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High-throughput Purification of Affinity-tagged Recombinant Proteins
Published on: August 26, 2012
Detection and consequences of recombinant protein isoforms: implications for biological potency
M M Federici1, K Venkat, N Bam
1GlaxoSmithKline Pharmaceuticals, King of Prussia, PA 10496-0939, USA. Marcia_m_federici@sbphrd.com
Developments in Biologicals
|November 19, 2003
Summary
Structural variants in recombinant DNA products, known as isoforms, can affect biological activity. This study isolated and characterized specific monoclonal antibody isoforms to assess their impact on bioactivity.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Chemistry
Background:
- Recombinant DNA-derived products can exhibit structural variants called isoforms.
- These isoforms include variations in post-translational modifications, processing, and chemical modifications.
- The impact of these structural variations on biological activity is not fully understood.
Purpose of the Study:
- To isolate and characterize specific molecular isoforms of a monoclonal antibody product.
- To assess the effects of these structural variations on the product's biological activity.
Main Methods:
- Isolation and enrichment of specific isoforms.
- Sophisticated analytical techniques for molecular characterization.
- Bioassays to assess biological activity.
Main Results:
- Specific molecular isoforms of the monoclonal antibody were isolated and characterized.
- The study assessed the impact of these isoforms on biological activity, addressing variability in bioassays.
Conclusions:
- Understanding and characterizing structural variants (isoforms) is crucial for recombinant protein products.
- Assessing the biological activity of specific isoforms is essential for product efficacy and safety.
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