Background: Lysine acetyltransferases (KATs) are a crucial class of enzymes responsible for the acetylation of lysine residues on histones and other proteins. This acetylation process plays a significant role in regulating gene expression, protein function, and chromatin dynamics. Dysregulation of KAT activity has been implicated in various diseases, including cancer, neurodegenerative disorders, and inflammatory conditions. Targeting KATs with specific inhibitors offers a promising therapeutic strategy, as it can potentially reverse abnormal acetylation patterns, thereby restoring normal gene expression and cellular functions.

KAT Inhibition and Detection: At ICE Bioscience, we focus on detecting the inhibitory effects of small molecules on KAT activity using the advanced TR-FRET (Time-Resolved Fluorescence Resonance Energy Transfer) method. This highly sensitive and specific technique allows us to monitor changes in acetylation activity, providing valuable insights into the efficacy of potential KAT inhibitors. Our TR-FRET-based assays are designed to deliver accurate and reproducible results, making them an essential tool in the drug discovery process.

Comprehensive KAT Target Assays: Our platform has successfully completed assays for a comprehensive range of KAT targets, including HAT1, GCN5, CREBBP, P300, TIP60, MOZ, MORF, MYST2, and MYST1. These targets are critical in various cellular processes, and their dysregulation is associated with significant pathological conditions. By offering a broad spectrum of KAT target assays, we provide our clients with the necessary data to assess the selectivity and potency of their KAT inhibitors, aiding in the development of targeted therapies.