The organic anion transporting polypeptides, OATP-A (also designated OATP1, OATP1A2 and SLC21A3) and OATP-C (also designated OATP2, SLC21A6 and LST1), mediate hepatic uptake of cardiac glycosides. The expression of OATP-C, but not OATP-A, is inducible by phenobarbital and pregnenolone-16a-carbonitrile, resulting in the increased capacity of the liver to extract cardiac glycosides from the plasma. OATP-A is expressed in liver and kidney and helps mediate sodium-independent uptake of the anionic steroid conjugates dehydroepiandrosterone sulfate, estradiol-17-glucuronide and prostaglandin. OATP-C is exclusively expressed in liver and is localized to the basolateral hepatocyte membrane. Although OATP-C mRNA levels decrease during pregnancy and increase postpartum, OATP-C protein levels remain relatively constant. OATP-C transports taurocholic acid, the adrenal androgen dehydroepiandroserone sulfate, thyroid hormone, hydroxymethylglutaryl-CoA reductase inhibitor and pravastatin. OATP-C is therefore a novel organic anion transport protein that has overlapping but not identical substrate specificities with other subtypes of OATP. OATP-A and OATP-C are both pravastatin transporters, suggesting that they are responsible for the hepatic uptake of the liver-specific hydroxymethylglutaryl-CoA reductase inhibitor in mouse, rat and human.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of OATP-A of human origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 611-665 mapping near the C-terminus of OATP-A of human origin
Tissue Specificity
epitope corresponding to amino acids 611-665 mapping near the C-terminus of OATP-A of human origin