Effect of inducible co-overexpression of protein disulfide isomerase and endoplasmic reticulum oxidoreductase on the specific antibody productivity of recombinant chinese hamster ovary cells

Biotechnology and Bioengineering

Volumn 107, Issue 2, 2010, Pages 337-346

  Mohan, Chaya ^a   Lee, Gyun Min ^a  

^a Korea Advanced Institute of Science and Technology (KAIST)   (South Korea)

Author keywords

Chinese hamster ovary (CHO) cells; Endoplasmic reticulum oxidoreductase (ERO1L); Inducible expression system; Protein disulfide isomerase (PDI)

Indexed keywords

ANTIBODY PRODUCTION; CELL LINES; CHINESE HAMSTER OVARY; CHINESE HAMSTER OVARY CELLS; DISULFIDE BOND FORMATION; DISULFIDE BONDS; ENDOPLASMIC RETICULUM; EXPRESSION LEVELS; INDUCIBLE EXPRESSION; OVER-EXPRESSION; OXIDATION STATE; OXIDIZED STATE; OXIDOREDUCTASES; PROTEIN DISULFIDE ISOMERASE (PDI); PROTEIN DISULFIDE ISOMERASES; RATE-LIMITING STEPS; STABLE CLONES; TRANSIENT EXPRESSION; TRANSIENT GENE EXPRESSIONS;

ANTIBODIES; CELL CULTURE; CLONE CELLS; OXIDATION; PRODUCTIVITY; PROTEIN FOLDING; BIOSYNTHESIS; CELL MEMBRANES; COVALENT BONDS; GENE EXPRESSION; PHYSIOLOGY;

GENE EXPRESSION; RECOMBINANT PROTEINS;

ANTIBODY; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE; DISULFIDE; RECOMBINANT PROTEIN; ENDOPLASMIC RETICULUM OXIDOREDUCTASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL EXPERIMENT; ANTIBODY PRODUCTION; ARTICLE; CHO CELL; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; GENE EXPRESSION; HUMAN; NONHUMAN; PROTEIN EXPRESSION; PROTEIN FOLDING; TRANSIENT EXPRESSION; ANIMAL; BIOSYNTHESIS; CRICETULUS; ENZYMOLOGY; HAMSTER; METABOLISM; OXIDATION REDUCTION REACTION; ANTIBODY SPECIFICITY; DISULFIDE BOND; FEMALE; GENE OVEREXPRESSION; MOLECULAR CLONING; NUCLEOTIDE SEQUENCE; OXIDATION; PROTEIN PROTEIN INTERACTION;

CRICETULUS GRISEUS;

ANIMALS; ANTIBODIES; CHO CELLS; CRICETINAE; CRICETULUS; DISULFIDES; ENDOPLASMIC RETICULUM; GENE EXPRESSION; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN DISULFIDE-ISOMERASES; RECOMBINANT PROTEINS;

EID: 78149250499     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.22781     Document Type: Article

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