Rich, high quality mass spectrometry data is greatly affected by sample processing upstream to the instrument as well as by the analysis methods used afterwards. The dPC™ platform seamlessly integrates with your current mass spec workflow, giving superior reproducibility, depth of coverage and a powerful tool to streamline data analysis. This ultimately allows the researcher to quickly identify key features (e.g. post-translational modifications, biomarkers, high molecular weight proteins, 550 kD) from robust and reproducible data within minutes after database searching is complete.

The dPC™ Fractionation Technology

The dPC™ separates complex biological samples into fractions suitable for mass spectroscopy, chromatography and blotting using the principle of parallel isoelectric focusing. Proteins or peptides will be charged in an environment that is either above or below their isoelectric point allowing them to migrate in an electric field. Charged proteins/peptides will migrate back and forth through the dPC™ chip between the acidic and basic sides of the chip until they encounter a gel plug that is at or near their isoelectric point where they will become neutral. The uncharged protein or peptide will no longer migrate and will become enriched and separated from other proteins with slightly different isoelectric points.

Proteins/peptides at pH higher than pI (basic) will be negatively charged. Proteins/peptides at pH below their pI (acidic) will be positively charged. Proteins/peptides at pH equal to their pI will be uncharged

Charged proteins/peptides migrate through the dPC™ chip between the acidic and basic sides until they encounter a gel plug whose pH is at or near their pI. The uncharged protein/peptide will no longer migrate and become "trapped" in these plugs.