BellBrook Labs, a leader in high throughput screening assays for drug discovery, announced the launch of a TR-FRET (time resolved Forster resonance energy transfer) version of the company's Transcreener UDP Assay, a high throughput screening assay for glycosyltransferases and other UDP-producing enzymes. The new assay will allow for sensitive detection of hundreds of human and microbial enzymes of potential therapeutic interest for cancer, inherited metabolic disorders, infectious diseases, and other diseases. The TR-FRET detection mode is a preferred readout for HTS because it relies on a time-gated luminescence signal, making it resistant to interference from fluorescent compounds in chemical libraries. The new Transcreener UDP TR-FRET Assay will better serve a growing need for robust, HTS-proven glycosyltransferase assays for drug discovery.
Glycosylation controls the function and localization of thousands of human proteins and is central in bacterial cell wall synthesis. Selective targeting of glycosyltransferases may offer new avenues for therapeutic intervention in diverse diseases, including cancer, inherited metabolic disorders, and infectious diseases. BellBrook Labs pioneered the development of HTS-compatible assays for glycosyltransferases with the introduction of the Transcreener UDP Assay in 2005. Transcreener is the only HTS-compatible glycosyltransferase assay method that relies on direct detection of reaction products and does not depend on coupling enzymes, which are prone to interference. Designed specifically for HTS and featuring a single addition mix-and-read format and room temperature reagent stability, the Transcreener UDP TR-FRET Assay is compatible with plate readers typically found in research labs as well as those used in HTS core facilities. These improvements should accelerate efforts to identify glycosyltransferase inhibitors for use as molecular probes and as potential drug scaffolds.
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