OSBP2 / ORP4

GWB-2C5291

Peptide with sequence KEKQDWHMCPNIF from the C Terminus of the pr Notes: Peptide ELISA: antibody detection limit dilution > 1:32 000. Western Blot: Preliminary experiments gave no signal but low background in Human Testis and Brain extracts at up to 1ug/ml. Summary: Oxysterols are byproducts of cholesterol that can have cytotoxic effects on many cell types. The membrane-bound protein encoded by this gene contains a pleckstrin homology (PH) domain and an oxysterol-binding region. It binds oxysterols such as 7-ketocholesterol and may inhibit their cytotoxicity. Alternate transcriptional splice variants have been observed but have not been fully characterized. [1] Wyles J. P. Perry R. J. and Ridgway N. D. et al. Characterization of the sterol-binding domain of oxysterol-binding protein (OSBP)-related protein 4 reveals a novel role in vimentin organization[2] Torrini M. Marchese C. Vanzetti M. Marini V. Origone P. Garre C. and Mareni C. Mutation analysis of oxisterol-binding-protein gene in patients with age-related macular degeneration[3] Henriques Silva N. Vasconcellos Fournier M. Pimenta G. Pulcheri W. A. Spector N. and da Costa Carvalho Mda G. HLM/OSBP2 is expressed in chronic myeloid leukemia[4] Wang C. JeBailey L. and Ridgway N. D. et al. Oxysterol-binding-protein (OSBP)-related protein 4 binds 25-hydroxycholesterol and interacts with vimentin intermediate filaments[5] Jaworski C. J. Moreira E. Li A. Lee R. and Rodriguez I. R. et al. A family of 12 human genes containing oxysterol-binding domains