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OSBPL8 encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Additionally we are shipping Oxysterol Binding Protein-Like 8 Kits (7) and Oxysterol Binding Protein-Like 8 Proteins (5) and many more products for this protein.
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ORP5/8 regulate Ca(2+) signaling at specific membrane contact sites foci.
Examination of a series of deletion constructs demonstrated that both the N-terminal polybasic region and the PH domain are required for proper targeting of the short splice variant ORP8S to the PM-ER contact site in Chinese hamster ovary cells.
ORP5/8 are endoplasmic reticulum (ER) membrane proteins implicated in lipid trafficking that localize to ER-plasma membrane (PM) contacts and maintain membrane homeostasis. Here the authors show that PtdIns(4,5)P 2 plays a critical role in the targeting and function of ORP5/8 at the PM.
we found that overexpression of ORP8 significantly inhibits GC cell proliferation and implanted tumor growth in vivo. Induction of ER stress, inhibition of Wnt signaling, and apoptotic cell death are involved in ORP8-induced inhibition of GC cell proliferation.
mammalian ORP5 and ORP8 proteins localize to ER-mitochondrial MCS, in addition to ER-PM contact sites.
the present study suggests that ORP8 may mediate the cytotoxicity of 25-hydroxycholesterol.
ORP5 and ORP8 could mediate PI4P/phosphatidylserine (PS) countertransport between the endoplasmic reticulum (ER) and the plasma membrane (PM), thus delivering PI4P to the ER-localized PI4P phosphatase Sac1 for degradation and PS from the ER to the PM.
role of ORP8 in Fas translocation to the plasma membrane and its down-regulation by miR-143 offer a putative mechanistic explanation for HCC resistance to apoptosis
Data indicate that miR-143 impairs insulin action via downregulation of oxysterol-binding protein-related protein 8 (ORP8).
ORP8 overexpression resulted in reduced expression of the aP2 mRNA, while down-regulation of adiponectin and aP2 was observed in ORP11 silenced cells. ORP8 overexpression or silencing of ORP11 markedly decreased cellular triglyceride storage.
results reveal that ORP8 has the capacity to modulate lipid homeostasis and SREBP activity, probably through an indirect mechanism, and provide clues of an entirely new mode of ORP action
Data identify ORP8 as a negative regulator of ABCA1 expression and macrophage cholesterol efflux. ORP8 may, thus, modulate the development of atherosclerosis.
occurrence of an unusual TG 3' splice site in intron 2
Orp8 deficiency in bone marrow-derived cells reduces atherosclerotic lesion progression in LDL receptor knockout mice.
Osbpl8 deficiency in mouse causes an elevation of high-density lipoproteins and gender-specific alterations of lipid metabolism.
aspects of ORP8 function in macrophages not directly involving lipid metabolism, but rather associated with nuclear functions, microtubule organization, and migration capacity
This gene encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Like most members, the encoded protein contains an N-terminal pleckstrin homology domain and a highly conserved C-terminal OSBP-like sterol-binding domain. Two transcript variants encoding different isoforms have been found for this gene.
oxysterol-binding protein-related protein 8
, oxysterol binding protein-like 8
, oxysterol-binding protein-like protein 8
, oxysterol-binding protein-related protein 8-like
, OSBP-related protein 8