Lysine Methyltransferases are enzymes that play a critical role in epigenetic control of gene expression by facilitating transfer of one, two or three methyl groups to specific nucleophilic sites on proteins and nucleic acids. Methyltransferases fall into two major families—protein lysine methyltransferases (KMTs) and protein arginine methyltransferases (PRMT). Each family contains an evolutionarily conserved catalytic SET domain, which transfers methyl groups from S-Adenosyl methionine (SAM) to the target residue. Aberrant expression of HMTs has been detected in multiple myeloma and various genetic diseases making it a potential therapeutic target.
What We Offer
SAMDI Tech offers a plug-and-play format for quantitative analysis of methyltransferase activity using native substrates. Native peptide and protein substrates can be captured and purified onto SAMDI 384 or 1536 biochip arrays for analysis by mass spectrometry. No need for cumbersome fluorescent-labeled substrates that can interfere with activity and lead to increase false positive rates. SAMDI has the capability to monitor all methylated states simultaneously in a single assay.
- Fast – Eliminates labels and reduces assay development time
- Efficient – Multi-analyte detection and 10,000s of samples analyzed per day
- Quantitative – Measures enzyme kinetics, mechanism of action, and IC50s
Types of Methyltransferases Assays
- KMTs- Lysine methyltransferases (NSD1, NSD2, EZH1, EZH2)
- PRMTs- Arginine methyltransferases (PRMT1, PRMT2, PRMT5)
- DNMTs- DNA Methyltransferases (DNMT1, DNMT3) and more…
SAMDI surface chemistry for purification of peptide analytes prior to mass spectrometry. Methyltransferase is reacted with peptide substrate and both substrate and product are captured to SAMDI arrays.
SAMDI Mass Spectrometry
SAMDI mass spectrum of a methylation event where 20% of substrate is converted to mono-methylated product.
SAMDI is quantitative and can measure enzyme kinetics including: Vo vs [Enzyme], enzyme linearity, Km determination, and plate uniformity.