| 货号 | 10319-100ug |
| 描述 | Methylation of lysine can promote transcriptional activation or repression and is critical in regulating histone function. Lysine residues can be mono-, di-, or tri-methylated.1 SET8 selectively mono-methylates histone H4 at lysine 20, an event proven to have an important role in chromatin structure and transcriptional activation.2,3 SET8 is also a novel regulator of p53, mono-methylating lysine 382 of the tumor suppressor.4 SET8’s ability to suppress p53 transcriptional activity implies that it may play a significant role in tumorigenesis. |
| 别名 | KMT5a;PR-Set7;SETD8;SET domain-containing (lysine methyltransferase) 8; |
| 供应商 | Cayman |
| 应用文献 | |
| 1.Bhaumik, S.R.,Smith, E. and Shilatifard, A. Covalent modifications of histones during development and disease pathogenesis. Nat. Struct. Mol. Biol. 14(11), 1008-1016 (2007). 2.Couture, J.F.,Collazo, E.,Brunzelle, J.S., et al. Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase. Genes & Development 19, 1455-1465 (2005). 3.Yin, Y.,Liu, C.,Tsai, S.N., et al. SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone H4 and mono-methylates lysine 20. The Journal of Biological Chemisty 280(34), 30025-30031 (2005). 4.Shi, X.,Kachirskaia, I.,Yamaguchi, H., et al. Modulation of p53 function by SET8-mediated methylation at lysine 382. Molecular Cell 27(4), 636-646 (2007). | |
| 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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