| 货号 | 9001953-100ug |
| 描述 | Tudor domains are small protein structural motifs of ~50 amino acids related to the “royal family” of methyl readers, which also includes chromo, MBT, PWWP, and Agenet-like domains.1,2 Tudor domains occur either alone, in tandem, or with other domains and are found in many proteins that are involved in RNA metabolism, germ cell development, transposon silencing, DNA damage response, histone modification, and chromatin remodeling.3 The tudor domains recognize symmetric methylated arginine or methylated lysine residues.4,5,6,7JMJD2C is an α-ketoglutarate-dependent Fe (II) oxygenase that catalyzes the demethylation of trimethylated histone H3 at lysine residues 9 and 36 (H3K9me3 and H3K36me3).8 This protein product contains the tandem tudor domains of JMJD2C |
| 别名 | GASC-1 Protein;KDM4C;Lysine-specific Demethylase 4C;JmjC Domain-containing Histone Demethylation Protein 3C;Jumonji Domain-containing Protein 2C; |
| 供应商 | Cayman |
| 应用文献 | |
| 1.Maurer-Stroh, S.,Dickens, N.J.,Hughes-Davies, L., et al. The Tudor domain Royal Family: Tudor, plant Agenet, Chromo, PWWP and MBT domains. Trends in Biochemical Sciences 28(2), 69-74 (2003). 2.Chen, C.,Nott, T.J.,Jin, J., et al. Deciphering arginine methylation: Tudor tells the tale. Nature Reviews.Molecular Cell Biology 12(10), 629-642 (2011). 3.Kim, J.,Daniel, J.,Espejo, A., et al. Tudor, MBT and chromo domains gauge the degree of lysine methylation. EMBO reports 7(4), 397-403 (2006). 4.Pedersen, M.T.,Agger, K.,Laugesen, A., et al. The demethylase JMJD2C localizes to H3K4me3-positive transcription start sites and is dispensable for embryonic development. Molecular and Cellular Biology 34(6), 1031-1045 (2014). | |
| 运输条件 | Dry ice in continental US; may vary elsewhere |
| 存放说明 | -80 |
| 纯度 | estimated by SDS-PAGE |
| 稳定性 | ≥ 6 months |
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