title: Expression and purification of recombinant antibody formats and antibody fusion proteins.
abstract: In the laboratory-scale production of antibody fragments or antibody fusion proteins, it is often difficult to keep track on the most suitable affinity tags for protein purification from either prokaryotic or eukaryotic host systems. Here, we describe how such recombinant proteins derived from Escherichia coli lysates as well as HEK293 cell culture supernatants are purified by IMAC and by different affinity chromatography methods based on fusions to FLAG-tag, Strep-tag, and Fc domains.
authors: Institut für Zellbiologie und Immunologie, Universität Stuttgart, Stuttgart, Germany.
authors: Martin
authors: M
authors: Siegemund
authors: Fabian
authors: F
authors: Richter
authors: Oliver
authors: O
authors: Seifert
authors: Felix
authors: F
authors: Unverdorben
authors: Roland E
authors: RE
authors: Kontermann
mesh_terms: D000906:Antibodies / Q000235:genetics / Q000378:metabolism*; D002460:Cell Line; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006801:Humans; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D000906:Antibodies; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins