Recombinant Anti-Mouse Abcb1a VHH Single Domain Antibody (Nb592)

Figure 1 Nb592 is a strong inhibitor of P-gp’s ATPase activity.

Nb592 inhibits verapamil-stimulated ATPase activity with an IC50 of 520 ± 57 nM. Data points indicate the average activity ± SEM from four independent experiments, relative to P-gp's activity in the absence of Nb592.

Ward, A. B., Szewczyk, P., Grimard, V., Lee, C. W., Martinez, L., Doshi, R., ... & Swartz, D. J. (2013). Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain. Proceedings of the National Academy of Sciences, 110(33), 13386-13391.

Figure 2 Nb592 is a strong inhibitor of P-gp’s ATPase activity.

Inhibition of verapamil-stimulated ATPase activity in the presence of 5 mM DTT, without or with 7.5 μM Nb592 (n = 4).

Ward, A. B., Szewczyk, P., Grimard, V., Lee, C. W., Martinez, L., Doshi, R., ... & Swartz, D. J. (2013). Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain. Proceedings of the National Academy of Sciences, 110(33), 13386-13391.

Figure 3 Nb592 is a strong inhibitor of P-gp’s ATPase activity.

Nb592 prevents vanadate-induced 8-azido-[α³²P]-ADP trapping in P-gp's catalytic sites. P-gp was incubated with 100 μM verapamil (VER) and 200 μM orthovanadate (Vi) in the 8-azido-[α³²P]-ATP hydrolysis/trapping reaction as indicated above the lanes.

Ward, A. B., Szewczyk, P., Grimard, V., Lee, C. W., Martinez, L., Doshi, R., ... & Swartz, D. J. (2013). Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain. Proceedings of the National Academy of Sciences, 110(33), 13386-13391.