Description General description A cell-permeable quinolinecarboxamide compound that is shown to inhibit the mitochondrial SIRT3 in a substrate AceCS2- (Acetyl-CoA synthetase 2) competitive (Ki = 0.56 µM; Km = 2.44 µM; Vmax = 173.35 µM/min), but NAD+-uncompetitive (Ki = 0.34 µM; Km = 280 µM; Vmax = 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. A cell-permeable quinolinecarboxamide compound that is shown to inhibit the mitochondrial SIRT3 in a substrate AceCS2-competitive (Ki = 0.56 µM; Km = 2.44 µM), but NAD+-uncompetitive (Ki = 0.34 µM; Km = 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). Packaging 10 mg in Glass bottle Packaged under inert gas Warning Toxicity: Regulatory Review (Z) 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, 1751 Pacholec, M., et al. 2010. J. Biol. Chem.285, 8340 Jin, L., et al. 2009. Protein Sci.18, 514 Feige, J.N., et al. 2008. Cell Metab.8, 347 Milne, J.C., et al. 2007. Nature450, 712.