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Dileucine motif in the extracellular N-terminal region is essential for OSTB plasma membrane targeting.
Hepatic OSTalpha (show OSTALPHA Proteins)-OSTbeta expression is induced by hypoxia.
OSTbeta is a target of RARalpha (show RARA Proteins)-mediated (by binding to DR5 (show TNFRSF10B Proteins) response element) gene regulation pathways
Ostbeta is required for both proper trafficking of Ostalpha (show OSTALPHA Proteins) and formation of the functional transport unit, and identify specific residues of Ostbeta critical for these processes.
The present report summarizes the evidence for a pleiotropic role of Ostalpha (show OSTALPHA Proteins)-Ostbeta in different tissues.
OSTbeta is localized to steroidogenic cells of the brain and adrenal gland, and it modulates DHEA/DHEAS (show SULT2A1 Proteins) homeostasis
OSTbeta has roles in biological transport and is widely expressed in human tissues
overexpr (show OSTALPHA Proteins)ession of human OSTalpha and OSTbeta facilitated the uptake of conjugated chenodeoxycholate (show NR1H4 Proteins) and the activation of FXR target genes
OSTalpha (show OSTALPHA Proteins)/OSTbeta expression is induced by bile acids through ligand-dependent transactivation of both OST (show DDOST Proteins) genes by the nuclear bile acid receptor (show NR1H4 Proteins)/farnesoid X receptor (show xpr1 Proteins) (FXR (show NR1H4 Proteins)).
the selective localization of OSTalpha (show OSTALPHA Proteins) and OSTbeta to the basolateral plasma membrane of epithelial cells responsible for bile acid and sterol reabsorption.
Data suggest that transport of bile acid taurocholate is retained when OstB is truncated to contain only the transmembrane domain with 15 additional residues on each side and co-expressed with intact OstA (organic solute transporter alpha subunit (show OSTALPHA Proteins)); shorter fragments of OstB are inactive.
Co-expression of mouse Ostalpha (show OSTALPHA Proteins)-Ostbeta, but not the individual subunits, stimulated Na(+)-independent bile acid uptake and the apical-to-basolateral transport of taurocholate
OSTalpha (show OSTALPHA Proteins) and OSTbeta mRNA levels were induced in the adrenals and kidneys of wild-type, but not FXR (show NR1H4 Proteins)-/-, mice
In conclusion, we identified Ost-alpha (show OSTALPHA Proteins)/Ost-beta as a novel FXR (show NR1H4 Proteins) target. Absent Ost-alpha (show OSTALPHA Proteins)/Ost-beta induction in CA-fed FXR (show NR1H4 Proteins)(-/-) animals may contribute to increased liver injury in these animals.
The mouse Ostalpha (show OSTALPHA Proteins) and Ostbeta promoters are unusual in that they contain functional FXR (show NR1H4 Proteins) and LRH elements, which mediate, respectively, positive and negative feedback regulation by bile acids.
These results indicate that expression of Ostalpha (show OSTALPHA Proteins) and Ostbeta are highly regulated in response to cholestasis and that this response is dependent on the FXR bile acid receptor (show NR1H4 Proteins).
LXRalpha (show NR1H3 Proteins) transcriptionally regulate mouse organic solute transporter alpha (show OSTALPHA Proteins)/beta via inverted repeat-1 elements shared with farnesoid X receptor (show xpr1 Proteins)
Present as heterodimers (with Ost alpha (show OSTALPHA Proteins)) and/or heteromultimers; the interaction between Ostalpha (show OSTALPHA Proteins) and Ostbeta increases the stability of the proteins and is required for delivery of the heteromeric complex to the plasma membrane.
These data indicate that Ostalpha (show OSTALPHA Proteins)-Ostbeta is essential for intestinal bile acid transport in mice.
Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood. Efficiently transports the major species of bile acids (By similarity).
organic solute transporter beta
, organic solute transporter subunit beta
, solute carrier family 51 subunit beta
, organic solute transporter beta subunit
, Ost beta