Online Purchasing Account You are logged on as Guest. LoginRegister a New AccountShopping cart (Empty)
United States 

FLUOR DE LYS® HDAC1 fluorometric drug discovery assay kit

BML-AK511-0001 96 wells 864.00 USD
Do you need bulk/larger quantities?
  • 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.
FLUOR DE LYS® HDAC1 fluorometric drug discovery assay kit image
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.
Please mouse over
FLUOR DE LYS® HDAC1 fluorometric drug discovery assay kit image

Product Details

Alternative Name:Histone deacetylase 1 fluorescent assay kit
Applications:Fluorescent detection, HTS
Activity assay, Cell-based assays
Use/Stability: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.
Shipping:Dry Ice
Long Term Storage:-80°C
Contents:HDAC1 (Histone Deacetylase 1) (human, recombinant) (Prod. No. (BML-SE456)
(50 µg; 10mM TRIS, pH 7.5, 100mM sodium chloride, 3mM magnesium chloride, 10% glycerol)
Storage: -80°C, avoid freeze/thaw cycles
FLUOR DE LYS® SIRT1, Deacetylase Substrate (Prod. No. BML-KI177)
(100µl; 5mM solution in 50mM TRIS/Cl, pH 8.0, 137mM sodium chloride, 2.7mM potassium chloride, 1mM magnesium chloride)
Storage: -80°C
FLUOR DE LYS® Developer II Concentrate (5x) (Prod. No. BML-KI176)
(5 x 250 µl; 5x Stock Solution; Dilute in Assay Buffer before use)
Storage: -80°C
Trichostatin A (HDAC Inhibitor) (Prod. No. BML-GR-309-9090)
(100 µl; 0.2mM in DMSO)
Storage: -80°C
FLUOR DE LYS® Deacetylated Standard (Prod. No. BML-KI142)
(30 µl; 10mM in DMSO)
Storage: -80°C
HDAC Assay Buffer II (50mM TRIS/Cl, pH 8.0, 137mM sodium chloride, 2.7mM potassium chloride, 1mM magnesium chloride, 1mg/ml bovine serum albumin) (Prod. No. BML-KI422)
(20 ml)
Storage: -20°C (or -80°C)
HDAC Assay Buffer (50mM TRIS/Cl, pH 8.0, 137mM sodium chloride, 2.7mM potassium chloride, 1mM magnesium chloride) (Prod. No. BML-KI143)
(20 ml)
Storage: -20°C (or -80°C)
1/2 Volume Microplates (Prod. No. 80-2407)
1 clear and 1 white, 96-well
Storage: Ambient
Scientific Background: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

Apigenin Alleviates Oxidative Stress-Induced Cellular Senescence via Modulation of the SIRT1-NAD-CD38 Axis: B.S. Li, et al.; Am. J. Chin. Med. 49, 1235 (2021), Abstract;
Synthesis and Biological Evaluation of HDAC Inhibitors With a Novel Zinc Binding Group: J. He, et al.; Front. Chem. 8, 256 (2020), Abstract; Full Text
Evaluation of WO2017018805: 1,3,4-oxadiazole sulfamide derivatives as selective HDAC6 inhibitors: Y.Y. Liang, et al.; Expert Opin. Ther. Pat. 28, 647 (2018), Abstract;
New 5-Aryl-Substituted 2-Aminobenzamide-Type HDAC Inhibitors with a Diketopiperazine Group and Their Ameliorating Effects on Ischemia-Induced Neuronal Cell Death: Y. Hirata, et al.; Sci. Rep. 8, 1400 (2018), Abstract; Full Text
Reverse Biosynthesis: Generating Combinatorial Pools of Drug Leads from Enzyme-Mediated Fragmentation of Natural Products: T. Richardson-Sanchez, et al.; Chembiochem 18, 368 (2017), Abstract;
Computer-aided identification of new histone deacetylase 6 selective inhibitor with anti-sepsis activity: J. Yoo, et al.; Eur. J. Med. Chem. 116, 126 (2016), Abstract;
Influence of the carbamate fungicide benomyl on the gene expression and activity of aromatase in the human breast carcinoma cell line MCF-7: Y. Kawaratani, et al.; Environ. Toxicol. Pharmacol. 39, 292 (2015), Abstract;
Targeting the invasive phenotype of cisplatin-resistant Non-Small Cell Lung Cancer cells by a novel histone deacetylase inhibitor: V. Zuco, et al.; Biochem. Pharmacol. 94, 79 (2015), Application(s): Assay, Abstract;
Design, synthesis, and biological activity of NCC149 derivatives as histone deacetylase 8-selective inhibitors: T. Suzuki, et al.; ChemMedChem. 9, 657 (2014), Abstract;
Inhibition of HDAC3 promotes ligand-independent PPARγ activation by protein acetylation: X. Jiang, et al.; J. Mol. Endocrinol. 53, 191 (2014), Abstract;
A novel series of l-2-benzyloxycarbonylamino-8-(2-pyridyl)-disulfidyloctanoic acid derivatives as histone deacetylase inhibitors: design, synthesis and molecular modeling study: D. Huang, et al.; Eur. J. Med. Chem. 52, 111 (2012), Abstract;
Anti-tumor activity of new orally bioavailable 2-amino-5-(thiophen-2-yl)benzamide-series histone deacetylase inhibitors, possessing an aqueous soluble functional group as a surface recognition domain: Y. Hirata, et al.; Bioorg. Med. Chem. Lett. 22, 1926 (2012), Abstract;
Synthesis, evaluation and molecular modeling of cyclic tetrapeptide histone deacetylase inhibitors as anticancer agents: D. Huang, et al.; J. Pep. Sci. 18, 242 (2012), Abstract;
Targeting metalloproteins by fragment-based lead discovery: S. Johnson, et al.; Chem. Biol. Drug Des. 78, 211 (2011), Abstract; Full Text

