Sirtuin
Silent information regulator 2 (Sir2) proteins, also known as sirtuins, are a family of nicotine adenine dinucleotide (NAD) dependent protein deacetylases in organisms ranging from bacteria to humans that are characterized by the presence of a unique and highly conserved catalytic domain of approximately 260 amino acids. Sirtuins are divided into 5 classes, including Class I (subclasses Ia, Ib and Ic), Class II, Class III, Class IV (subclasses IVa and IVb) and Class U (Gram-positive bacteria specific). The catalytic domain of sirtuins is comprised of two bilobed globular domains, the large domain containing the NAD-binding pocket and the small domain binding the acetyl-lysine substrate.
- B5971 Triacetyl ResveratrolSummary: Cell-permeable resveratrol prodrug
- B6063 SIRT1/2 Inhibitor IVSummary: SIRT1 and SIRT2 inhibitor
- C3552 4'-bromo-Resveratrol1 CitationSummary: Sirt1 and Sirt3 inhibitor
- C3888 JGB1741Summary: SIRT1 inhibitor
- C5180 JFD00244Summary: inhibitor of SIRT2
- C5709 AGK7Summary: cell-permeable, selective inhibitor of SIRT2
- B4713 AK-7Summary: selective and brain-permeable SIRT2 inhibitor
- A8302 Tenovin-6Target: Sir2-like Family Deacetylases (Sirtuins)Summary: SIRT inhibitor and p53 activator
- A8567 Tenovin-3Summary: p53 activator
- B3272 InauhzinTarget: Sir2-like Family Deacetylases (Sirtuins)Summary: SIRT1 inhibitor