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Updated: Jun 23, 2026

Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay

Detection of Heterodimerization of Protein Isoforms Using an in Situ Proximity Ligation Assay

Published on: October 20, 2018

Assessing different Protein A resins' homodimer separation potentials through processing a two-antibody-containing

Gaoya Yuan¹, Meng Qu¹, Yifeng Li¹

¹Downstream Process Development (DSPD), WuXi Biologics, 31 Yiwei Road, Waigaoqiao Free Trade Zone, Shanghai, 200131, China.

Protein Expression and Purification

|June 21, 2026

Summary

This summary is machine-generated.

Protein A resins can effectively remove homodimer byproducts during asymmetric bispecific antibody (bsAb) production. MabSelect SuRe LX and MabCaptureC resins demonstrated complete separation of antibody components, simplifying purification.

Keywords:

Binding valency Bispecific antibody (bsAb)Homodimer Molecular weight Protein A Protein L VH3

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Area of Science:

Biotechnology
Protein Chemistry
Biopharmaceutical Manufacturing

Background:

Homodimers are challenging byproducts in asymmetric bispecific antibody (bsAb) production.
Affinity chromatography using Protein A resins offers potential for separating antibodies with differential binding strengths.

Purpose of the Study:

To evaluate the capacity of three Protein A resins (MabSelect SuRe LX, MabSelect PrismA, MabCaptureC) for separating antibody variants.
To assess the effectiveness of these resins in removing homodimer byproducts during bsAb purification.

Main Methods:

An artificial mixture of two antibodies with distinct variable heavy chain (VH) origins and molecular weights was processed.
Three Protein A resins were tested under identical conditions to observe separation patterns.
Purification of an asymmetric bsAb with distinct parental VH origins was performed using MabCaptureC.

Main Results:

The three Protein A resins exhibited distinct separation profiles for the antibody mixture.
MabSelect SuRe LX and MabCaptureC achieved complete separation of the two antibody components under optimized conditions.
MabCaptureC effectively separated the target heterodimer from homodimers in asymmetric bsAb purification.

Conclusions:

The choice of Protein A affinity medium significantly impacts the separation of antibody variants.
MabCaptureC demonstrates high efficacy in removing homodimer byproducts during asymmetric bsAb purification.
Optimized affinity chromatography can simplify downstream purification processes by removing difficult byproducts during initial capture.