FLUOR DE LYS® Substrate is a highly sensitive and convenient alternative to radiolabeled, acetylated histones or peptide/HPLC methods for the assay of histone deacetylases. The FLUOR DE LYS® Substrate, which comprises an acetylated lysine side chain, is incubated with a sample containing HDAC activity (nuclear or cellular extract, purified enzyme, bead-bound immunocomplex, etc.). Deacetylation of the substrate sensitizes the substrate so that, in a second step, treatment with the FLUOR DE LYS® Developer produces a fluorophore. Histone deacetylases from all known classes have been successfully assayed with the FLUOR DE LYS® Substrate. These include human HDACs 1, 2, 3 and 8 (class I), human HDACs 4 and 9 (class II) and the sirtuins yeast Sir2, human SIRT1 and human SIRT2 (class III; reaction must include the sirtuin substrate NAD+). The substrate is cell-permeable and serves as the basis for the HDAC Cellular Activity Assay Kit (Prod. No. BML-AK503). NOTE: Must be used in conjunction with FLUOR DE LYS® Developer (Prod. No. BML-KI105). Sufficient for 100-1000 assays of HDACs or sirtuins (50 µl reaction volume, 50-500 µM (substrate).
Product Details
MW: | 387.4 |
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Quantity: | 2.5 µmol (50 µl) |
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Formulation: | Supplied as a 50 mM solution (50 µl) in dimethylsulfoxide (DMSO). |
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Purity: | ≥95% (HPLC) |
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Shipping: | Dry Ice |
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Long Term Storage: | -80°C |
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Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Identification of novel multi-stage histone deacetylase (HDAC) inhibitors that impair Schistosoma mansoni viability and egg production: A. Guidi, et al.; Parasit. Vectors
11, 668 (2018),
Abstract;
Divergent JNK Phosphorylation of HDAC3 in Triple-Negative Breast Cancer Cells Determines HDAC Inhibitor Binding and Selectivity: T.W. Hanigan, et al.; Cell Chem. Biol.
24, 1356 (2017),
Abstract;
Full Text
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
Histone deacetylase 1 plays a predominant pro-oncogenic role in Eμ-myc driven B cell lymphoma: V. Pillonel, et al.; Sci. Rep.
6, 37772 (2016),
Abstract;
Full Text
Histone deacetylase 1 plays a predominant pro-oncogenic role in Eµ-myc driven B cell lymphoma: V. Pillonel, et al.; Sci. Rep.
6, 37772 (2016),
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, et al.; Biochemistry
45, 4692 (2015),
Application(s): Inhibitory activity of acetylpolyamine amidohydrolase assay ,
Abstract;
Full Text
Mechanism of N-acylthiourea Mediated Activation of Human Histone Deacetylase 8 (HDAC8) at Molecular and Cellular levels: R. Singh, et al.; J. Biol. Chem.
290, 6607 (2015),
Application(s): HDAC8 catalyzed reaction of human neuroblastoma cells,
Abstract;
Full Text
Synthesis and evaluation of N⁸-acetylspermidine analogues as inhibitors of bacterial acetylpolyamine amidohydrolase: C. Decroos, et al.; Bioorg. Med. Chem.
21, 4530 (2013),
Application(s): APAH expression in E.coli analyzed using assay.,
Abstract;
Full Text
Histone deacetylase (HDAC) inhibitors targeting HDAC3 and HDAC1 ameliorate polyglutamine-elicited phenotypes in model systems of Huntington's disease: H. Jia, et al.; Neurobiol. Dis.
46, 351 (2012),
Abstract;
Improved Histone Deacetylase Inhibitors as Therapeutics for the Neurodegenerative Disease Friedreich’s Ataxia: A New Synthetic Route : C. Xu, et al.; Pharmaceuticals
4, 1578 (2011),
Application(s): Assay of human FRDA lymphoblastoid cells,
Abstract;
Full Text
General Literature References
A microplate reader-based nonisotopic histone deacetylase activity assay: B. Heltweg and M. Jung; Anal. Biochem.
302, 175 (2002),
Abstract;
A molecular mechanism of action of theophylline: Induction of histone deacetylase activity to decrease inflammatory gene expression: K. Ito et al.; PNAS
99, 8921 (2002),
Abstract;
Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1: K.J. Bitterman et al.; J. Biol. Chem.
277, 45099 (2002),
Abstract;
Proliferating cell nuclear antigen associates with histone deacetylase activity, integrating DNA replication and chromatin modification: S. Milutinovic et al.; J. Biol. Chem.
277, 20974 (2002),
Abstract;
Cloning and characterization of a histone deacetylase, HDAC9: X. Zhou et al.; PNAS
98, 10572 (2001),
Abstract;
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