High level transient production of recombinant antibodies and antibody fusion proteins in HEK293 cells.

Jäger, Volker; Büssow, Konrad; Wagner, Andreas; Weber, Susanne; Hust, Michael; Frenzel, André; Schirrmann, Thomas

dc.contributor.author	Jäger, Volker
dc.contributor.author	Büssow, Konrad
dc.contributor.author	Wagner, Andreas
dc.contributor.author	Weber, Susanne
dc.contributor.author	Hust, Michael
dc.contributor.author	Frenzel, André
dc.contributor.author	Schirrmann, Thomas
dc.date.accessioned	2016-07-13T13:14:38Z
dc.date.available	2016-07-13T13:14:38Z
dc.date.issued	2013
dc.identifier.citation	High level transient production of recombinant antibodies and antibody fusion proteins in HEK293 cells. 2013, 13:52 BMC Biotechnol.	en
dc.identifier.issn	1472-6750
dc.identifier.pmid	23802841
dc.identifier.doi	10.1186/1472-6750-13-52
dc.identifier.uri	http://hdl.handle.net/10033/615999
dc.description.abstract	The demand of monospecific high affinity binding reagents, particularly monoclonal antibodies, has been steadily increasing over the last years. Enhanced throughput of antibody generation has been addressed by optimizing in vitro selection using phage display which moved the major bottleneck to the production and purification of recombinant antibodies in an end-user friendly format. Single chain (sc)Fv antibody fragments require additional tags for detection and are not as suitable as immunoglobulins (Ig)G in many immunoassays. In contrast, the bivalent scFv-Fc antibody format shares many properties with IgG and has a very high application compatibility.
dc.language.iso	en	en
dc.subject.mesh	Cloning, Molecular	en
dc.subject.mesh	Genetic Vectors	en
dc.subject.mesh	HEK293 Cells	en
dc.subject.mesh	Humans	en
dc.subject.mesh	Immunoglobulin Fc Fragments	en
dc.subject.mesh	Peptide Library	en
dc.subject.mesh	Recombinant Fusion Proteins	en
dc.subject.mesh	Ribonucleases	en
dc.subject.mesh	Single-Chain Antibodies	en
dc.title	High level transient production of recombinant antibodies and antibody fusion proteins in HEK293 cells.	en
dc.type	Article	en
dc.contributor.department	Helmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.	en
dc.identifier.journal	BMC biotechnology	en
refterms.dateFOA	2018-06-12T17:33:00Z
html.description.abstract	The demand of monospecific high affinity binding reagents, particularly monoclonal antibodies, has been steadily increasing over the last years. Enhanced throughput of antibody generation has been addressed by optimizing in vitro selection using phage display which moved the major bottleneck to the production and purification of recombinant antibodies in an end-user friendly format. Single chain (sc)Fv antibody fragments require additional tags for detection and are not as suitable as immunoglobulins (Ig)G in many immunoassays. In contrast, the bivalent scFv-Fc antibody format shares many properties with IgG and has a very high application compatibility.