Hoffmann-la Roche Inc.

Roche Palo Alto LLC

Maxygen, Inc.

Roche Diagnostics Gmbh

Roche Glycart Ag

Other

F. Hoffmann-la Roche Ag

Stefan Seeber

Georg Fertig

Klaus Kaluza

Carola Ries

Alexander Fidler

Marlene Thomas

Martin Lanzendoerfer

Christian Klein

Ralf Schumacher

Jens Fischer

Guy Georges

Nikolaos Dimoudis

Pablo Umana

Joerg Thomas Regula

Phillip A Patten

Stephan Fischer

Tilman Schlothauer

Torben Lauesgaard Nissen

Joerg Moelleken

Andreas Schaubmar

Paul Parren

Jan Van De Winkel

Sabine Imhof-Jung

Yvo Graus

Ekkehard Moessner

Wolfgang Schaefer

Ulrich Brinkmann

Aran Frank Labrijn

Stefan Dengl

Hubert Kettenberger

Elsie M Eugui

Ralf Hosse

Erhard Kopetzki

Pablo Umaña

Petra Rueger

Werner Scheuer

Anita Kavlie

Juergen Michael Schanzer

Peter Bruenker

Michael Brandt

Claudia Ferrara Koller

Adelbert Grossmann

Sandra Grau-Richards

Valeria G Nicolini

Kay-Gunnar Stubenrauch

Thomas U Hofer

Michael Molhoj

Roberto Falkenstein

Georg Tiefenthaler

Christian Schantz

Joerg Benz

Huisheng Wang

Maria Amann

Christina Claus

Sridhar Viswanathan

Anne Vogt

Harald Kropshofer

Valeria Lifke

Martine Van Vugt

Frank Rebers

Inja Waldhauer

Johannes Auer

Hans Koll

Maria Elena Fuentes

Remko Griep

Monika Baehner

Viktor Levitski

Martin Bader

Stefan Lorenz

Laura Codarri Deak

Markus Thomas

Mario Perro

Adrian Zwick

Joseph Endl

Laura Codarri-Deak

Ildiko Wuensche

Laurent Lariviere

Kathryn Elizabeth Packman

Sonja Offner

Achal Mukundrao Pashine

Maximiliane Koenig

Barbara Weiser

Huifeng Niu

Sherif Daouti

Ningping Feng

Laura Lauener

Rudiger Ruger

Friederike Hesse

Josef Endl

Apollon Papadimitriou

Josef Platzer

Valeria Runza

Jan Olaf Stracke

Alexander Knaupp

Sebastian Neumann

Victor Levitsky

Peter Kern

Stefan Jenewein

Marlene Pickl

Patrick Alexander Aaron Weber

The invention relates to bispecific antibodies comprising a first antigen-binding site that specifically binds to PD1 and a second antigen-binding site that specifically binds to TIM3, in particular to bispecific antibodies, wherein the bispecific antibody binds to 5 TIM3 with a lower binding affinity when compared to the binding to PD1. The invention further relates to methods of producing these molecules and to methods of using the same.

Bispecific antibodies specific for PD1 and TIM3

The invention relates autonomous VH domains (aVH) with cysteines in positions 52a and 71 or in positions 33 and 52 in order to stabilize the autonomous VH domains. Said cysteines are capable of forming a disulfide bond and/or form a disulfide bond under suitable conditions. The invention further relates to aVH libraries.

Stabilized immunoglobulin domains

The present invention generally relates to immunoconjugates, particularly immunoconjugates comprising a mutant interleukin-2 polypeptide and an antibody that binds to PD-1. In addition, the invention relates to polynucleotide molecules encoding the immunoconjugates, and vectors and host cells comprising such polynucleotide molecules. The invention further relates to methods for producing the mutant immunoconjugates, pharmaceutical compositions comprising the same, and uses thereof.

