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FLUOR DE LYS®-SIRT1 deacetylase substrate

BML-KI177-0005 0.5 µmol 262.00 USD
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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).

Product Details

Quantity:0.5 µmol (100 µl)
Formulation:Supplied as a 5 mM solution in HDAC Assay Buffer.
Purity:≥95% (HPLC)
Shipping:Dry Ice
Long Term Storage:-80┬░C
Regulatory Status:RUO - Research Use Only

Product Literature References

High-throughput screening of histone deacetylases and determination of kinetic parameters using fluorogenic assays: C. Moreno-Yruela, et al.; STAR Protoc. 2, 100313 (2021), Application(s): HTS protocol to identify deacylase activities, Abstract; Full Text
Inhibition of histone deacetylase 6 suppresses inflammatory responses and invasiveness of fibroblast-like-synoviocytes in inflammatory arthritis: J. K. Park, et al.; Arthritis Res. Ther. 23, 13075 (2021), Abstract;
Resveratrol-induced Sirt1 phosphorylation by LKB1 mediates mitochondrial metabolism: Y. Huang, et al.; J. Biol. Chem. 297, 100929 (2021), Abstract;
The Contribution of Romidepsin to the Herbicidal Activity of Burkholderia rinojensis Biopesticide: D.K. Owens, et al.; J. Nat. Prod. 83, 843 (2020), Abstract;
Identification of Diketopiperazine-Containing 2-Anilinobenzamides as Potent Sirtuin 2 (SIRT2)-Selective Inhibitors Targeting the "Selectivity Pocket", Substrate-Binding Site, and NAD+-Binding Site: P. Mellini, et al.; J. Med. Chem. 62, 5844 (2019), Abstract;
Pharmacophore modeling and virtual screening studies to identify novel selective SIRT2 inhibitors: G. Eren, et al.; J. Mol. Graph. Model. 10, 1313 (2019), Abstract;
Design, synthesis and biological screening of 2-aminobenzamides as selective HDAC3 inhibitors with promising anticancer effects: P. Trivedi, et al.; Eur. J. Pharm. Sci. 124, 165 (2018), Abstract;
Two Novel Proline-Containing Catechin Glucoside from Water-Soluble Extract of Codonopsis pilosula: F.Y. Qin, et al.; Molecules 23, E180 (2018), Application(s):SIRT1 Inhibition, Abstract; Full Text
Design, synthesis of allosteric peptide activator for human SIRT1 and its biological evaluation in cellular model of Alzheimer's disease: R. Kuma, et al.; Eur. J. Med. Chem. 127, 909 (2017), Abstract;
Human histone deacetylase 6 shows strong preference for tubulin dimers over assembled microtubules: L. Skultetyova, et al.; Sci. Rep. 7, 11547 (2017), Abstract; Full Text
BET Inhibition Upregulates SIRT1 and Alleviates Inflammatory Responses: T. Kokkola, et al.; Chembiochem 16, 1997 (2015), Abstract; Full Text
AROS has a context-dependent effect on SIRT1: T. Kokkola, et al.; FEBS Lett. 2, 588 (2014), Abstract;
Synthesis and evaluation of aliphatic-chain hydroxamates capped with osthole derivatives as histone deacetylase inhibitors: W.H. Huang, et al.; Eur. J. Med. Chem. 46, 4042 (2011), Abstract;

General Literature References

MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation: A. Ito, et al.; EMBO J. 21, 6236 (2002), 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;

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