title: Prokaryotic expression of antibodies.
abstract: Maximizing the expression yields of recombinant whole antibodies and antibody fragments such as Fabs, single-chain Fvs and single-domain antibodies is highly desirable since it leads to lower production costs. Various eukaryotic and prokaryotic expression systems have been exploited to accommodate antibody expression but Escherichia coli systems have enjoyed popularity, in particular with respect to antibody fragments, because of their low cost and convenience. In many instances, product yields have been less than adequate and intrinsic and extrinsic variables have been investigated in an effort to improve yields. This review deals with various aspects of antibody expression in E. coli with a particular focus on single-domain antibodies.
authors.affiliation: Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario. roger.mackenzie@nrc-cnrc.gc.ca
authors.forename: Mehdi
authors.initials: M
authors.lastname: Arbabi-Ghahroudi
authors.forename: Jamshid
authors.initials: J
authors.lastname: Tanha
authors.forename: Roger
authors.initials: R
authors.lastname: MacKenzie
mesh_terms: D000818:Animals; D000906:Antibodies / Q000235:genetics / Q000378:metabolism*; D000936:Antigen-Antibody Complex; D004926:Escherichia coli / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D006801:Humans; D007128:Immunoglobulin Fragments / Q000096:biosynthesis / Q000235:genetics; D007150:Immunohistochemistry; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000302:isolation & purification
chemical_list: D000906:Antibodies; D000936:Antigen-Antibody Complex; D007128:Immunoglobulin Fragments; D011994:Recombinant Proteins