
, oxysterol-binding protein 1