Anti-OSBP1 Antibody Picoband® Fluoro647 Conjugated

OSBP (Oxysterol-Binding Protein), also called OSBP1, is a protein that in humans is encoded by the OSBP gene. Im et al. (2005) reported the structure of the full-length yeast oxysterol-binding-protein Osh4, a member of the OSBP-related protein (ORP) family, at 1.5- to 1.9-angstrom resolution in complexes with ergosterol, cholesterol, and 7-, 20- and 25-hydroxy cholesterol. Moreira et al. (2001) refined the localization of the OSBP1 gene to chromosome 11q12.1 by radiation hybrid analysis. Wang et al. (2005) found that OSBP functions as a cholesterol-binding scaffolding protein coordinating the activity of 2 phosphatases to control the extracellular signal-regulated kinase (ERK) signaling pathway. Cytosolic OSBP formed an approximately 440-kD oligomer with a member of the PTPPBS family of tyrosine phosphatases, the serine/threonine phosphatase PP2A, and cholesterol.

Cardiovascular, Cholesterol Metabolism, Lipid and Lipoprotein Metabolism, Lipid Metabolism, Lipids/Lipoproteins, Metabolic Signaling Pathways, Metabolism, Pathways and Processes, Signal Transduction

Binds cholesterol and a range of oxysterols including 25-hydroxycholesterol (PubMed:15746430, PubMed:17428193) . Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25-hydroxycholesterol causes its disassembly (PubMed:15746430) . Regulates cholesterol efflux by decreasing ABCA1 stability (PubMed:18450749) . .

1. Im, Y. J., Raychaudhuri, S., Prinz, W. A., Hurley, J. H. Structural mechanism for sterol sensing and transport by OSBP-related proteins. Nature 437: 154-158, 2005. 2. Moreira, E. F., Jaworski, C., Li, A., Rodriguez, I. R. Molecular and biochemical characterization of a novel oxysterol-binding protein (OSBP2) highly expressed in retina. J. Biol. Chem. 276: 18570-18578, 2001. 3. Wang, P., Weng, J., Anderson, R. G. W. OSBP is a cholesterol-regulated scaffolding protein in control of ERK1/2 activation. Science 307: 1472-1476, 2005.