Overexpression of a cytosolic chaperone to improve solubility and secretion of a recombinant IgG protein in insect cells

Biotechnology and Bioengineering

Volumn 58, Issue 2-3, 1998, Pages 196-203

  Ailor, Eric ^a   Betenbaugh, Michael J ^a  

^a Johns Hopkins University   (United States)

Author keywords

Baculovirus; Chaperone; hsp70; Immunoglobulin; Insect cell

Indexed keywords

ANTIBODIES; METABOLISM; OLIGOMERS; POLYPEPTIDES; SOLUBILITY; VIRUSES;

CYTOSOLIC CHAPERONE; ENDOPLASMIC RETICULUM; IMMUNOGLOBULIN; INSECT CELLS;

GENETIC ENGINEERING;

CHAPERONE; HEAT SHOCK PROTEIN 70; IMMUNOGLOBULIN G;

ANIMAL CELL; ARTICLE; BACULOVIRUS; ENDOPLASMIC RETICULUM; GENE OVEREXPRESSION; IMMUNOBLOTTING; INSECT; NONHUMAN; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN PROCESSING;

ANIMALS; BLOTTING, WESTERN; CARRIER PROTEINS; CELLS, CULTURED; CYTOSOL; DENSITOMETRY; ENDOPLASMIC RETICULUM; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; IMMUNOGLOBULIN G; MOLECULAR CHAPERONES; MOTHS; PROTEIN FOLDING; RECOMBINANT PROTEINS; SOLUBILITY;

ANIMALIA; ARACHNIDA; HEXAPODA; INSECTA; UNIDENTIFIED BACULOVIRUS;

EID: 0032485869     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19980420)58:2/3<196::AID-BIT12>3.0.CO;2-B     Document Type: Article

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