P
Pete Gagnon
Researcher at Agency for Science, Technology and Research
Publications - 53
Citations - 1244
Pete Gagnon is an academic researcher from Agency for Science, Technology and Research. The author has contributed to research in topics: Adsorption & Size-exclusion chromatography. The author has an hindex of 19, co-authored 53 publications receiving 1110 citations.
Papers
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Journal ArticleDOI
Technology trends in antibody purification.
TL;DR: Technology trends in antibody purification are reviewed, including recent innovations in size exclusion, anion exchange, cation exchange, hydrophobic interaction, immobilized metal affinity, mixed-mode, and bioaffinity chromatography.
Journal ArticleDOI
Cleavage efficient 2A peptides for high level monoclonal antibody expression in CHO cells.
Jake Chng,Tianhua Wang,Rui Nian,Ally Lau,Kong Meng Hoi,Steven C. L. Ho,Pete Gagnon,Xuezhi Bi,Yuansheng Yang +8 more
TL;DR: The vector and methods presented provide an easy process beneficial for both mAb development and manufacturing, and enhance the cleavage efficiency and thus the mAb expression level.
Journal ArticleDOI
Nonspecific interactions of chromatin with immunoglobulin G and protein A, and their impact on purification performance.
Pete Gagnon,Rui Nian,Jeremy Lee,Lihan Tan,Sarah Maria Abdul Latiff,Chiew Ling Lim,Cindy Chuah,Xuezhi Bi,Yuansheng Yang,Wei Zhang,Hui Theng Gan +10 more
TL;DR: Host protein contamination was reduced about 100-fold compared to protein A loaded with harvest clarified by centrifugation and microfiltration, and IgG binding capacity increased ~20%, and Turbidity of eluted IgG upon pH neutralization was nearly eliminated.
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Principles and applications of steric exclusion chromatography
Jeremy Lee,Hui Theng Gan,Sarah Maria Abdul Latiff,Cindy Chuah,Wan Yee Lee,Yuansheng Yang,Bernard Loo,Say Kong Ng,Pete Gagnon +8 more
TL;DR: Hydroxyl-substituted polymethacrylate monoliths provide a hydrophilic surface and support convective mass transport that is unaffected by the viscosity of the PEG.
Journal ArticleDOI
Transient conformational modification of immunoglobulin G during purification by protein A affinity chromatography.
TL;DR: Protein A-mediated formation of the reduced-size conformation is probably universal during purification of human IgG1 antibodies, and may occur with other subclasses and IgG from other species, as well as Fc-fusion proteins.