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LSD1 fluorometric drug discovery kit

BML-AK544-0001 96 wells 369.00 USD
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The LSD1 Fluorimetric Drug Discovery Kit provides human recombinant LSD1 and all reagents for measuring its activity in a sensitive, real-time fluorescent assay. LSD1 catalyzed demethylation of the Histone H3 Dimethyl Lysine-4 Peptide (H3K4Me2 Peptide; Prod. No. BML-P256) produces hydrogen peroxide. A fluorescent signal is generated via the horseradish peroxidase (HRP) catalyzed reaction of the hydrogen peroxide with the CELLESTIAL® Red Peroxidase Substrate (Prod. No. BML-KI565). Although fluorescence detection will be more sensitive (Excitation in range of 530-570 nm; Emission ca. 590 nm), the CELLESTIAL® Red peroxidation product may also be detected by following absorbance (see "Detection by Absorbance at 563 nm").

Product Specification

Alternative Name:Lysine-specific Histone Demethylase 1, KDM1, AOF2
Applications:Fluorescent detection, HTS
Activity assay, Cell-based assays
Shipping:Shipped on Dry Ice
Long Term Storage:-80°C
Contents:Recombinant human LSD1 (50µg, >1000U)
Histone H3 Dimethyl Lysine-4 Peptide Substrate
CELLESTIAL® Red Peroxidase Substrate
Horseradish Peroxidase
H2O2 Standard
Tranylcypromine (LSD1 inhibitor)
Black and clear 1/2-vol. 96-well plates
Detailed instructions
Scientific Background:LSD1 (aka KDM1; lysine-specific histone demethylase 1; AOF2), a flavin-containing amine oxidase homolog and component of various corepressor complexes, was the first enzyme demonstrated to be capable of lysine demethylation1. LSD1 catalyzes the oxidative demethylation of mono- and dimethylated histone 3 lysine-4 (H3K4Me2/1), producing hydrogen peroxide and formaldehyde in the process. H3K4 methylation is considered a transcription-activating chromatin mark and, in vivo, LSD1 is frequently found in association with the transcriptional corepressor protein CoREST and HDACs 1 or 23. LSD1 is inhibited by a number of established monoamine oxidase inhibitor drugs, including tranylcypromine. That and the fact that its expression is elevated in a number of cancers may make it a promising target for drug development.
UniProt ID:O60341

Product Literature References

Design, synthesis, and biological evaluation of a conjugate of 5-fluorouracil and an LSD1 inhibitor: Y. Ota, et al.; Chem. Pharm. Bull. 67, 192 (2019), Abstract;
Design, synthesis and evaluation of γ-turn mimetics as LSD1-selective inhibitors: Y. Ota, et al.; Bioorg. Med. Chem. 26, 775 (2018), Abstract;
Design, Synthesis, and In Vitro Evaluation of Novel Histone H3 Peptide-Based LSD1 Inactivators Incorporating α,α-Disubstituted Amino Acids with γ-Turn-Inducing Structures: Y. Ota, et al.; Molecules 23, E1099 (2018), Abstract; Full Text
Histone H3 peptides incorporating modified lysine residues as lysine-specific demethylase 1 inhibitors: T. Kakizawa, et al.; Bioorg. Med. Chem. Lett. 28, 167 (2018), Abstract;
Identification of JL1037 as a novel, specific, reversible lysine-specific demethylase 1 inhibitor that induce apoptosis and autophagy of AML cells: S. Liu, et al.; Oncotarget 8, 31901 (2017), Abstract; Full Text
LSD1 Substrate Binding and Gene Expression Are Affected by HDAC1-Mediated Deacetylation: D.A. Nalawansha, et al.; ACS Chem. Biol. 12, 254 (2017), Abstract; Full Text
C-H activation enables a rapid structure-activity relationship study of arylcyclopropyl amines for potent and selective LSD1 inhibitors: S. Miyamura, et al.; Org. Biomol. Chem. 14, 8576 (2016), Abstract;

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