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FLUOR DE LYS^®-HDAC8 deacetylase substrate

BML-KI178

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A fluorogenic, diacetylated peptide substrate for HDAC8 (histone deacetylase-8).

FLUOR DE LYS^®-HDAC8 is a fluorogenic, diacetylated peptide substrate for HDAC8 (histone deacetylase-8). Based on residues 379-382 of p53 (Arg-His-Lys(Ac)-Lys(Ac)), a site of regulatory acetylation by the p300 and CBP acetyltransferases (lysines 381, 382), it was the best for HDAC8 from among a panel of substrates patterned on p53, histone H3 and histone H4 acetylation sites. FLUOR DE LYS^®-HDAC8 is deacetylated by HDAC8 at a rate of more than 10-fold that of the acetylated lysine substrate, FLUOR DE LYS^® (BML-KI104; substrates both at 100 µM). Although named because of HDAC8’s preference for it, it is also an excellent substrate for SIRT1 (BMl-SE239; 5x the rate of BML-KI104 at 25 µM, 0.5 mM NAD⁺), SIRT2 and HeLa Nuclear Extract (BML-KI140; 3x KI-104 rate, 25 µM). Must be used in conjunction with FLUOR DE LYS^® Developer II (BML-KI176). Sufficient for 100-200 assays of human recombinant HDAC8 (BML-SE145; 1 U/well, 50-100 µM substrate).

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Product Details

Formulation	Supplied as a 5 mM solution (100 µl) in HDAC Assay Buffer.
Purity	≥95%

Handling & Storage

Use/Stability	As indicated on product label or CoA when stored as recommended.
Long Term Storage	-80°C
Shipping	Dry Ice

Regulatory Status	RUO – Research Use Only

Synthesis, Biochemical, and Cellular Evaluation of HDAC6 Targeting Proteolysis Targeting Chimeras: S. Darwish, et al.; Methods Mol. Biol. 2023, 2589 (2023), Abstract
Species-selective targeting of pathogens revealed by the atypical structure and active site of Trypanosoma cruzi histone deacetylase DAC2: M. Marek, et al.; Cell Reports 37, 110129 (2021), Abstract
High-throughput screening of histone deacetylases and determination of kinetic parameters using fluorogenic assays: C. Moreno-Yruela, et al.; STAR Protoc. 2, 100313 (2021), Application(s): HTS protocol to identify deacylase activities, Abstract — Full Text
The Contribution of Romidepsin to the Herbicidal Activity of Burkholderia rinojensis Biopesticide: D.K. Owens, et al.; J. Nat. Prod. 83, 843 (2020), Abstract
A Novel Class of Schistosoma mansoni Histone Deacetylase 8 (HDAC8) Inhibitors Identified by Structure-Based Virtual Screening and In Vitro Testing: C.V. Simoben, et al.; Molecules 23, E566 (2018), Abstract — Full Text
Carbamates as Potential Prodrugs and a New Warhead for HDAC Inhibition: K. King, et al.; Molecules 23, E321 (2018), Abstract — Full Text
Structural and Functional Influence of the Glycine-Rich Loop G302GGGY on the Catalytic Tyrosine of Histone Deacetylase 8: N.J. Porter, et al.; Biochemistry. 55, 6718 (2016), Reactant(s): E. coli, Abstract
Structure-Based Design and Synthesis of Novel Inhibitors Targeting HDAC8 from Schistosoma mansoni for the Treatment of Schistosomiasis: T. Heimburg, et al.; J. Med. Chem. 59, 2423 (2016), Application(s): Enzyme activity assays, Abstract — Full Text
General Base-General Acid Catalysis in Human Histone Deacetylase 8: S.M. Gantt, et al.; Biochemistry 55, 820 (2016), Abstract — Full Text
Selective Sirt2 inhibition by ligand-induced rearrangement of the active site: T. Rumpf, et al.; Nat. Commun. 6, 6263 (2015), Abstract — Full Text