BD140

BD140 (0.2 μM; 0.66 μg/mL PM_2.5) specifically detects HSA bound to cyclone-collected PM_2.5 particles via targeted fluorescence emission at 356/585 nm^[1].
BD140 (3 μM) exhibits a 41-fold fluorescence quantum yield increase upon binding to human serum albumin, with a quantum yield of 0.15 in the presence of 30 μM HSA^[2].
BD140 (3 μM) binds to human serum albumin in a 1:1 stoichiometry with a dissociation constant (K_D) of 4.1 μM^[2].
BD140 (3 μM; 30 min) when combined with DNSA, enables multiplex mapping of human serum albumin drug binding sites, accurately identifying site 2-specific drug displacement, including in a high-throughput screen of 640 FDA-approved drugs where 112 compounds showed binding site activity^[2].
BD140 (3 μM; 30 min) binds specifically to HSA site 2 with a 41-fold fluorescence quantum yield increase, and this binding is not competed by DIC, BSH, or MID^[3].

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