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OSBPL9 encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Zusätzlich bieten wir Ihnen OSBPL9 Proteine (8) und OSBPL9 Kits (2) und viele weitere Produktgruppen zu diesem Protein an.
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Human Polyclonal OSBPL9 Primary Antibody für 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 (zeige OSBPL11 Antikörper) as an OSBP (zeige OSBP Antikörper) homologue distributing at the Golgi-LE interface and define the ORP9-ORP11 (zeige OSBPL11 Antikörper) 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 (zeige FRAP1 Antikörper) was implicated in ORP9L phosphorylation in HEK293 cells. These studies identify ORP9 as a PDK-2 (zeige PDK2 Antikörper) substrate and negative regulator of Akt (zeige AKT1 Antikörper) phosphorylation at the PDK-2 (zeige PDK2 Antikörper) 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 (zeige DNMT1 Antikörper) 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