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Nat Biotechnol. 1997 Feb;15(2):159-63.

Design and production of novel tetravalent bispecific antibodies.

Author information

1
Department of Microbiology and Molecular Genetics, University of California at Los Angeles 90095, USA.

Abstract

We have produced novel bispecific antibodies by fusing the DNA encoding a single chain antibody (ScFv) after the C terminus (CH3-ScFv) or after the hinge (Hinge-ScFv) with an antibody of a different specificity. The fusion protein is expressed by gene transfection in the context of a murine variable region. Transfectomas secrete a homogeneous population of the recombinant antibody with two different specificities, one at the N terminus (anti-dextran) and one at the C terminus (anti-dansyl). The CH3-ScFv antibody, which maintains the constant region of human IgG3, has some of the associated effector functions such as long half-life and Fc receptor binding. The Hinge-ScFv antibody which lacks the CH2 and CH3 domains has no known effector functions.

Comment in

PMID:
9035142
DOI:
10.1038/nbt0297-159
[Indexed for MEDLINE]

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