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Related Concept Videos

Immunoprecipitation01:20

Immunoprecipitation

Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
Chromatin Immunoprecipitation
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Vaccine production involves a sequence of upstream and downstream processes to generate a safe and effective immunological product. It begins with cultivating microorganisms, such as viruses or bacteria, to obtain antigenic material. For viral vaccines, mammalian host cells are grown in bioreactors and subsequently infected with the target virus. The virus replicates within the host cells, which are lysed to release viral particles. This lysate is then clarified through filtration or...

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Laboratory Scale Production and Purification of a Therapeutic Antibody
09:54

Laboratory Scale Production and Purification of a Therapeutic Antibody

Published on: January 24, 2017

Relevant shaking stress conditions for antibody preformulation development.

Annette Eppler1, Markus Weigandt, Andrea Hanefeld

  • 1Merck Serono, CMC Development, Darmstadt, Germany.

European Journal of Pharmaceutics and Biopharmaceutics : Official Journal of Arbeitsgemeinschaft Fur Pharmazeutische Verfahrenstechnik E.V
|November 20, 2009
PubMed
Summary

This study optimized shaking stress conditions for antibody formulation development. The best method uses a 2ml vial with 1ml protein solution shaken at 200rpm, rapidly distinguishing stable from unstable antibody formulations.

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Area of Science:

  • Protein formulation development
  • Biopharmaceutical stability testing
  • Antibody aggregation

Background:

  • Shaking stress is crucial for assessing antibody formulation stability against aggregation.
  • Lack of standardized shaking stress protocols leads to variable results.
  • Optimized conditions are needed for reliable stability assessment.

Purpose of the Study:

  • To establish a rapid and discriminating shaking stress design for protein formulation development.
  • To identify optimal parameters for distinguishing poor vs. promising antibody formulations.
  • To develop a small-scale method suitable for preformulation studies.

Main Methods:

  • Investigated shaking stress using monoclonal IgG antibodies in buffered solutions and marketed formulations.
  • Varied parameters: filling degree, container type/size, and shaking intensity.
  • Assessed stability via visual inspection, UV-VIS spectrophotometry, and size exclusion chromatography.

Main Results:

  • All tested parameters significantly influenced stability outcomes.
  • Optimal conditions: 2ml injection vial, 1ml protein solution, 200rpm shaking.
  • This setup clearly differentiated between buffered solutions and marketed products.

Conclusions:

  • A standardized shaking stress protocol (200rpm, 1ml in 2ml vial) effectively assesses antibody formulation stability.
  • This method allows rapid discrimination of formulation stability with minimal protein.
  • The findings are valuable for optimizing antibody formulation development and preformulation studies.