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SET7/9 SAM-Screener™ Assay Kit

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    SET7/9 SAM-<wbr/>Screener™ Assay Kit
  • SET7/9 SAM-<wbr/>Screener™ Assay Kit
Cat No: 600490
Assays - Miscellaneous
Cayman
€461.00
Price is excluding VAT and does not include packaging neither shipping

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. SET7/9 (KMT7) is a SET domain-containing mono-methyltransferase that act...

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Territorial Availability: Available through Bertin Technologies only in Europe
Special Advice: This kit has multiple shipping temperatures
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. 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 α. 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.
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. 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 α. 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
Size: 384 wells
Shipping: dry ice
Stability: Store at -80 degrees; shelf life 180 days maximum after production
Custom Code: 3822000002
UNSPSC code: 41116104

Dhayalan, A., Kudithipudi, S., Rathert, P., et al. Specificity analysis-based identification of new methylation targets of the SET7/9 protein lysine methyltransferase. Chem Biol 18 111-120 (2011).

Bannister, A.J., and Kouzarides, T. Regulation of ch

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Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.

Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.

Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.

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ISO Guide 34:2009

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