SET7/9 is a MT that acts on various substrates including histone 3 at lysine residue 4 (H3K4), p53, and the transcription factor TAF 10. In Cayman’s SET7/9 MT Inhibitor Screening Assay the transfer of the methyl group from SAM by SET7/9 to the acceptor peptide (TAF 10) generates SAH, which is rapidly converted to urate and H₂O₂ using an enzyme mixture provided in the kit. A subsequent reaction between H₂O₂ and ADHP produces the highly fluorescent compound resorufin.

Couture, J., Collazo, E., Hauk, G., et al. Structural basis for the methylation site specificity of SET7/9. Nat Struct Mol Biol 13(2) 140-146 (2006).

Dorgan, K.M., Wooderchak, W.L., Wynn, D.P., et al. An enzyme-coupled continuous spectrophotometric assay for S-adenosylmethionine-dependent methyltransferases. Anal Biochem 350 249-255 (2006).

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

Chiang, P.K., Gordon, R.K., Tal, J., et al. S-adenosylmethionine and methylation. FASEB J 10 471-480 (1996).

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).

Loenen, W.A.M. S-Adenosylmethionine: Jack of all trades and master of everything? Biochem Soc Trans 34(2) 330-333 (2006).

Song, M., and Ghosh, A. FGF2-induced chromatin remodeling regulates CNTF-mediated gene expression and astrocyte differentiation. Nat Neurosci 7(3) 229-235 (2004).

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