LSD1 polyclonal antibody

Histone methylation regulates chromatin structure and transcription and maintains an epigenetic state of the cell. Histone methylation is dynamically regulated by histone methylases and demethylases. Lysine-specific histone demethylase 1 (LSD1), also designated BHC110, is a flavin-dependent amine oxidase which catalyzes the removal of one or two methyl groups from the methyl-lysine-4 side chain of Histone H3. The LSD1 protein contains a SWIRM domain, a FAD-binding motif and an amine oxidase domain. Association with CoREST, a SANT domain-containing corepressor, positively regulates LSD1. CoREST mediates the demethylation ability of LSD1 and protects it from proteasomal degradation in vivo. PHF21A (also designated BCH80), a PHD domain-containing protein, inhibits activity of LSD1/CoREST mediated de-methylation. The LSD1 protein also co-localizes with the androgen receptor in human prostate tumor cells and in unaffected prostate cells, stimulating androgen-receptor-dependent transcription.