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Strategies for analysing and improving the expression and quality of recombinant proteins made in mammalian cells
Author(s) -
Jenkins Nigel,
Meleady Paula,
Tyther Raymond,
Murphy Lisa
Publication year - 2009
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1042/ba20080258
Subject(s) - recombinant dna , protein expression , quality (philosophy) , computational biology , monoclonal antibody , yield (engineering) , biochemical engineering , protein quality , biology , microbiology and biotechnology , biochemistry , antibody , engineering , gene , immunology , philosophy , materials science , epistemology , metallurgy
The production of monoclonal antibodies and other recombinant proteins is one of the highest growth areas in the pharmaceutical industry. Mammalian cells are used to manufacture the majority of biotherapeutics, largely due to their ability to perform complex post‐translational modifications. Although significant progress has been made recently in improving product yields and protein quality, many challenges still lie ahead to achieve consistently high yields while avoiding potentially damaging protein modifications. The present review first considers the strategies used to analyse and improve recombinant protein expression of industrial cell lines, with an emphasis on proteomic technologies. Next, cellular and environmental influences on protein production and quality are examined, and strategies for improvements in product yield and quality are reviewed. The analytical techniques required to detect these protein changes are also described, together with prospects for assay improvements.