General description

A cell-permeable quinolinecarboxamide compound that is shown to inhibit the mitochondrial SIRT3 in a substrate AceCS2-competitive (K_i = 0.56 µM; K_m = 2.44 µM), but NAD⁺-uncompetitive (K_i = 0.34 µM; K_m = 280 µM), manner. Also reported to decrease cellular p53 Lys382 acetylation (Effective conc. = 10 µM in U2OS and MEF cultures) and inhibit p300 HAT activity (IC₅₀ = 9 µM) in vitro, as well as offer therapeutic benefits in several murine and rodent type 2 diabetes models (100 mg/kg/dayl p.o.) in vivo. Whether and how SRT1720 activates SIRT1 activity remains uncertain. Also available as a 25 mM solution in DMSO (Cat. No. 530748).

A cell-permeable quinolinecarboxamide compound that is shown to inhibit the mitochondrial SIRT3 in a substrate AceCS2- (Acetyl-CoA synthetase 2) competitive (K_i = 0.56 µM; K_m = 2.44 µM; V_max = 173.35 µM/min), but NAD⁺-uncompetitive (K_i = 0.34 µM; K_m = 280 µM; V_max = 0.86 µM/min), manner, indicative of NAD⁺ binding as a prerequisite for inhibitor binding. Also reported to decrease cellular p53 Lys382 acetylation (Effective conc. = 10 µM in U2OS and MEF cultures) and inhibit p300 HAT activity (IC₅₀ = 9 µM) in vitro, as well as offer therapeutic benefits in several murine and rodent type 2 diabetes models (100 mg/kg/dayl p.o.) in vivo. Whether and how SRT1720 activates SIRT1 activity remains uncertain.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Other Notes

Baur, J.A., et al. 2012. Nat. Rev. Drug Discov.11, 443.Minor, R.K., et al. 2011. Sci. Rep.1, 70.Huber, J.L., et al. 2010. Future Med. Chem.2, 1751Pacholec, M., et al. 2010. J. Biol. Chem.285, 8340Jin, L., et al. 2009. Protein Sci.18, 514Feige, J.N., et al. 2008. Cell Metab.8, 347Milne, J.C., et al. 2007. Nature450, 712.

Packaging

Packaged under inert gas

10 mg in Glass bottle

Warning

Toxicity: Regulatory Review (Z)