SET7/9 SAM-Screener™ Assay Kit

Territorial Availability: Available through Bertin Technologies only in France

• Correlated keywords
  • kits assays measures measurements chromatins posttranslational modifications histones DNA deoxyribonucleic acids lysines methylations epigenetics regulations genomes mono-methyltransferases MTs domains S-adenosyl-L-methionines SAM AdoMet co-factors epsilons amino groups Dot1 KMT7 domain-containing non-histones H3 TAF10 p53 viral Tat estrogens receptors alpha .alpha. ? substrates humans diseases catalytic catabolism fluorescence EpiTrek polarizations fluorescent probes binding pockets endogenous cofactors sinefungin peptides high-throughput screener
• Product Overview:
  Most histone lysine methyltransferases contain a conserved domain (SET) that utilizes S-adenosyl-L-methionine (SAM or AdoMet) as a co-factor to catalyze the methylation of lysine.{20237} SET7/9 (KMT7) is a SET domain-containing mono-methyltransferase that acts on a large number of histone and non-histone targets including histone H3, TAF10, p53, viral Tat, and estrogen receptor ?.{16846,19351} Given this broad substrate specificity, SET7/9 has important implications for a variety of human diseases, and SET7/9 has emerged as a model for studying the catalytic mechanism SET domain histone methyltransferases. This fluorescence polarization assay is based upon a proprietary small molecule fluorescent probe* that binds to the SAM binding pocket in SET7/9. Binding of the small molecule probe to SET7/9 induces an increase in fluorescence polarization. Binding of the probe can be competed with the endogenous cofactor SAM or by the inhibitor sinefungin, but is unaffected by the histone H3 peptide substrate. The SET7/9 SAM-Screener™ Assay is robust (Z’ >0.6) and exhibits a greater than 100 mP shift over a range of 0-250 nM SET7/9. The assay is suitable for high-throughput screening in the provided 384-well plate or can be scaled to higher density plate formats (e.g., 1,536-well) if desired.*United States Patent 9,120,820