Uploaded March 2026 | Updated September 2026, 2 weeks ago
Large molecule purification presents significant challenges due to their considerable size. For instance, Immunoglobulin M (IgM) molecules, ranging from 900 to 1,000 kD, play pivotal roles in mammalian immune responses and find extensive applications in diagnostics and therapeutics. Purification of such molecules is particularly intricate owing to several factors including their weak Protein A binding sites, limited dynamic binding capacity, and slow diffusion rates.
Moreover, IgMs exert notable effects on chromatographic purification processes. Their inability to penetrate small pores necessitates higher pore volume utilization, resulting in sluggish diffusion and mass transfer kinetics within traditional chromatography resins. Consequently, this diminishes binding capacity and resolution, thereby complicating purification efforts.
This webinar will delve into innovative strategies to surmount these challenges, employing design of experiments (DOE) methodologies and offering insightful case studies centered around plasma protein and virus purification. These real-world applications showcase tangible enhancements in productivity and overall process economics within large molecule purification.
Key Takeaways:
• Slow diffusion in traditional chromatography resins affects binding capacity and resolution
• Highlight DOE and case studies on plasma protein and virus purification.
• Advanced chromatography resins enhance efficiency and productivity in large molecule purification.
• Optimized mass transfer kinetics improve binding capacities, resolution, and processing time.
#pharmaceutical #biopharma #chromatography
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Presenter:
Artur Stanczak Field Application Specialist
Process Chromatography, Bio-Rad Laboratories
Artur Stanczak is a process chromatography field application specialist at Bio-Rad Laboratories. He received his master's degree in biotechnology from the University of Maria Skłodowska-Curie in Lublin. Artur has more than 13 years of experience in the biotechnology and biopharma industry, specializing in downstream processing of therapeutics. He also has experience in process development, characterization, scale-up, and validation of biologics. Artur supports method development and downstream purification applications, while managing the process chromatography application laboratory located in Munich, Germany.
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Connect with Bio-Rad Online:
Visit Bio-Rad's Website → bio-rad.com
Follow Bio-Rad on LinkedIn → linkedin.com/company/bio-rad
Follow Bio-Rad on Instagram → instagram.com/bioradlabs
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Subscribe to Bio-Rad for the latest breakthroughs in life science research and clinical diagnostics.
©2024 Bio-Rad is a trademark of Bio-Rad Laboratories, Inc. in certain jurisdictions. All trademarks used herein are the property of their respective owner.
Large molecule purification presents significant challenges due to their considerable size. For instance, Immunoglobulin M (IgM) molecules, ranging from 900 to 1,000 kD, play pivotal roles in mammalian immune responses and find extensive applications in diagnostics and therapeutics. Purification of such molecules is particularly intricate owing to several factors including their weak Protein A binding sites, limited dynamic binding capacity, and slow diffusion rates.
Moreover, IgMs exert notable effects on chromatographic purification processes. Their inability to penetrate small pores necessitates higher pore volume utilization, resulting in sluggish diffusion and mass transfer kinetics within traditional chromatography resins. Consequently, this diminishes binding capacity and resolution, thereby complicating purification efforts.
This webinar will delve into innovative strategies to surmount these challenges, employing design of experiments (DOE) methodologies and offering insightful case studies centered around plasma protein and virus purification. These real-world applications showcase tangible enhancements in productivity and overall process economics within large molecule purification.
Key Takeaways:
• Slow diffusion in traditional chromatography resins affects binding capacity and resolution
• Highlight DOE and case studies on plasma protein and virus purification.
• Advanced chromatography resins enhance efficiency and productivity in large molecule purification.
• Optimized mass transfer kinetics improve binding capacities, resolution, and processing time.
#pharmaceutical #biopharma #chromatography
---
Presenter:
Artur Stanczak Field Application Specialist
Process Chromatography, Bio-Rad Laboratories
Artur Stanczak is a process chromatography field application specialist at Bio-Rad Laboratories. He received his master's degree in biotechnology from the University of Maria Skłodowska-Curie in Lublin. Artur has more than 13 years of experience in the biotechnology and biopharma industry, specializing in downstream processing of therapeutics. He also has experience in process development, characterization, scale-up, and validation of biologics. Artur supports method development and downstream purification applications, while managing the process chromatography application laboratory located in Munich, Germany.
---
Connect with Bio-Rad Online:
Visit Bio-Rad's Website → bio-rad.com
Follow Bio-Rad on LinkedIn → linkedin.com/company/bio-rad
Follow Bio-Rad on Instagram → instagram.com/bioradlabs
Follow Bio-Rad on Facebook → facebook.com/biorad
Subscribe to Bio-Rad for the latest breakthroughs in life science research and clinical diagnostics.
©2024 Bio-Rad is a trademark of Bio-Rad Laboratories, Inc. in certain jurisdictions. All trademarks used herein are the property of their respective owner.
