Thierry Rabilloud has been doing proteomics since long before the word proteome was even coined. For years Rabilloud, currently at the Atomic Energy Commission Research Center in Grenoble, France, used two-dimensional gel electrophoresis (2-DE) to break complex protein mixtures down into their component parts, purified individual proteins that interested him, and then sent these out for identification by mass spectrometry (MS). But at this point his research hit a bottleneck: the MS facility could accept only a few samples at a time, because the sample processing procedure was so labor-intensive. Then the MS lab acquired robots to automate the processing steps, and the bottleneck disappeared. "Before we were sending in maybe 10 spots. It was a lot of work," he recalls. "Now we can send 50 spots. That's a piece of cake."
Rabilloud's experience is not unique. Traditionally, the 2-DE-based workflow is labor-intensive, technically challenging, difficult to reproduce, and low-throughput. ...
