Does protein G binds to murine Fab fragments?
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Protein G has been shown to bind to murine Fab fragments. Research has indicated that protein G chromatography can be considered as an alternative for Fc removal during IgG fragmentation processes in mice, demonstrating strong protein G-Fab2 interaction under standard physiological conditions . Additionally, studies have found that the Fab fragment of a hamster anti-mouse antibody can bind to protein G-sepharose, providing a useful method for removing contaminating proteins during antibody purification . These findings suggest that protein G can interact with murine Fab fragments, highlighting its potential utility in various purification processes involving antibody fragments.
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| Papers (5) | Insight |
|---|---|
| The biomimetic Protein G affinity adsorbent, based on the third IgG-binding domain of Protein G, effectively binds to murine Fab fragments, enabling their purification with high purity. | |
19 Citations | Yes, the Fab-selective mutant of protein G (SpGC3FabRR) binds to murine Fab fragments, improving half-life extension properties of therapeutic proteins in mice. |
Open access•Journal Article | Yes, protein G binds to murine Fab fragments, specifically demonstrated with the 145-2C11 hamster anti-mouse CD3ε antibody, providing a new purification method for these fragments. |
7 Citations | Protein G shows negligible binding to murine Fc but strong interaction with Fab2 fragments, as observed in the study on Ficin-derived mouse IgG1 digests. |
| Not addressed in the paper. |
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