The SIRTainty™ Class III HDAC Assay utilizes a novel patent pending technology for the sensitive detection of all known sirtuin family members. This easy to perform assay employs nicotinamidase to measure nicotinamide generated upon cleavage of NAD+ during sirtuin mediated deacetylation of a substrate providing a direct assessment of the activity of class III HDAC enzymes.
Unlike conventional assays that are dependent upon a single pre-labeled fluorescently tagged substrate, the SIRTainty Class III HDAC Assay employs untagged acetylated peptide substrate for the detection sirtuin activity. This approach not only enables unparalleled flexibility in the choice of sirtuin isoform and peptide substrate, but also eliminates the potential for artifacts due to the use of artificial substrates containing bulky fluorophores.
Features and Benefits:
- Sensitive Detection – assay design enables detection of all known sirtuin family members. Extensively validiated for sirtuins 1-3.
- Unparalleled Flexibility – use of unlabeled substrates enables assay customization and the analysis of a variety of peptide substrates.
- High Throughput – 96-well plate format ideal for inhibitor/activator assays and the study of enzyme mechanisms. Assay design can be adapted to 384-well plates.
- Easy-to-use – simple protocol, homogeneous, no wash format.
- Reliable Chemistry – unlabeled peptide substrate avoids detection artifacts due compounds such as resveratrol.
- Rapid Results –easy two step assay with minimal hands on time allows you to go from sample to results in about 90 minutes.