Co‐expression of human protein disulphide isomerase (PDI) can increase the yield of an antibody Fab′ fragment expressed in Escherichia coli
[摘要] Secretion to the periplasm of Escherichia coli enables production of many eukaryotic extracellular proteins in a soluble form. The complex disulphide bond arrangement of such proteins is probably a major factor in determining the low yield of correctly folded product observed in many cases. Here we show that co-expression of human protein disulphide isomerase increased the yield of a monoclonal antibody Gab′ fragment in the periplasm of E. coli.
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[效力级别] [学科分类] 生物化学/生物物理
[关键词] Protein disulphide isomerase;Antibody fragment;E. coli periplasm;Protein folding;Carb;carbenicillin;Cm;chloramphenicol;Fab′;antibody fragment with hinge containing the variable and first constant domains of both heavy and light chain;FCS;foetal calf serum (heat inactivated);IAA;3-β-indole acrylic acid;IPTG;isopropyl β-d-thiogalactopyranoside;PBS;phosphate buffered saline;PDI;protein disulphide isomerase;PPIase;peptidyl-prolyl-cis-trans-isomerase;TMB;3;3′;5;5′-tetramethylbenzidine;Tween-20;polyoxyethylenesorbitan monolaurate [时效性]
