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High capacity magnetic supports for automated antibody and epitope-tagged protein purifications

Speaker
  • Senior R&D Manager, Protein Biology, Thermo Fisher Scientific
    Biography
      Barbara Kaboord received a Ph.D. in Biochemistry at the Medical College of Wisconsin, where she developed a method to affinity isolate DNA replication complexes from actively-replicating cells and followed up with a postdoctoral fellowship at the Pennsylvania State University in Stephen Benkovic's laboratory. Currently, Barbara is the Sr. R&D Manager of the Protein Preparation group at Thermo Fisher Scientific where her team is responsible for the development of numerous protein extraction, stabilization, purification, and clean-up products.

    Abstract

    For academic, biotech, and pharmaceutical scientists who are screening clones or performing high throughput protein purification, the goal is to automate the sample processing without sacrificing binding capacity. Traditionally, magnetic beads have facilitated process automation, but they lack the high binding capacity of agarose resins. On the other hand, agarose or sepharose resins have high binding capacity, but are not amenable to automation. Magnetic agarose resins combine the best of both formats by enabling high throughput sample processing with high protein binding capacity. Here we demonstrate the advantages of using magnetic agarose resins in simple benchtop  protein purifications as well as their utility in 1) the screening of recombinant antibodies using the InvitrogenExpiCHOExpression Systems and 2) the purification of recombinant proteins expressed by in vitro translation (cell-free) systems using the Thermo Scientific KingFisherFlex magnetic particle processor. Both the Protein AG and anti-DYKDDDDK magnetic agarose supports result in isolation of >0.5mg protein per sample at >90% purity.


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