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New proteomics tool offers a clear look at cellular proteins IDAT can detect proteins at an unprecedented resolution for research and clinical use

(Philadelphia PA) Scientists may have identified the genes in the human genome, but proteomics is the growing field of research that describes how proteins encoded in those genes work. Researchers at the University of Pennsylvania School of Medicine have created the first new technology for the proteomic era, a technique sensitive enough to detect individual proteins and robust enough to screen hundreds or thousands of molecules in mass automation.

The versatile technique, called IDAT, has a variety of potential uses from detecting cancer earlier to sifting through samples of molecules to find new candidates for drug research. In todays edition of Proceedings of the National Academy of Science, the researchers describe how they used IDAT to identify a protein marker for breast cancer at a resolution up to nine orders of magnitude more powerful than conventional techniques, and explain how the technique can be further refined.

"Nine orders of magnitude is a significant jump. If we were discussing computers, we would be talking about the differences between bytes and Gigabytes," said Mark I. Greene, MD, PhD, Professor in the Penn Department of Pathology and Laboratory Medicine. "IDAT has the potential to do for proteomics what PCR did for genomics in the last two decades."

IDAT works by snagging a target protein even in a vast mixture of separate molecules and broadcasting the presence of the targeted protein with a strong signal. IDAT stands for Immuno-Detection Amplified by T7 RNA polymerase and it combines the detecting ability of antibodies, highly specific immune system molecules, with the speed of a particular enzyme, T7 RNA polymerase, to act as an alarm system. The enzyme and the antibody both interact through another molecule called a promoter. When the antibody snags the targeted protein, it triggers the promoter that, in turn, triggers the enzyme into creating the signal. Researchers could then screen for the signal, actually a molecule
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Contact: Greg Lester
lesterg@uphs.upenn.edu
215-349-5658
University of Pennsylvania School of Medicine
22-Apr-2001


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