Cayman Chemical | SET7/9 (human recombinant) | Description • KMT7; SETD7/9; SET Domain-containing Protein 7/9

10320 SET7/9 (human recombinant)

KMT7; SETD7/9; SET Domain-containing Protein 7/9

• See more Enzyme Activity; High Throughput Screening; Proteins; Recombinant Proteins; Cancer; Chromatin Research; Epigenetics; Gene Regulation; Histone Modification

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Source: recombinant N-terminal hexahistidine-tagged SET7/9 amino acids 1-366, purified from E. coli · M_r: 43.3 · Methylation of lysine can promote transcriptional activation or repression and is critical in regulating histone function.¹ Lysine residues can be mono-, di-, or tri-methylated, and unlike most SET proteins, SET7/9 is exclusively a mono-methylase.² SET7/9 methylates histone H3, tumor suppressor p53, and transcription factor TAF10.³ Recently, SET7/9 was shown to catalyze methylation of p53 in response to DNA damage thereby activating p53 for subsequent acetylation.¹ SET7/9 is able to modulate p53 activity in a human cancer cell line, implying that it may play a significant role in human tumorigenesis.

1 Kurash, J.K., Lei, H., Shen, Q., et al. Methylation of p53 by Set7/9 mediates p53 acetylation and activity in vivo. Molecular Cell 29 392-400 (2008).

2 Xiao, B., Jing, C., Wilson, J.R., et al. Structure and catalytic mechanism of the human histone methyltransferase SET7/9. Nature 421 652-656 (2003).

3 Couture, J., Collazo, E., Hauk, G., et al. Structural basis for the methylation site specificity of SET7/9. Nature Structural and Molecular Biology 13(2) 140-146 (2006).

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Pricing updated 2010-03-18.
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