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LSD1 (human recombinant)

Cayman Chemical Item Number 10245

NPAO; AOF2; KDM1; p110b; BHC110; Lysine-Specific Demethylase 1

LSD1 (human recombinant)

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Description

Source: active human recombinant N-terminal His-tagged enzyme expressed in E. coli; BC048134 · Mr: 94 kDa · 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

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. Mol Cell 19 864 (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., and 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., and Chen, X. Protein methylation: A new mechanism of p53 tumor suppressor regulation. Histol Histopathol 23 1143-1149 (2008).

Synonyms
  • NPAO
  • AOF2
  • KDM1
  • p110b
  • BHC110
  • Lysine-Specific Demethylase 1
Formulation 50 mM sodium phosphate, pH 7.2 containing 100 mM sodium chloride and 20% glycerol
Purity ≥50%
Stability 6 months
Storage -80°C
Shipping Dry ice in continental US; may vary elsewhere

Background Reading

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).

Shi, Y., Matson, C., Lan, F., et al. Regulation of LSD1 histone demethylase activity by its associated factors. Mol Cell 19 864 (2005).

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).

Huang, J., Sengupta, R., Espejo, A.B., et al. p53 is regulated by the lysine demethylase LSD1. Nature 449 105-108 (2007).

Scoumanne, A., and 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).

Shi, Y., Lan, F., Matson, C., et al. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119 941-953 (2004).

Scoumanne, A., and Chen, X. Protein methylation: A new mechanism of p53 tumor suppressor regulation. Histol Histopathol 23 1143-1149 (2008).

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Size Price Quantity Subtotal
25 units $102.00 $0.00
50 units $194.00 $0.00
100 units $367.00 $0.00
Bulk Contact
Cart Total $0.00

This product is available in custom sizes and/or larger quantities.

Please contact our Sales Department for a quote or to purchase.

Pricing updated 2012-05-26. Prices are subject to change without notice.

To ask for assistance with one of our products please contact a Technical Support Scientist.

Warning This product is not for human or veterinary use.

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