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Related Concept Videos

Affinity Chromatography01:03

Affinity Chromatography

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Affinity chromatography is a powerful technique extensively utilized for separating and purifying specific biomolecules from complex mixtures. It capitalizes on the highly selective binding between an analyte and its counterpart, such as antibody-antigen interactions. The counterpart is immobilized on the stationary phase, forming an affinity column. The stationary phase typically consists of solid support, such as agarose or porous glass beads, immobilizing the affinity ligand. The mobile...
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Immunoprecipitation01:20

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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.
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The stability and compatibility of column material with samples are crucial for efficient purification in chromatographic techniques. Various operating parameters such as pH, temperature, or solvent affect the packing of the column material, thereby determining the purification efficiency. The choice of column material also plays an essential role in deciding the operating parameters and can be modified based on the proteins that need to be purified.
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Related Experiment Video

Updated: Dec 3, 2025

Activated Cross-linked Agarose for the Rapid Development of Affinity Chromatography Resins - Antibody Capture as a Case Study
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Antibody Aggregate Removal Using a Mixed-Mode Chromatography Resin.

Tao Chen1, Gaili Guo1, Guoqing Tan1

  • 1Technology and Process Development (TPD), WuXi Biologics, Shanghai, China.

Methods in Molecular Biology (Clifton, N.J.)
|October 31, 2020
PubMed
Summary

Antibody aggregates are common impurities in monoclonal antibody production. A new mixed-mode chromatography resin effectively removes these aggregates, improving purification processes.

Keywords:
Antibody aggregateCapto MMC ImpResMixed-mode resinNative gel electrophoresisSize-exclusion chromatography (SEC)

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Area of Science:

  • Biopharmaceutical manufacturing
  • Protein purification
  • Chromatography

Background:

  • Monoclonal antibody (mAb) production generates product-related impurities, notably aggregates.
  • Aggregates pose challenges in downstream processing and require efficient removal.
  • Standard Protein A chromatography often shows limited efficacy in aggregate clearance.

Purpose of the Study:

  • To evaluate the effectiveness of a mixed-mode chromatography resin for antibody aggregate removal.
  • To establish a robust method for clearing aggregates during mAb purification.

Main Methods:

  • Utilized the mixed-mode chromatography resin Capto MMC ImpRes for aggregate removal.
  • Employed analytical size-exclusion chromatography (SEC) for aggregate quantification.
  • Verified aggregate clearance using native gel electrophoresis.

Main Results:

  • Demonstrated effective clearance of antibody aggregates using Capto MMC ImpRes.
  • Confirmed the resin's capability to reduce aggregate load in downstream processing.
  • Validated the findings through orthogonal analytical techniques.

Conclusions:

  • Capto MMC ImpRes offers a viable solution for removing antibody aggregates.
  • This mixed-mode chromatography approach enhances the purity of monoclonal antibody products.
  • Improved aggregate removal contributes to more efficient biopharmaceutical manufacturing.