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Antibodies 2015, 4(3), 259-277;

Antibody Fragments and Their Purification by Protein L Affinity Chromatography

GE Healthcare Life Sciences, Uppsala 75184, Sweden
JMVA Biotech, Stockholm 11254, Sweden
Industrial Biotechnology, Royal Institute of Technology (KTH), Stockholm 10691, Sweden
These authors contributed equally to this work.
Author to whom correspondence should be addressed.
Academic Editor: Satoshi Ohtake
Received: 29 June 2015 / Revised: 5 August 2015 / Accepted: 27 August 2015 / Published: 11 September 2015
(This article belongs to the Special Issue Antibody Constructs)
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Antibodies and related proteins comprise one of the largest and fastest-growing classes of protein pharmaceuticals. A majority of such molecules are monoclonal antibodies; however, many new entities are antibody fragments. Due to their structural, physiological, and pharmacological properties, antibody fragments offer new biopharmaceutical opportunities. In the case of recombinant full-length antibodies with suitable Fc regions, two or three column purification processes centered around Protein A affinity chromatography have proven to be fast, efficient, robust, cost-effective, and scalable. Most antibody fragments lack Fc and suitable affinity for Protein A. Adapting proven antibody purification processes to antibody fragments demands different affinity chromatography. Such technology must offer the unit operation advantages noted above, and be suitable for most of the many different types of antibody fragments. Protein L affinity chromatography appears to fulfill these criteria—suggesting its consideration as a key unit operation in antibody fragment processing. View Full-Text
Keywords: affinity; antibody fragment; bioprocess; chromatography; monoclonal antibody; protein A; protein L affinity; antibody fragment; bioprocess; chromatography; monoclonal antibody; protein A; protein L

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Rodrigo, G.; Gruvegård, M.; Van Alstine, J.M. Antibody Fragments and Their Purification by Protein L Affinity Chromatography. Antibodies 2015, 4, 259-277.

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