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BML-KI177 Revised 05-Mar-10
Fluor-de-Lys™ -SIRT1 deacetylase substrate
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PRODUCT LINE Kits & Sets
PRODUCT CATEGORY Kit Components
Ordering Information
Product Numbers: Format: Size: Unit Price: Quantity: Add To Cart
BML-KI177-0005   0.5 µmol 154.00 USD Add To Cart
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
Product Description
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 Km 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).
General Information
General Literature References
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
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
Acetylation of p53 activates transcription through recruitment of coactivators/histone acetyltransferases: N.A. Barletv et al.; Mol Cell 8, 1243 (2001) Abstract
MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation: A. Ito et al.; Embo J 21, 6236 (6236) Abstract
BIOMOL Research Laboratories, Inc.; Unpublished results
 
 

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