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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 Proteins (5) and Oxysterol Binding Protein Kits (2) and many more products for this protein.
Showing 10 out of 61 products:
Human Polyclonal OSBP Primary Antibody for ELISA, WB - ABIN250354
Romeo, Kazlauskas: Oxysterol and diabetes activate STAT3 and control endothelial expression of profilin-1 via OSBP1. in The Journal of biological chemistry 2008
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Human Polyclonal OSBP Primary Antibody for IP, ELISA - ABIN250053
Moreira, Jaworski, Li, Rodriguez: Molecular and biochemical characterization of a novel oxysterol-binding protein (OSBP2) highly expressed in retina. in The Journal of biological chemistry 2001
Show all 2 Pubmed References
Cow (Bovine) Polyclonal OSBP Primary Antibody for WB - ABIN611390
Watanabe, Ikejima, Suzuki, Shimada: Genomic organization and expression of the human MSH3 gene. in Genomics 1997
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Study identified an OSBP- and FAN (show NSMAF Antibodies)-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 (show IQGAP1 Antibodies) in mTORC1 signaling
These results suggest that poliovirus proteins modulate PI4KB (show PI4KB Antibodies) 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 Antibodies) negatively regulates HCV secretion/release by attenuating OSBP and CERT (show COL4A3BP Antibodies) 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 Antibodies) 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.
OSBP may be a target and downstream effector of miR (show MLXIP Antibodies)-124 for regulating neurite outgrowth and elongation.
Partitioning of Osbp between the endoplasmic reticulum and the Golgi apparatus is regulated by Vapa (show VAPA Antibodies).
OSBP opposes the activity of LXR (show NR1H3 Antibodies) by negatively regulating ABCA1 (show ABCA1 Antibodies) 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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