General Literature References

Histone deacetylase inhibitors: molecular mechanisms of action: W.S. Xu, et al.; Oncogene 26, 5541 (2007), Abstract;
Endogenous inhibition of histone deacetylase 1 by tumor-suppressive maspin: X. Li, et al.; Cancer Res. 66, 9323 (2006), Abstract;
Histone deacetylase 3 (HDAC3) and other class I HDACs regulate colon cell maturation and p21 expression and are deregulated in human colon cancer: A.J. Wilsone, et al.; J. Biol. Chem. 281, 13548 (2006), Abstract;
Acetylation and deacetylation of non-histone proteins: M.A. Glozak, et al.; Gene 363, 15 (2005), Abstract;
Quantitation of HDAC1 mRNA expression in invasive carcinoma of the breast*: Z. Zhang, et al.; Breast Cancer Res. Treat. 94, 11 (2005), Abstract;
Upregulation and nuclear recruitment of HDAC1 in hormone refractory prostate cancer: K. Halkidou, et al.; Prostate 59, 177 (2004), Abstract;
Histone deacetylases (HDACs): characterization of the classical HDAC family: A.J. de Ruijter; Biochem. J. 370, 737 (2003), Abstract;
N-CoR-HDAC corepressor complexes: roles in transcriptional regulation by nuclear hormone receptors: P.L. Jones, et al.; Curr. Top. Microbiol. Immunol. 274, 237 (2003), Abstract;
SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities: G. David, et al.; J. Biol. Chem. 277, 23658 (2002), Abstract;
Cloning and characterization of a histone deacetylase, HDAC9: X. Zhou, et al.; PNAS 98, 10572 (2001), Abstract;
CoREST is an integral component of the CoREST- human histone deacetylase complex: A. You, et al.; PNAS 98, 1454 (2001), Abstract;
Expression profile of histone deacetylase 1 in gastric cancer tissues: J.H. Choi, et al.; Jpn. J. Cancer Res. 92, 1300 (2001), Abstract;
Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation: M.K. Pflum, et al.; J. Biol. Chem. 276, 47733 (2001), Abstract;
Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1: G.W. Humphrey; J. Biol. Chem. 276, 6817 (2001), Abstract;
Acetylation and chromosomal functions: W.L. Cheung et al.; Curr. Opin. Cell. Biol. 12, 326 (2000), Abstract;
Cloning and characterization of a novel human class I histone deacetylase that functions as a transcription repressor: E. Hu, et al.; J. Biol. Chem. 275, 15254 (2000), Abstract;
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;
Enzymatic deacetylation of histone: A. Inoue, et al.; Biochem. Biophys. Res. Commun. 36, 146 (1969), Abstract;

Related Products

FLUOR DE LYS®-Green HDAC2 fluorometric drug discovery assay kit 

Fluorescent detection, HTS, Activity assay, Cell-based assays | Print as PDF
BML-AK512-0001 96 wells 866.00 USD
Do you need bulk/larger quantities?

FLUOR DE LYS® HDAC fluorometric cellular activity assay kit 

Monitor HDAC activity in cell culture using cell-permeable FLUOR DE LYS® substrate
Fluorescent detection, HTS, Activity assay, Cell-based assays | Print as PDF
BML-AK503-0001 96 wells 587.00 USD
Do you need bulk/larger quantities?

FLUOR DE LYS® HDAC fluorometric activity assay kit 

First-to-market by the leader in Epigenetics research tools
Fluorescent detection, HTS, Activity assay | Print as PDF
BML-AK500-0001 96 wells 638.00 USD
Do you need bulk/larger quantities?

FLUOR DE LYS®-Green HDAC fluorometric activity assay kit 

Fluorescent detection, HTS, Activity assay, Cell-based assays | Print as PDF
BML-AK530-0001 96 wells Inquire for pricing
Do you need bulk/larger quantities?

HDAC1 (human), (recombinant) (His-tag) 

Highly active
Produced in insect cells. HDAC1 from human cDNA (482 aa). Produced in a baculovirus expression system. | Print as PDF
BML-SE456-0050 50 µg 569.00 USD
Do you need bulk/larger quantities?

Related Literature

Stem Cells
Stem Cells
Download as PDF

Download as PDF

All new literature pieces