Fluor de Lys®-SIRT1 is a fluorogenic, acetylated peptide substrate for SIRT1 (human Sirtuin 1). Based on residues 379-382 of p53 (Arg-His-Lys-Lys(Ac)), a site of regulatory acetylation by the p300 and CBP acetyltransferases (lysines 381, 382), it was the best substrate for SIRT1 from among a panel of substrates patterned on p53, histone H3, and histone H4 acetylation sites. Fluor de Lys
®-SIRT1 is deacetylated by SIRT1 (BML-SE239) at a rate of more then 8-fold that of the acetylated lysine substrate, Fluor de Lys
® (Prod. No. BML-KI104; acetylated substrates both at 25 µM, 500 µM NAD
+).
The K
m of
Fluor de Lys®-SIRT1 for human recombinant Sirtuin 1 is 108 µM (determined at 37°C, 500 µM NAD
+). Must be used in conjunction with Fluor de Lys
® Developer II (Prod. No. BML-KI176). Fluorescent signal indicates deacetylation of Lys382. Sufficient for 100-200 assays of human recombinant SIRT1 (1U/well, 50-100 µM substrate).
Product Specification
General Literature References
MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation: A. Ito et al.; Embo J
21, 6236 (6236),
Abstract;
Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases: N.A. Barletv et al.; Mol Cell
8, 1243 (2001),
Abstract;
p300/CBP-mediated p53 acetylation is commonly induced by p53-activating agents and inhibited by MDM2: A. Ito et al.; Embo J
20, 1331 (2001),
Abstract;
p53 sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage: L. Liu et al.; Mol Cell Biol
19, 1202 (1999),
Abstract;
DNA damage activates p53 through a phosphorylation-acetylation cascade: K. Sakaguchi et al.; Genes Dev.
12, 2831 (1998),
Abstract;
Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain: W. Gu et al.; Cell
90, 595 (1997),
Abstract;
BIOMOL Research Laboratories, Inc.; Unpublished results (0),