Fluor-de-Lys^® -SIRT1 deacetylase substrate



BML-KI177-0005	0.5 µmol	159.00 USD

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⁺).

more

Product Specification

Quantity:	0.5 µmol (100 µl)

Purity:	≥95% (HPLC)

Formulation:	Supplied as a 5 mM solution in HDAC Assay Buffer.

Long Term Storage:	-80°C

Background / Technical Information:	Please click here for the comprehensive product datasheet.

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BIOMOL Research Laboratories, Inc.; Unpublished results (0),