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FLUOR DE LYS® deacetylase substrate

Highly sensitive and convenient alternative to radiolabeled, acetylated histones or peptide/HPLC methods for the assay of histone deacetylases.
 
BML-KI104-0050 50 µl 170.00 USD
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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 Specification

MW:387.4
 
Quantity:2.5 µmol (50 µl)
 
Formulation:Supplied as a 50 mM solution (50 µl) in dimethylsulfoxide (DMSO).
 
Purity:≥95% (HPLC)
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 

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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