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Performance Comparison of the Experion Automated Electrophoresis System and a Competing Automated System for Protein Analysis, Rev A

tive protocol exists for their quantitation. By loading a chip with a series of known concentrations of a purified protein, the user can generate a calibration curve. An equation derived from the linear fit of the data points comprising this curve is then used to quantitate each protein in the other sample wells. This form of absolute quantitation performs best when the protein used for calibration is the same as that undergoing quantitation.

We applied this absolute quantitation approach using both microfluidic systems to see if the quantitation accuracy for CA could be improved. The software of each system was directed to generate a calibration curve from a dilution series, and then use a linear fit of the data to quantitate two concentrations of CA. Using this approach, accuracy of quantitation by the Pro260 assay was significantly improved, to within 15.8% of the UV-determined concentration, and the protein 200 plus assay, to within 10.5% (Table 2).

Resolution
Another important parameter that defines the overall performance of a protein separation system is its capacity for resolving one protein from another. Identification and quantitation improve as a protein of interest is separated to a greater degree from neighboring proteins.

To evaluate the resolution capabilities of each automated electrophoresis system, a 2 mg/ml E. coli protein lysate was separated with the Pro260 and protein 200 plus LabChip kits, and the total number of peaks detected by the software was recorded. An average of 35 protein peaks were identified with the Pro260 assay upon separation of this complex protein sample; essentially the same number of protein bands were observed when the same sampl
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