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OSBPL9 encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Additionally we are shipping OSBPL9 Proteins (8) and OSBPL9 Kits (2) and many more products for this protein.
Showing 10 out of 37 products:
Human Polyclonal OSBPL9 Primary Antibody for IHC (p), IHC - ABIN250068
Lehto, Laitinen, Chinetti, Johansson, Ehnholm, Staels, Ikonen, Olkkonen: The OSBP-related protein family in humans. in Journal of lipid research 2001
Show all 2 Pubmed References
These studies identify ORP9 as a dual sterol/PI-4P binding protein that could regulate PI-4P in the Golgi apparatus.
T allele of rs768529 may be a risk factor for the formation of the carotid vulnerable plaque in Chinese Hunan Han population
The results identify ORP11 (show OSBPL11 Antibodies) as an OSBP (show OSBP Antibodies) homologue distributing at the Golgi-LE interface and define the ORP9-ORP11 (show OSBPL11 Antibodies) dimer as a functional unit that may act as an intracellular lipid sensor or transporter.
Includes data showing N-alpha terminal acetylation of this protein (OSBL9_HUMAN), which begins with nASIMEGPLSK following cleavage of the initiating Met-1 residue.
Furthermore, mammalian target of rapamycin (show FRAP1 Antibodies) was implicated in ORP9L phosphorylation in HEK293 cells. These studies identify ORP9 as a PDK-2 (show PDK2 Antibodies) substrate and negative regulator of Akt (show AKT1 Antibodies) phosphorylation at the PDK-2 (show PDK2 Antibodies) site.
MicroRNA-125a-5p may partly provide post-transcriptional regulation of the proinflammatory response, lipid uptake, and expression of ORP9 in oxLDL-stimulated monocyte/macrophages.
Includes data showing N-alpha terminal acetylation of the homologous human protein (OSBL9_HUMAN), where the N-terminal sequence is nASIMEGPLSK following cleavage of the initiating Met-1 (show DNMT1 Antibodies) derived from a downstream start codon in the transcript.
This gene encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Most members contain an N-terminal pleckstrin homology domain and a highly conserved C-terminal OSBP-like sterol-binding domain, although some members contain only the sterol-binding domain. This family member functions as a cholesterol transfer protein that regulates Golgi structure and function. Multiple transcript variants, most of which encode distinct isoforms, have been identified. Related pseudogenes have been identified on chromosomes 3, 11 and 12.
oxysterol binding protein-like 9
, oxysterol-binding protein-related protein 9
, oxysterol-binding protein-like protein 9
, hypothetical protein LOC779737
, Oxysterol-binding protein-related protein 9
, oxysterol-binding protein-related protein 9-like
, OSBP-related protein 9