Heidi Jones is the market development manager for chromatography, applications, and collaborations at Bio-Rad Laboratories. Over the course of 17 years at Amgen and BioMarin prior to joining Bio-Rad, Heidi specialized in protein purification as a pilot and bench scale R&D scientist for a wide variety of proteins including monoclonal antibodies, bi-specifics, fc-fusions, peptides, and enzymes. Heidi holds a master’s degree in business administration from Saint Mary’s College of Moraga, California and a bachelor's degree in biology from the University of California, Los Angeles.
About this event:
Date: November 4, 2025
Time: 11 am EDT | 8 am PDT | 5 pm CEST
Duration: 15 minutes
Traditional Protein A affinity chromatography is the gold standard for Fc-fusion protein purification, but it can introduce challenges such as protein denaturation and degradation due to low pH elution.
This webcast presents a proof-of-concept study demonstrating the use of a new weak anion exchange hydrophobic chromatography resin, Nuvia™ wPrime 2A, and a strong high-performance anion exchange resin, Nuvia HP-Q, for the purification of EGFR:Fc fusion proteins.
The two-step process achieves high purity and yield, offering a gentler, non-affinity-based alternative that preserves protein integrity and is suitable when Protein A workflows are suboptimal.
Gain insights into comparative performance, workflow flexibility, and practical considerations for implementing this approach in your process development.
Key Takeaways:
Mixed-mode and anion exchange chromatography can achieve comparable purity and yield to Protein A methods, offering more flexibility.
Neutral pH purification reduces the risk of Fc-fusion protein denaturation and degradation.
Fc-fusion proteins are effective for where affinity chromatography isn’t suitable, expanding options for biologics purification.
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