
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.
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Informations pour la commande
| Nom du produit | Ref. Catalogue | COND. | Prix HT | QTÉ | Favoris | |
Anticorps LSD1 (1B2E5) | sc-53875 | 200 µg/ml | $322.00 | |||
LSD1 (1B2E5): m-IgGκ BP-HRP Kit | sc-520995 | 200 µg Ab, 40 µg BP | $361.00 |