Evidence map›Paper›PMID 41415880›Full record

ArticleJournal of biological methods2025

Advantages of MabSelect VH3, a novel VH3-specific Protein A resin, over its two conventional counterparts in purifying a VHH-based trispecific antibody.

Dongdong Fang, Wenjing Qi, Yifeng Li

Abstract read
In one paragraph

Article in Journal of biological methods, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Review
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4 · The record

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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Dongdong FangDownstream Process Development, WuXi Biologics, Shanghai 200131, China.
Wenjing QiDownstream Process Development, WuXi Biologics, Shanghai 200131, China.
Yifeng LiDownstream Process Development, WuXi Biologics, Shanghai 200131, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: Protein A affinity chromatography represents the most extensively used technique for initial product capture in antibody purification. The ligands of commercial Protein A resins from different, or even the same, vendors may exhibit distinct binding specificity. For example, MabSelect SuRe LX and MabSelect PrismA bind the antibody's fragment crystallizable region and both the fragment crystallizable and variable heavy chain 3 (VH3) regions, respectively, while MabSelect VH3, a newly launched Protein A resin, binds the VH3 region exclusively. Objective: This study aimed to compare the capabilities of three Protein A resins-namely, MabSelect SuRe LX, MabSelect PrismA, and MabSelect VH3-in removing byproducts associated with a variable domain of heavy chain-only antibody-based trispecific antibody (TsAb). Methods: Clarified culture harvest containing the TsAb was processed separately using MabSelect SuRe LX, MabSelect PrismA, and MabSelect VH3 columns. For each column, byproduct separation was monitored by analyzing relevant elution fractions with sodium dodecyl sulfate-polyacrylamide gel electrophoresis and size-exclusion chromatography-high-performance liquid chromatography. Results: MabSelect VH3 demonstrated superior byproduct removal performance compared with the other two Protein A resins. Conclusion: MabSelect VH3 is particularly suitable for the purification of bispecific antibodies and TsAbs, where the product and byproducts contain different numbers of VH3 domains. For multispecific antibody purification, screening different affinity resins with distinct binding specificity is recommended, as this can help identify the most effective option for separation.

Indexed as

AggregateHalf-antibodyHomodimerMabSelect VH3Protein ATrispecific antibody

Identifiers

PMID41415880
PMCPMC12709518

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.