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FLUOR DE LYS® HDAC8 fluorometric drug discovery kit

BML-AK518-0001 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 HDAC8 Fluorescent Activity Assay/Drug Discovery Kit is a complete assay system designed to measure the lysyl deacetylase activity of the recombinant human HDAC8 included in the kit. The kit is ideal for chemical library screening for candidate inhibitors or activators or kinetic assay of the enzyme under varying conditions. The FLUOR DE LYS® HDAC8 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 HDAC6. Deacetylation of the substrate sensitizes the substrate so that, in the second step, treatment with the FLUOR DE LYS® Developer produces a fluorophore.

Product Details

Alternative Name:Histone deacetylase 8 fluorescent assay kit
Applications:Fluorescent detection, HTS
Activity assay, Cell-based assays
Shipping:Dry Ice
Long Term Storage:-80°C
Contents:HDAC8 (human) (recombinant)
FLUOR DE LYS®-HDAC8 substrate and developer II
Assay buffer
Trichostatin A (HDAC inhibitor)
White and clear 1/2-vol. 96-well plates, detailed instructions
Scientific Background:Although early studies suggested that HDAC8 (histone deacetylase 8) localized to the nucleus and was ubiquitously expressed, subsequent work indicates that in normal tissue it is primarily cytosolic and expressed in smooth muscle cells. However, like other class I HDACs, HDAC8 exhibits trichostatin A-inhibitable histone deacetylase activity and can mediate transcription repression. A crystal structure has been obtained for HDAC8 complexed with another, more potent inhibitor in the trichostatin class (hydroxamic acids). HDAC8 localizes to stress-fibers, along with smooth muscle a-actin and its expression appears to be essential for smooth muscle contractility. This affinity for cytoskeletal proteins may underlie HDAC8’s binding to the core binding factor β/smooth muscle myosin heavy chain fusion protein (CBFβ/SMMHC), which is created by the inversion(16) chromosomal translocation (inv(16)). CBFβ/SMMHC can associate with the mSin3A corepressor and may thereby act as a dominant repressor of genes regulated by CBFβ-AML1. Repression of these genes, which in the case of inv(16) would appear to be mediated by HDAC8 activity, is implicated in the genesis of acute myeloid leukemia (AML). siRNA-knockdown of HDAC8 expression has been shown to inhibit the growth of several human tumor cell lines, suggesting that HDAC8 activity may be significant in the pathogenesis of solid as well as hematologic tumors.
UniProt ID:Q9BY41
Regulatory Status:RUO - Research Use Only

Product Literature References

Crystal structures of Schistosoma mansoni histone deacetylase 8 reveal a novel binding site for allosteric inhibitors: F. Saccoccia, et al.; J. Biol. Chem. 298, 102375 (2022), Abstract;
Harnessing the Role of HDAC6 in Idiopathic Pulmonary Fibrosis: Design, Synthesis, Structural Analysis, and Biological Evaluation of Potent Inhibitors: G. Campiani, et al.; J. Med. Chem. 64, 9960 (2021), Abstract;
Kinetic Characterization of Human Histone Deacetylase 8 With Medium-Chain Fatty Acyl Lysine: H. Yoo & G.A. Polsinelli; Epigenet. Insights 14, 25168657211065685 (2021), Abstract;
Overexpressed HDAC8 in cervical cancer cells shows functional redundancy of tubulin deacetylation with HDAC6: G.R. Vanaja, et al.; Cell Commun. Signal. 16, 20 (2018), Abstract; Full Text
Acetanilide and bromoacetyl-lysine derivatives as activators for human histone deacetylase 8: Y.M. Mukhtar, et al.; Bioorg. Med. Chem. Lett. 27, 2319 (2017), Abstract;
Docking and QSAR Studies of Aryl-valproic Acid Derivatives to Identify Antiproliferative Agents Targeting the HDAC8: H. Martinez-Pacheco, et al.; Anticancer Agents Med. Chem. 17, 927 (2017), Abstract;
Screening and profiling assays for HDACs and sirtuins: K.T. Howitz, et al.; Drug. Discov. Today Technol. 18, 38 (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;
Tenovin-D3, a novel small-molecule inhibitor of sirtuin SirT2, increases p21 (CDKN1A) expression in a p53-independent manner: A.R. McCarthy, et al.; Mol. Cancer Ther. 12, 352 (2013), Abstract; Full Text
Acetylation of heat shock protein 20 (Hsp20) regulates human myometrial activity: M. Karolczak-Bayatti, et al.; J. Biol. Chem. 286, 34346 (2011), Abstract; Full Text
Targeting metalloproteins by fragment-based lead discovery: S. Johnson, et al.; Chem. Biol. Drug Des. 78, 211 (2011), Abstract; Full Text
The histone deacetylase inhibitor ITF2357 decreases surface CXCR4 and CCR5 expression on CD4(+) T-cells and monocytes and is superior to valproic acid for latent HIV-1 expression in vitro: S. Matalon, et al.; J. Acquir. Immune Defic. Syndr. 54, 1 (2010), Application(s): HDAC8 inhibition assay on HIV-infected cells, Abstract; Full Text

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