- Universal - suitable for any SAM-dependent MT
- Flexible - add desired amount of SAM
- Sensitive - fluorescent detection allows for both DNA and protein assays
- Simple - homogeneous mix-and-read plate-based assay
The Methyltransferase HT activity kit is a homogeneous mix-and-read fluorescent assay for the determination of any S-adenosyl-L-methionine (AdoMet/SAM) dependent methyltransferase activity. It is suitable for end-point or kinetic read options, which is ideal for determining mechanism of action, kinetics, and screening candidate compounds. This kit is ideal for high throughout (HT) applications as the SAM is provided separately giving you the flexibility to titrate the SAM to be in excess for your specific MT of interest. This is ideal for driving kinetics of low turnover enzymes and getting more utility by using less precious sample.
Product Details
Applications: | Fluorescent detection, HTS Activity assay
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Application Notes: | For the measurement of AdoMet-dependent methyltransferase activity in purified in vitro samples that do not contain reductants from any species. |
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Species reactivity: | Species independent
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Use/Stability: | Store assay buffer +4°, and all other components at -20°. |
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Shipping: | Shipped on Blue Ice |
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Contents: | Black Microtiter plate, SAM-Free Reaction buffer, Assay buffer, Detection solution, SAM, Positive control |
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Scientific Background: | The methylation of proteins, xenobiotic drugs, nucleic acids, and oligosaccharides is known to regulate important cellular events including meiosis, biosynthesis, development, signal transduction, chromatin remodeling, and gene silencing. The most frequent methyl donor for this type of enzymatic modification is S-adenosyl-L-methionine (AdoMet/SAM). Based on the predicted binding motif for AdoMet, it is estimated that 1% of the mammalian genome encodes a variety of substrate-specific methyltransferases. |
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Regulatory Status: | RUO - Research Use Only |
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Product Literature References
In vitro anthelmintic efficacy of inhibitors of phosphoethanolamine Methyltransferases in Haemonchus contortus: W.H. Witola, et al.; Int. J. Parasitol. Drugs Drug Resist.
6, 44 (2016),
Abstract;
Full Text
Identification of novel bacterial M.SssI DNA methyltransferase inhibitors: M. Hupkes, et al.; J. Biomol. Screen.
18, 348 (2013),
Abstract;