BiOptic Inc.'s CGE (capillary gel electrophoresis) based analyzer can also be used on protein analysis. (Coming soon......)
Useful characteristics of proteins include their structure, function, sequence, concentration, and binding characteristics. A significant number of proteins, especially those of interest to the pharmaceutical industry, are embedded in the cellular membrane, which confers on them a particular three-dimensional structure. To date, no method exists that can determine both the structure and function of membrane proteins in their in vivo conformation. Common methods of protein characterization include slab gel separations, mass spectrometry, fluorescence imaging, x-ray crystallography, and NMR spectroscopy.
While 2D slab gel separations reveal size and charge information for proteins, and have historically been the lab workhorse for analyzing proteins (e.g., Western blots), they do not provide any information about polypeptide sequence, which is needed for identifying unknown proteins.
Mass spectrometry is a powerful tool, but high concentrations of common biological proteins that may also be present in a sample, such as albumin, can mask signals from less concentrated proteins important to cellular activity. Fluorescence methods can reveal useful information, but preparing fluorescent markers is often time-consuming, tedious, and expensive. Because a large number of proteins cannot be monitored easily with these techniques, the throughput of discovery and monitoring of complex intracellular interactions is limited.
Figure 1: The analysis of amino acid groups.
Figure 2: FITC labeled phospho-amino acid analysis