Antigen: human recombinant SET7/9 (amino acids 1-366) · Host: rabbit · Application(s): WB · Diverse signal transduction pathways impinging on the N-terminal tails of histones lead to a number of post-translational modifications including acetylation, phosphorylation, poly (ADP-ribosylation), ubiquitination, and methylation. These modifications play critical roles in regulating chromatin structure and gene expression.¹ Histone methyltransferases selectively methylate evolutionarily conserved arginine or lysine residues, primarily in the N-terminal tails of histones H3 and H4. SET7/9 utilizes S-adenosylmethionine to methylate histone H3 at lysine 4.^2,3,4 Human SET7/9 is a 366 amino acid protein with observed migration on SDS-PAGE at 49 kDa.

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., 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).

3 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).

4 Kwon, T., Chang, J.H., Kwak, E., et al. Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet. EMBO J 22(2) 292-303 (2003).

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).

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).

Kume, A., Miyazaki, T., Kitamura, Y., et al. High levels of saturated very long-chain fatty acid (hexacosanoic acid; C₂₆:0) in whole blood are associated with metabolic syndrome in Japanese men. Diabetes Res Clin Pract 80 259-264 (2008).

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).

Kwon, T., Chang, J.H., Kwak, E., et al. Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet. EMBO J 22(2) 292-303 (2003).

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