Anti-OSBP

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Oxysterol-Binding Protein 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. Protein function: Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum (PubMed:24209621). 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). [The UniProt Consortium]