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FLUOR DE LYS®-HDAC8 deacetylase substrate

A fluorogenic, diacetylated peptide substrate for HDAC8 (histone deacetylase-8).
BML-KI178-0005 0.5 µmol 252.00 USD
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FLUOR DE LYS®-HDAC8 is a fluorogenic, diacetylated peptide substrate for HDAC8 (histone deacetylase-8). Based on residues 379-382 of p53 (Arg-His-Lys(Ac)-Lys(Ac)), a site of regulatory acetylation by the p300 and CBP acetyltransferases (lysines 381, 382), it was the best for HDAC8 from among a panel of substrates patterned on p53, histone H3 and histone H4 acetylation sites. FLUOR DE LYS®-HDAC8 is deacetylated by HDAC8 at a rate of more than 10-fold that of the acetylated lysine substrate, FLUOR DE LYS® (BML-KI104; substrates both at 100 µM). Although named because of HDAC8’s preference for it, it is also an excellent substrate for SIRT1 (BMl-SE239; 5x the rate of BML-KI104 at 25 µM, 0.5 mM NAD+), SIRT2 and HeLa Nuclear Extract (BML-KI140; 3x KI-104 rate, 25 µM). Must be used in conjunction with FLUOR DE LYS® Developer II (BML-KI176). Sufficient for 100-200 assays of human recombinant HDAC8 (BML-SE145; 1 U/well, 50-100 µM substrate).

Product Details

Formulation:Supplied as a 5 mM solution (100 µl) in HDAC Assay Buffer.
Shipping:Dry Ice
Long Term Storage:-80°C
Regulatory Status:RUO - Research Use Only

Product Literature References

Synthesis, Biochemical, and Cellular Evaluation of HDAC6 Targeting Proteolysis Targeting Chimeras: S. Darwish, et al.; Methods Mol. Biol. 2023, 2589 (2023), Abstract;
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
Species-selective targeting of pathogens revealed by the atypical structure and active site of Trypanosoma cruzi histone deacetylase DAC2: M. Marek, et al.; Cell Reports 37, 110129 (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;
A Novel Class of Schistosoma mansoni Histone Deacetylase 8 (HDAC8) Inhibitors Identified by Structure-Based Virtual Screening and In Vitro Testing: C.V. Simoben, et al.; Molecules 23, E566 (2018), Abstract; Full Text
Carbamates as Potential Prodrugs and a New Warhead for HDAC Inhibition: K. King, et al.; Molecules 23, E321 (2018), Abstract; Full Text
General Base-General Acid Catalysis in Human Histone Deacetylase 8: S.M. Gantt, et al.; Biochemistry 55, 820 (2016), Abstract; Full Text
Structural and Functional Influence of the Glycine-Rich Loop G302GGGY on the Catalytic Tyrosine of Histone Deacetylase 8: N.J. Porter, et al.; Biochemistry. 55, 6718 (2016), Abstract;
Structure-Based Design and Synthesis of Novel Inhibitors Targeting HDAC8 from Schistosoma mansoni for the Treatment of Schistosomiasis: T. Heimburg, et al.; J. Med. Chem. 59, 2423 (2016), Application(s): Enzyme activity assays, Abstract; Full Text
Biochemical and structural characterization of HDAC8 mutants associated with Cornelia de Lange syndrome spectrum disorders: C. Decroos, et al.; Biochemistry 54, 6501 (2015), Application(s): Enzyme activity assays, Abstract; Full Text
Crystal structure of an arginase-like protein from Trypanosoma brucei that evolved without a binuclear manganese cluster: Y. Hai, et al.; Biochemistry 54, 458 (2015), Application(s): Enzyme activity assays, Abstract; Full Text
Design, Synthesis, and Evaluation of Polyamine Deacetylase Inhibitors, and High-Resolution Crystal Structures of Their Complexes with Acetylpolyamine Amidohydrolase: C. Decroos & D.W. Christianson; Biochemistry 54, 4692 (2015), Abstract; Full Text
Selective Sirt2 inhibition by ligand-induced rearrangement of the active site: T. Rumpf, et al.; Nat. Commun. 6, 6263 (2015), Abstract; Full Text
Compromised Structure and Function of HDAC8 Mutants Identified in Cornelia de Lange Syndrome Spectrum Disorders: C. Decroos, et al.; ACS Chem. Biol. 9, 2157 (2014), Application(s): Measure the catalytic activities of HDAC8 mutants, Abstract;
Discovery of inhibitors of Schistosoma mansoni HDAC8 by combining homology modeling, virtual screening, and in vitro validation: S. Kannan, et al.; J. Chem. Inf. Model. 54, 3005 (2014), Abstract;
Loss-of-function HDAC8 mutations cause a phenotypic spectrum of Cornelia de Lange syndrome-like features, ocular hypertelorism, large fontanelle and X-linked inheritance: F.J. Kaiser, et al.; Hum. Mol. Gen. 23, 2888 (2014), Application(s): Enzyme activity assays, Abstract; Full Text
Molecular Basis for the Antiparasitic Activity of a Mercaptoacetamide Derivative That Inhibits Histone Deacetylase 8 (HDAC8) from the Human Pathogen Schistosoma mansoni: D. Stolfa, et al.; J. Mol. Biol. 426, 3442 (2014), Application(s): In vitro HDAC inhibition assay of parasitic flatworm, Abstract;
Structural basis for the inhibition of histone deacetylase 8 (HDAC8), a key epigenetic player in the blood fluke Schistosoma mansoni: M. Marek, et al.; PLoS Pathog. 9, e1003645 (2013), Application(s): Human and smHDAC8 activity assay, Abstract; Full Text
Insights from comprehensive multiple receptor docking to HDAC8: M. Brunsteiner, et al.; J. Mol. Model. 18, 3927 (2012), Abstract;

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