PD151242

[¹²⁵I]-PD151242 (8 pM-8 nM; 2 h) binds to a single population of high-affinity endothelin receptors in frozen sections of normal human kidneys, with a K_D value of 0.75 nM^[1].
[¹²⁵I]-PD151242 (8 nM; 2 h) remains stable under the receptor binding assay conditions using frozen sections of normal human kidneys, with over 95% of the radioligand remaining intact after a 2 h incubation^[1].
[¹²⁵I]-PD151242 (0.1 nM) selectively localizes to ET_A receptors on intrarenal blood vessels (including arcuate arteries, veins, and arterioles) in frozen sections of normal human kidneys^[1].
[¹²⁵I]-PD151242 (0.1 nM) binds specifically to ET_A receptors in confluent rat A10 aortic vascular smooth muscle cells, as only ET_A-selective ligands can competitively inhibit this binding^[1].
PD151242 (2 h) exhibits over 10000-fold higher selectivity for ET_a receptors than for ET_B receptors in human left ventricular slices. It competes with [¹²⁵I]-ET-1 (HY-P0202) for binding, with a K_d of 7.21 nM at ET_a sites and 104 μM at ET_B sites^[2].
PD151242 (2 h) competes with [¹²⁵I]-PD151242 for binding to human left ventricular slices, with a high-affinity dissociation constant K_d of 0.65 nM^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.