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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].. Additionally we are shipping Oxysterol Binding Protein Antibodies (59) and Oxysterol Binding Protein Kits (2) and many more products for this protein.
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Study identified an OSBP- and FAN (show NSMAF Proteins)-mediated sterol requirement in Drosophila spermatogenesis
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 in mTORC1 signaling
These results suggest that poliovirus proteins modulate PI4KB (show PI4KB Proteins) 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 (show PRKD1 Proteins) negatively regulates HCV secretion/release by attenuating OSBP and CERT (show COL4A3BP Proteins) 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 (show PRKD1 Proteins) 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.
Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A (show VAPA Proteins) revealed by NMR and mutagenesis studies.
Partitioning of Osbp between the endoplasmic reticulum and the Golgi apparatus is regulated by Vapa (show VAPA Proteins).
OSBP opposes the activity of LXR (show NR1H3 Proteins) by negatively regulating ABCA1 (show ABCA1 Proteins) 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
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, oxysterol-binding protein
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