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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]. De plus, nous expédions Oxysterol Binding Protein Anticorps (61) et Oxysterol Binding Protein Protéines (5) et beaucoup plus de produits pour cette protéine.
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Study identified an OSBP- and FAN (Montrer NSMAF Kits ELISA)-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 (Montrer IQGAP1 Kits ELISA) in mTORC1 signaling
These results suggest that poliovirus proteins modulate PI4KB (Montrer PI4KB Kits ELISA) 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 (Montrer PRKD1 Kits ELISA) negatively regulates HCV secretion/release by attenuating OSBP and CERT (Montrer COL4A3BP Kits ELISA) 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 (Montrer PRKD1 Kits ELISA) 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 (Montrer VAPA Kits ELISA).
OSBP opposes the activity of LXR (Montrer NR1H3 Kits ELISA) by negatively regulating ABCA1 (Montrer ABCA1 Kits ELISA) 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