Antibody purification method based on porous polyprotein hydrogel


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Protein purification, protein research, quantification of proteins, drug discovery, vaccine production, pharmaceuticals, affinity purification

Target Problems

In current antibody purification techniques, antibodies bind in a single layer on a surface of agar beads reducing overall yield and increasing retention time.

Key Features

  • Easy– Straight forward process for making polyprotein-based porous hydrogel network.
  • Faster – Purify proteins in 10 minutes versus hours or days
  • More efficient – Captures 3X more antibody on a weight for weight basis due to increased surface area


Dr. Ionel Popa at University of Wisconsin, Milwaukee (UWM) has developed a new class of protein hydrogels made from soluble proteins into a porous 3-dimensional stable network. This technology is faster and more efficient without an increased cost.

This new method to produce polyprotein-based hydrogels with micron-sized pores facilitate their interaction with large particles and molecules, such as antibodies with increased active surface area. Unlike regular methods, where the antibodies bind in a single layer on a surface of agar beads, our method produces binding sites throughout the material. This method offers a much higher surface density of binding sites and provides improved retention time and yield over current antibody purification methods. These protein-based porous hydrogels can be attractive candidates for purification of research-based or therapeutic antibodies used for a broad range of targets in oncology, immunology, hematology and many more prevalent medical applications.

Intellectual Property

PCT filed 2023.


Ionel Popa Associate Professor, Physics Department

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