LSD1 human recombinant

Human recombinant LSD1 expressed in E. Coli

LSD1 catalyzes the oxidative demethylation of mono- and dimethylated H3K4, 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 2. LSD1 is inhibited by a number of established monoamine oxidase inhibitor drugs. That and the fact that its expression is elevated in a number of cancers may make it a promising target for drug development.

Human recombinant LSD1 expressed in E. Coli.

>20U/μg. One U=1 pmol/min at 30ºC as determined by a Peroxidase-Coupled Assay with a Histone H3 dimethyl lysine 4 peptide.

Format: Purified

Purity: Purity >90% by SDS-PAGE

6 mM Na2HPO4, 1.1 mM K2HPO4, pH 7.2, 82 mM sodium chloride, 1.6 mM KCl and 40% glycerol. Frozen solution.

Stable for 12 months at -80ºC from date of receipt. The enzyme is stable on ice for 30 to 60 min, but may lose activity with prolonged storage on ice. It is recommended that thawing and dilution of the enzyme be done within as short a time as possible before start of the assay. The remaining, unused, undiluted enzyme should be refrozen quickly by, for example, snap freezing in a dry/ice ethanol bath or liquid nitrogen. Freezing and storage of diluted enzyme is not recommended.

6 mM Na2HPO4, 1.1 mM K2HPO4, pH 7.2, 82 mM sodium chloride, 1.6 mM KCl and 40% glycerol. Frozen solution.

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Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.