Residues 1-21 from the N-terminal tail of human histone H3, dimethylated on the side-chain (ε-amino function) of Lys4. Useful as a substrate for histone lysine demethylases, for example LSD1.
Product Details
| Sequence: | Ala-Arg-Thr-Lys(Me2) Gln-Thr-Ala-Arg-Lys-Ser-Thr-Gly-Gly-Lys-Ala-Pro-Arg-Lys-Gln-Leu-Ala- NH2 |
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| MW: | 2281.5 |
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| Formulation: | Lyophilized. |
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| Purity: | ≥95% (HPLC) |
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| Appearance: | Lyophilized solid. |
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| Solubility: | Soluble in Water. |
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| Shipping: | Blue Ice |
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| Long Term Storage: | -20°C |
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| Regulatory Status: | RUO - Research Use Only |
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Product Literature References
Histone H3 lysine 4 demethylation is a target of nonselective antidepressive medications: M.G. Lee, et al.; Chem. Biol.
13, 563 (2006),
Abstract;
Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process: F. Forneris, et al.; FEBS Lett.
579, 2203 (2005),
Abstract;
Human histone demethylase LSD1 reads the histone code: F. Forneris, et al.; J. Biol. Chem.
280, 41360 (2005),
Abstract;
Full Text
Histone demethylation mediated by the nuclear amine oxidase homolog LSD1: Y. Shi, et al.; Cell
119, 941 (2004),
Abstract;
