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Source:
human recombinant N-terminal hexahistidine tagged enzyme expressed in E. coli; BC048134
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Mr:
94 kDa
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LSD1 belongs to the family of flavin adenine dinucleotide (FAD)-dependent amine oxidases that include monoamine oxidases (MAOs) and polyamine oxidase (PAO).1 LSD1 is a component of several histone deacetylase co-repressor complexes, including histone deacetylases 1 and 2, CtBP, and the neuronal CoREST complexes.2 LSD1, with the help of its cofactor CoREST, specifically demethylates mono- and dimethylated histone H3 lysine 4 (H3-K4), resulting in transcriptional repression.3 In addition to demethylating histones, LSD1 controls the tumor suppressor activity of p53 by demethylating a specific p53 lysine residue (LYS370). 4 This activity does not seem to require CoREST and p53 demethylation of LYS370 prevents p53 interaction with its co-activator 53BP1 to induce apoptosis. 4,5,6,7
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1
Shi, Y., Lan, F., Matson, C., et al. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119 941-953 (2004).
2
Shi, Y., Matson, C., Lan, F., et al. Regulation of LSD1 histone demethylase activity by its associated factors. Molecular Cell 19 864-864 (2005).
3
Forneris, F., Binda, C., Vanoni, M.A., et al. Human histone demethylase LSD1 reads the histone code. J Biol Chem 280(50) 41360-41365 (2005).
4
Huang, J., Sengupta, R., Espejo, A.B., et al. p53 is regulated by the lysine demethylase LSD1. Nature 449 105-108 (2007).
5
Scoumanne, A., Chen, X. The lysine-specific demethylase 1 is required for cell proliferation in both p53-dependent and -independent manners. J Biol Chem 282(21) 15471-15475 (2007).
6
Tsai, W., Nguyen, T.T., Shi, Y., et al. p53-targeted LSD1 functions in repression of chromatin structure and transcription in vivo. Mol Cell Biol 28(17) 5139-5146 (2008).
7
Scoumanne, A., Chen, X. Protein methylation: A new mechanism of p53 tumor suppressor regulation. Histol Histopathol 23 1143-1149 (2008).
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