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- Tel: 858.663.9055
- Email: info@nsjbio.com
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LSD1 is a histone demethylase that specifically demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. LSD1 contains a SWIRM domain, a FAD-binding motif, and an amine oxidase domain. This protein is a component of several histone deacetylase complexes, though it silences genes by functioning as a histone demethylase. It acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. LSD1 demethylates both mono- and tri-methylted 'Lys-4' of histone H3. This protein may play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3 'Lys-4' on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. It may also demethylate 'Lys-9' of histone H3, a specific tag for epigenetic transcriptional repression, thereby leading to derepression of androgen receptor target genes.
Titration of the LSD1 antibody may be required due to differences in protocols and secondary/substrate sensitivity.
A portion of amino acids 457-490 from the human protein was used as the immunogen for this LSD1 antibody.
Aliquot the LSD1 antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
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