Immunoconjugates

In the method as reported herein the isolation of nucleic acid segments encoding antibody variable domains and the insertion of the isolated nucleic acid segments in eukaryotic expression plasmids is performed without the intermediate isolation and analysis of clonal intermediate plasmids. Thus, in the method as reported herein the intermediate cloning, isolation and analysis of intermediate plasmids is not required, e.g. by analysis of isolated transformedcells.

Rapid method for cloning and expression of cognate antibody variable gene segments

Herein is reported a fusion polypeptide according to formula I (TAG-X1-C1qA-X2-C1qB-X3-C1qC-X4), comprising a fragment of SEQ ID NO: 01 (C1qA), a fragment of SEQ ID NO: 03 (C1qB), a fragment of SEQ ID NO: 05 (C1qC) and optionally a tag (TAG).

Complement factor based affinity chromatography

The invention relates to bispecific antibodies comprising a first antigen binding domain that specifically binds to PD1 and a second antigen binding domain that specifically binds to LAG3. The invention further relates to methods of producing these molecules and to methods of using the same.

Bispecific antibodies specifically binding to PD1 and LAG3

Herein is reported a method for the production of a polypeptide that is biologically active as n-mer comprising a nucleic acid encoding a fusion polypeptide according to the following formula (B-CS-I-CS-FC-CS-I-CS-B), wherein B denotes a polypeptide that is biologically active as n-mer and forms non-defined aggregates/multimers upon expression in the absence of a fused Fc-region, FC denotes a heavy chain Fc-region polypeptide, CS denotes a cleavage site, and I denotes an intervening amino acid sequence, wherein FC does not substantially bind to an Fc-receptor, recovering the fusion polypeptide from the cell or the cultivation medium, optionally cleaving the fusion polypeptide with a protease, and thereby producing a polypeptide that is biologically active as n-mer and forms non-defined aggregates/multimers upon expression in the absence of a fused Fc-region.

Method for producing monomeric and multimeric molecules and uses thereof

The present invention relates to bispecific antibodies comprising at least one antigen binding site specific for DR5 and at least one antigen binding site specific for FAP, antibodies specific for DR5, methods for their production, pharmaceutical compositions containing said antibodies, and uses thereof.

Antibodies specific for DR5 and methods of use

Herein is reported a method for the determination of the simultaneous binding of a bispecific antibody to a first and a second antigen comprising the steps of a) incubating a cell expressing cell-membrane bound FRET-donor-tagged first antigen and FRET-acceptor-tagged second antigen with the bispecific antibody, and b) determining the simultaneous binding of the bispecific antibody by determining the energy transfer from the FRET-donor to the FRET-acceptor.

Cellular based fret assay for the determination of simultaneous binding

Herein is reported a method for the production of a polypeptide that is biologically active as n-mer comprising a nucleic acid encoding a fusion polypeptide according to the following formula (B-CS-I-CS-FC-CS-ICS-B), wherein B denotes a polypeptide that is biologically active as n-mer and forms non-defined aggregates/multimers upon expression in the absence of a fused Fc-region, FC denotes a heavy chain Fc-region polypeptide, CS denotes a cleavage site, and I denotes an intervening amino acid sequence, wherein FC does not substantially bind to an Fc-receptor, recovering the fusion polypeptide from the cell or the cultivation medium, optionally cleaving the fusion polypeptide with a protease, and thereby producing a polypeptide that is biologically active as n-mer and forms non-defined aggregates/multimers upon expression in the absence of a fused Fc-region.

The present invention relates to antibodies against human CSF-1R (CSF-1R antibody), methods for their production, pharmaceutical compositions containing said antibodies, and uses thereof.

Antibodies against human CSF-1R and uses thereof

Bispecific tetravalent antibodies against IL-17 and TNFa, useful in therapy, e.g. the treatment of rheumatoid arthritis and other autoimmune diseases and/or to reduce pathological inflammatory conditions.

TNFa-IL-17 bispecific antibodies

The present invention relates to antibodies against human CSF-1R (anti-CSF-1R antibody), methods for their production, pharmaceutical compositions containing said antibodies, and uses thereof.

Growing community of inventors

Penzberg, Germany

Stefan Seeber