Hoffmann-la Roche Inc.

F. Hoffmann-la Roche Ag

Christian Gassner

Joerg Moelleken

Olaf Mundigl

Stefan Dengl

Guido Hartmann

Peter Michael Huelsmann

Guy Georges

Hubert Kettenberger

Michael Molhoj

Sabine Gruener

Sebastian Breuer

Joerg Thomas Regula

Sabine Imhof-Jung

Ralf Schumacher

Kristian Hobolt Jensen

Joerg Benz

Roland Beckmann

Apollon Papadimitriou

Barbara Weiser

Stefan Lorenz

Marc Bedoucha

Manuel Endesfelder

Joerg-Thomas Regula

Wolfgang Meschendoerfer

Thomas Joerg Regula

Herein is reported a method for determining the binding affinity of the binding sites of a bivalent full length antibody of the human IgG1 subclass to a homo-multimeric antigen comprising the steps of i) incubating a mixture comprising the antibody and a polypeptide that is derived from lysine-gingipain ofat a pH of from pH 7.5 to pH 8.5, in the presence of a reducing agent, at a temperature of from 30° C. to 42° C., for time of from 10 min. to 240 min. to cleave the antibody into Fabs and Fc-region, and ii) determining the binding affinity of the Fabs of the antibody for its antigen using a surface plasmon resonance method by directly applying the incubated reaction mixture obtained in the previous step in the surface plasmon resonance method and therewith determining the binding affinity of the binding sites of the bivalent full length antibody of the human IgG1 subclass.

Direct affinity measurement of human IgG1 binding multimeric antigens

Herein is reported a method for determining the binding interaction with a multimeric antigen of an antibody of the human IgG1 subclass that has at least two binding sites specifically binding to the antigen comprising the steps of 1) determining the binding affinity of the antibody for the multimeric antigen, and 2) incubating a mixture comprising the antibody and a polypeptide that is derived from lysine-gingipain ofunder conditions and for a time sufficient to cleave the antibody into Fabs and Fc-region, and determining the binding affinity of the Fabs of the antibody for the multimeric, whereby the binding affinity of the antibody to the multimeric antigen to be affinity-driven if the binding affinity determined in both steps are comparable and to be avidity-driven if the binding affinity determined in both steps are different.

Method for determining the in vivo interaction mode

The present invention relates to anti-VEGF/anti-IL-1beta antibodies and methods of using the same.

Antibody that binds to VEGF and IL-1beta and methods of use

Herein are reported novel bispecific antibodies that specifically bind to two different antigens selected from the group consisting of human ANG2, human VEGF, human IL-1beta and human PDGF-B.

Bispecific antibodies and methods of use in ophthalmology

Herein are reported humanized anti-IL-1beta antibodies that are humanized variants of the murine anti-IL-1beta antibody H34. A specific humanized antibody comprises (a) a HVR-H1 comprising the amino acid sequence of SEQ ID NO: 25, (b) a HVR-H2 comprising the amino acid sequence of SEQ ID NO: 27, and (c) a HVR-H3 comprising the amino acid sequence of SEQ ID NO: 28.

Anti-IL-1beta antibodies

Herein are reported anti-PDGF-B antibodies and their use in ophthalmology.

Anti-PDGF-B antibodies and methods of use

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Penzberg, Germany

Christian Gassner