Engineering the chaperone network of CHO cells for optimal recombinant protein production and authenticity

Methods in Molecular Biology

Volumn 824, Issue , 2012, Pages 595-608

  Jossé, Lyne ^a   Smales, C Mark ^a   Tuite, Mick F ^a  

^a UNIVERSITY OF KENT   (United Kingdom)

Author keywords

Chinese hamster ovary cells; Hsp104; Hsp40; Hsp70; Luciferase; Molecular chaperone; Protein aggregation; Protein folding; Recombinant antibody

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN; LUCIFERASE; RECOMBINANT PROTEIN;

ANIMAL; ARTICLE; BIOTECHNOLOGY; CHO CELL; CRICETULUS; GENETIC ENGINEERING; GENETIC TRANSFECTION; GENETICS; HAMSTER; METABOLISM; METHODOLOGY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN FOLDING; WESTERN BLOTTING;

ANIMALS; BIOTECHNOLOGY; BLOTTING, WESTERN; CHO CELLS; CRICETINAE; CRICETULUS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GENETIC ENGINEERING; HEAT-SHOCK PROTEINS; LUCIFERASES; MOLECULAR CHAPERONES; PROTEIN FOLDING; RECOMBINANT PROTEINS; TRANSFECTION;

CRICETULUS GRISEUS;

EID: 84855930910     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-61779-433-9_32     Document Type: Article

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