Fluor-de-Lys™ -SIRT1 deacetylase substrate



BML-KI177-0005	0.5 µmol	154.00 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⁺).

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Product Specification

Quantity:	0.5 µmol (100 µl)

Purity:	≥95% (HPLC)

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

Shipping:	SHIPPED ON DRY ICE

Long Term Storage:	-80°C

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

General Literature References

BIOMOL Research Laboratories, Inc. Unpublished results (0)

Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain W. Gu et al. Cell 90 595 (1997) Abstract

DNA damage activates p53 through a phosphorylation-acetylation cascade K. Sakaguchi et al. Genes Dev. 12 2831 (1998) 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

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

MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation A. Ito et al. Embo J 21 6236 (6236) Abstract