Cayman Chemical | SET8 (human recombinant) | Description • SETD8; SET domain-containing (lysine methyltransferase) 8; PR-Set7

10319 SET8 (human recombinant)

SETD8; SET domain-containing (lysine methyltransferase) 8; PR-Set7

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• See more Enzymes; Proteins; Recombinant Proteins; Cancer; Epigenetics; Histone Modification

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Source: recombinant N-terminal Histidine-tagged SET8 amino acids 190-352, purified from E. coli, NP-065115 · M_r: 21.1 kDa · 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.

1 Bhaumik, S.R., Smith, E., Shilatifard, A. Covalent modifications of histones during development and disease pathogenesis. Nature Structural & Molecular Biology 14(11) 1008-1016 (2007).

2 Couture, J., 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. J Biol Chem 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. Mol Cell 27(4) 636-646 (2007).

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Pricing updated 2010-03-13.
Prices are subject to change without notice.

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