Useful for inhibitor screening or characterizing enzyme kinetics
Includes optimal substrate selected from a panel of acetylated sites in p53 and histones
Supplied with enough recombinant enzyme for 96 assays (1 x 96-well plate)
A FLUOR DE LYS® fluorescent assay system. The HDAC1 Fluorescent Activity Assay/Drug Discovery Kit is a complete assay system designed to measure the lysyl deacetylase activity of the recombinant human HDAC1 included in the kit. The kit is ideal for chemical library screening for candidate inhibitors or kinetic assay of the enzyme under varying conditions. The FLUOR DE LYS® HDAC1 assay is based on the FLUOR DE LYS® Substrate and FLUOR DE LYS® Developer combination. The assay procedure has two steps. First, the FLUOR DE LYS® Substrate, which comprises an acetylated lysine side chain, is incubated with HDAC1. Deacetylation of the substrate sensitizes the substrate so that, in the second step, treatment with the FLUOR DE LYS®Developer produces a fluorophore.
Figure: Reaction Scheme of the HDAC1 Fluorimetric Activity Assay*. Deacetylation of the substrate sensitizes it to the Developer II, which then generates a fluorophore (symbol). The fluorophore is excited with 360 nm light and the emitted light (460 nm) is detected on a fluorometric plate reader.
Store all components except the microplate and instruction booklet at -80°C for the highest stability. The HDAC1 Enzyme (Prod. No. BML-SE456), must be handled with particular care in order to retain maximum enzymatic activity. Defrost it quickly in a RT water bath or by rubbing between fingers, then immediately store on an ice bath. The remaining unused enzyme should be refrozen quickly, by placing at -80°C. If possible, snap freeze in liquid nitrogen or a dry ice/ethanol bath. To minimize the number of freeze/thaw cycles, aliquot the enzyme into separate tubes and store at -80°C.
Human HDAC1 (HD1) was the first protein to be linked to histone deacetylase activity. It is homologous to the yeast protein Rpd3, a relationship which has since come to define the “class I HDACs”. HDAC1 promotes transcriptional repression by deacetylating lysine ε-amino groups in histone N-terminal tails, a function frequently carried out in association with multi-protein transcription repression complexes such as NuRD, Sin3> and CoREST. Ubiquitously expressed in human tissues, HDAC1-containing complexes appear to contribute the greater part of (at least class I) deacetylase activity in HeLa nuclear extracts. Aside from its interaction with co-repressors, HDAC1 activity may be regulated by post-translation modifications such as phosphorylation and sumoylation or binding to the inhibitor maspin, a tumor-suppressive serpin homolog. Although originally described as a “histone deacetylase”, HDAC1 has been shown to catalyze the regulatory deacetylation of non-histone proteins, including p53. Overexpression of HDAC1 has been found in various cancer types. HDAC inhibitors (HDACi) have shown considerable promise as anti-cancer agents and HDACi compounds from multiple chemical classes are in stages of drug development ranging from preclinical to phase III trials. HDAC inhibitors have shown promise as anti-tumor agents and naturally this has stimulated interest in the screening of compounds for HDAC1 inhibition.
UniProt ID:
Q13547
Regulatory Status:
RUO - Research Use Only
Product Literature References
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General Literature References
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Deacetylation of p53 modulates its effect on cell growth and apoptosis: J. Luo, et al.; Nature 408, 377 (2000), Abstract;
Histone deacetylases specifically down-regulate p53-dependent gene activation: L.J. Juan, et al.; J. Biol. Chem. 275, 20436 (2000), Abstract;
Histone deacetylases: silencers for hire: H.H. Ng, et al.; Trends. Biochem. Sci. 25, 121 (2000), Abstract;
Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression: H.-Y. Kao, et al.; Genes Dev. 14, 55 (2000), Abstract;
The language of covalent histone modifications: B.D. Strahl, et al.; Nature 403, 41 (2000), Abstract;
A new family of human histone deacetylases related to Saccharomyces cerevisiae HDA1p: W. Fischle, et al.; J. Biol. Chem. 274, 11713 (1999), Abstract;
HDAC4, a human histone deacetylase related to yeast HDA1, is a transcriptional corepressor: A.H. Wang, et al.; Mol. Cell. Biol. 19, 7816 (1999), Abstract;
Identification of a new family of higher eukaryotic histone deacetylases. Coordinate expression of differentiation-dependent chromatin modifiers: A. Verdel, et al.; J. Biol. Chem. 274, 2440 (1999), Abstract;
Purification of a histone deacetylase complex from Xenopus laevis: preparation of substrates and assay procedures: P.A. Wade, et al.; Methods Enzymol. 304, 715 (1999), Abstract;
Three proteins define a class of human histone deacetylases related to yeast Hda1p: C.M. Grozinger, et al.; PNAS 96, 4868 (1999), Abstract;
SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex: Y. Zhang, et al.; Mol. Cell 1, 1021 (1998), Abstract;
Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo: D. Kadosh, et al.; Mol. Cell Biol. 18, 5121 (1998), Abstract;
Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3: S.E.C. Rundlett, et al.; Nature 392, 831 (1998), Abstract;
Histone acetylation in chromatin structure and transcription: M. Grunstein; Nature 389, 349 (1997), Abstract;
Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression: C.D. Laherty, et al.; Cell 89, 349 (1997), Abstract;
Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family: W.M. Yang, et al.; J. Biol. Chem. 272, 28001 (1997), Abstract;
A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p: J. Taunton, et al.; Science 272, 408 (1996), Abstract;
Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3: W.M. Yang, et al.; PNAS 93, 12845 (1996), Abstract;
Bloodletting at weizhong point (UB 40) for treatment of acute lumbar sprain: Y. Zhang, et al.; J. Tradit. Chin. Med. 13, 192 (1993), Abstract;
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