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

e protein 200 plus LabChip kit produced highly reproducible results only when its own ladder was analyzed (CV ≤1%, as compared to a CV of 0.97.2% with the Pro260 ladder).

Overall, both systems appear to acceptably size each others ladder proteins, though the Experion system offers the advantages of better reproducibility and the capability to resolve and size fragments smaller than 14.4 kD and larger than 210 kD. This broader separation and sizing range is advantageous because it offers the potential for analysis of proteins encompassing a larger range of MW at one time.

Quantitation
For many downstream applications and investigations of the physical and chemical properties of proteins, concentration information is useful and often crucial. The Pro260 assay automatically determines the relative concentration of protein samples using a single-point calibration, wherein the peak area of a protein of interest is compared to the peak area of a 260 kD internal upper marker, which is present in each sample at a known concentration. Additionally, the user has the option to obtain an absolute protein concentration by using known concentrations of a purified protein to create a calibration curve on the chip.

To evaluate the accuracy and reproducibility of relative and absolute quantitation by the Pro260 and protein 200 plus assays, 100 ng/l stock solutions of BSA and bovine CA were prepared, quantitated by UV spectroscopy, and analyzed on the two systems. The results, shown in Table 2, reveal that the Pro260 assay delivered highly reproducible relative quantitation (CV of 4.3% and 10.7% for BSA and CA, respectively). In contrast, the relative quantitation generated by the pr
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