| 货号 | 11299-100ug |
| 描述 | Methylation of lysine residues of core histones plays a critical role in the regulation of gene expression.1 Jumonji domain containing 2A (JMJD2A) is the first reported trimethyllysine-specific histone demethylase.2 It catalyzes the demethylation of trimethylated forms of histone at lysine residues 9 and 36. Like other JmjC protein hydroxylase family members, JMJD2A is an α-ketoglutarate-dependent Fe (II) oxygenase.3 Purification of Fe-dependent JmjC family members by IMAC can result in displacement of the catalytic iron and decreased activity, therefore this Strep-tagged protein is purified by affinity chromatography using Strep-Tactin coated resin.4 JMJD2A’s transcriptional function appears to depend on protein associations, as it is implicated in both transcriptional silencing and upregulation of the androgen receptor-dependent genes.2 Because of their implication in cancer cell growth, jumonji C domain-containing histone demethylases may be drug discovery targets for therapeutic intervention.1 |
| 别名 | JHDM3A;Jumonji Domain Containing 2A;KDM4A; |
| 供应商 | Cayman |
| 应用文献 | |
| 1.Hamada, S.,Kim, T.D.,Suzuki, T., et al. Synthesis and activity of N-oxalylglycine and its derivatives as Jumonji C-domain-containing histone lysine demethylase inhibitors. Bioorganic & Medicinal Chemistry Letters 19, 2852-2855 (2009). 2.Marmorstein, R. and Trievel, R.C. Histone modifying enzymes: Structures, mechanisms, and specificities. Biochimica et Biophysica Acta 1789, 58-68 (2009). 3.Couture, J.F.,Collazo, E.,Ortiz-Tello, P.A., et al. Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Nature Structural & Molecular Biology 14(8), 689-695 (2007). 4.Krishnan, S.,Collazo, E.,Ortiz-Tello, P.A., et al. Purification and assay protocols for obtaining highly active Jumonji C demethylases. Analytical Biochemistry 420, 48-53 (2012). | |
| 运输条件 | Dry ice in continental US; may vary elsewhere |
| 存放说明 | -80 |
| 纯度 | ≥95% estimated by SDS-PAGE |
| 稳定性 | ≥ 6 months |
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