Validation of Multiplexed IgY-12 Immunoaffinity Column Chromatography for Discovery of Low Abundant Plasma Proteins

The ability to remove highly abundant proteins specifically and with high selectivity is increasingly important in proteomic studies, and success in this procedure is leading to an ever-increasing list of lower abundant proteins being identified in biological fluids.1–3 Several immunoaffinity columns are commercially available for the purpose of the removal of multiple high-abundant proteins from human plasma.4,5 These columns have been used by various laboratories for the successful removal of targeted proteins in high throughput proteomic analysis. Beckman Coulter is marketing a series of new products (ProteomeLab IgY-12 proteome partitioning systems) for proteomic sample preparation using polyclonal IgY antibodies immobilized to microbeads packed in spin columns or liquid chromatography (LC) columns to partition (deplete) 12 of the most highly abundant proteins from plasma that collectively constitute up to 96% of the total protein mass in plasma.

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