BellBrook Labs Develops a More Cost Effective Solution for Screening Phosphodiesterases, Ligases, and Synthetases

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Scientists at BellBrook Labs developed a new monoclonal antibody for AMP and used it to enhance the sensitivity of the company’s Transcreener AMP2/GMP2 Assay, a fluorescent high throughput screening assay that can be used for hundreds of enzymes, among them targets for cancer, cardiovascular diseases and infectious diseases. The increased sensitivity will reduce enzyme costs by as much as two- to four-fold for phosphodiesterase assays, ligase assays, and related assays, which could have a significant impact on high throughput screening decisions in the current cost-conscious drug discovery environment.

BellBrook Labs' Transcreener AMP2/GMP2 Assay

The diversity of enzymes that can be screened with the Transcreener AMP2/GMP2 Assay is truly amazing, and the new monoclonal makes that list even longer. Robert Lowery, Ph.D., BellBrook Labs CEO

BellBrook Labs announced the launch of an improved Transcreener AMP2/GMP2 Assay that uses a new monoclonal antibody, allowing more sensitive detection of hundreds of enzymes of potential therapuetic interest including ligases, synthetases, phosphodiesterases and sialyltransferases. These and related enzymes are being targeted for a diverse range of diseases, including cancer, cardiovascular disease and infectious diseases, and robust high throughput assays are critical for these efforts. As with the first generation assay, the new Transcreener AMP2/GMP2 Assay relies on a highly specific antibody that recognizes AMP, GMP and CMP, but not the cyclic or triphosphate forms of these nucleotides. This allows detection of nanomolar quanties of the nucleotide monophosphates in enzyme reactions without separating them from other reaction components; i.e., mix-and-read detection. The higher affinity of the new monoclonal antibody makes the assay more sensitive by a factor of two- to four-fold, which reduces the amount of enzyme required in screening assays by the same factor. Since the enzyme often accounts for half or more of the total reagent costs for an HTS campaign, the savings afforded by the new BellBrook assay will have a significant impact on screening decisions in the current cost-conscious drug discovery environment. In addition to decreasing costs, the more sensitive assay will expand the scope of screening capabilities to previously intractable enzymes with very low substrate requirements.

Transcreener® is a universal, high throughput biochemical assay platform based on detection of nucleotides, including ADP, GDP, AMP, GMP and UDP which are formed by thousands of cellular enzymes, many of which catalyze the covalent regulatory reactions that are central to cell signaling and represent new opportunities for therapeutic intervention. It relies on highly specific antibodies that detect nucleotides coupled with homogenous fluorescent detection formats suitable for automated HTS applications. A single Transcreener assay can be used with any enzyme that produces a given nucleotide, allowing detection of hundreds of different drug targets. It is the only enzyme assay method that allows direct detection of nucleotide enzyme products without the use of additional coupling or reporter enzymes, which are a common source of interference by chemical library compounds. BellBrook currently holds five issued patents on the Transcreener technology.

About BellBrook Labs. BellBrook Labs, LLC develops detection reagents and microfluidic devices that accelerate the discovery of more effective therapies for cancer and other debilitating diseases. Transcreener® is a patented high throughput screening assay platform that was introduced in 2005 and is used to identify inhibitors for kinases and other types of protein drug targets. The iuvo™ Microconduit Array technology and assay screening service is a line of unique microscale devices for miniaturization and automation of advanced cell models that are more representative of human physiology. Visit BellBrook’s website for more information:

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Robert Lowery
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