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BellBrook Labs Develops a TR-FRET Based Transcreener GTPase Assay
Date:7/16/2014

(PRWEB) July 16, 2014

BellBrook Labs announced the launch of a new Transcreener GDP Assay with a TR-FRET (time resolved Forster resonance energy transfer) readout, for sensitive detection of hundreds of enzymes of potential therapeutic interest including the large GTPase family as well as glycosyltransferase enzymes that use GDP-activated sugars; e.g., fucosyltransferases. These and related enzymes are being targeted for a diverse range of diseases, including cancers and anti-microbials, and robust high throughput assays are critical for these efforts. The TR-FRET detection mode is a highly preferred readout for HTS because it relies on a time-gated luminescence signal, making it resistant to prompt fluorescence screening compounds. Like the other Transcreener assays for ADP, AMP/GMP and UDP, the Transcreener GDP assay relies on direct immunodetection of the nucleotide product, and does not depend on coupling enzymes, which are prone to interference from screening compounds. It is the only HTS-compatible GTPase assay that uses direct GDP detection.

GTPases are a large family of enzymes that play diverse roles in normal and disease-related cell processes. It includes small GTPases in the Ras superfamily as well as the Galpha proteins that relay signals from G-protein coupled receptors. Though many GTPases are known to be intimately involved in disease pathways, they have yet to be exploited therapeutically, partially because they are difficult to incorporate into the high throughput screening assays used to identify lead drug molecules. The Transcreener GDP assay overcomes a longstanding problem in GTPase assays because it relies on direct detection of GDP rather than phosphate. Phosphate is a component of many b
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