Hoffmann-la Roche Inc.

Roche Glycart Ag

F. Hoffmann-la Roche Ag

Tilman Schlothauer

Guy Georges

Ekkehard Moessner

Hubert Kettenberger

Stefan Dengl

Jens Niewoehner

Ulrich Goepfert

Stefan Seeber

Michael Molhoj

Joerg Moelleken

Jens Fischer

Joerg Thomas Regula

Thomas Emrich

Christian Klein

Olaf Mundigl

Fiona Grueninger

Georg Fertig

Laurent Lariviere

Valeria Lifke

Viktor Levitski

Pablo Umana

Wolfgang Schaefer

Erhard Kopetzki

Pablo Umaña

Georg Tiefenthaler

Alexander Haas

Gregor Jordan

Peter Bruenker

Sabine Imhof-Jung

Kurt Lang

Petra Rueger

Claudia Ferrara Koller

Roberto Falkenstein

Guido Hartmann

Manfred Kubbies

Matthias Rueth

Christian Schantz

Andreas Schaubmar

Frank Herting

Monika Baehner

Thomas Friess

Claudio Sustmann

Sebastian Fenn

Richard Engh

Sylvia Herter

Stefan Jenewein

Maximiliane Koenig

Anton Jochner

Adrian Hugenmatter

Kevin Brady

Adrian Zwick

Mario Perro

Laura Codarri-Deak

Ildiko Wuensche

Shu Feng

Valeria Runza

Meher Majety

Martin Schaefer

Wei Shiong Adrian Ho

Michael Gertz

Runyi Adeline Lam

Maria Viert

Barbara Weiser

Hubert Hertenberger

Wolfgang Richter

Siok Wan Gan

Alexander Knaupp

Thomas Kraft

Angela Schoch

Ben-Fillippo Krippendorff

Christian Spick

Kasper Rand

Pernille Foged Jensen

Julia Schleypen

Herein is reported a method for determining the presence of antibody-Fab-FcRn interaction in an antibody-Fc-FcRn complex influencing the in vivo half-life comprising the steps of a) determining the retention time of the antibody on an FcRn affinity chromatography column with a positive linear pH gradient elution in the presence of a first sodium chloride concentration, and b) determining the retention time of the antibody on an FcRn affinity chromatography column with a positive linear pH gradient elution in the presence of a second sodium chloride concentration, whereby the presence of antibody-Fab-FcRn interaction in an antibody-Fc-FcRn complex influencing the in vivo half-life is determined if the retention time determined in step a) and the retention time determined in step b) are substantially different.

Vitro prediction of in vivo half-life

Herein is reported a polypeptide comprising a first polypeptide and a second polypeptide each comprising in N-terminal to C-terminal direction at least a portion of an immunoglobulin hinge region, which comprises one or more cysteine residues, an immunoglobulin CH2-domain and an immunoglobulin CH3-domain, wherein the first, the second, or the first and the second polypeptide comprise the mutation Y436A (numbering according to the EU index).

Method for producing bispecific antibodies comprising a Y436A Fc-region mutation for improved protein A-binding

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 provides humanized anti-human Tau(pS422) antibodies and methods of using the same.

Humanized anti-Tau(PS422) antibodies and methods of use

The present invention relates to antibodies and Fc-region fusion polypeptides which are asymmetrically modified with respect to their Fc-receptor, especially their FcRn, and methods of using the same.

Fc-receptor binding modified asymmetric antibodies and methods of use

Herein is reported an anti-transferrin receptor antibody that specifically binds to human transferrin receptor and cynomolgus transferrin receptor, which comprises i) a humanized heavy chain variable domain derived from the heavy chain variable domain of SEQ ID NO: 01, and ii) a humanized light chain variable domain derived from the light chain variable domain of SEQ ID NO: 26, wherein the antibody has an off-rate for the human transferrin receptor that is equal to or less than (i.e. at most) the off-rate of the anti-transferrin receptor antibody 128.1 for the cynomolgus transferrin receptor, whereby the off-rates are determined by surface plasmon resonance, and whereby the anti-transferrin receptor antibody 128.1 has a heavy chain variable domain of SEQ ID NO: 64 and a light chain variable domain of SEQ ID NO: 65.

Anti-transferrin receptor antibodies with tailored affinity

Herein is reported an antibody that specifically hinds to human CD 19, wherein the antibody comprises (a) HVR-H1 comprising the amino acid sequence of SEQ ID NO: 03, (b) HVR-H2 comprising the amino acid sequence of SEQ ID NO: 11, (c) HVR-H3 comprising the amino acid sequence of SEQ ID NO: 05, (d) HVR-L1 comprising the amino acid sequence of SEQ ID NO: 20 or 28, (e) HVR-L2 comprising the amino acid sequence of SEQ ID NO: 07, and (f) HVR-L3 comprising the amino acid sequence of SEQ ID NO: 08, as well as methods of using the same.

Humanized anti-human CD19 antibodies and methods of use

The present invention relates to bispecific anti-CCL2 antibodies binding to two different epitopes on human CCL2, pharmaceutical compositions thereof, their manufacture, and use as medicaments for the treatment of cancers, inflammatory, autoimmune and ophthalmologic diseases.

Bispecific anti-CCL2 antibodies

Herein is reported the use of an immobilized non-covalent complex of a neonatal Fc receptor (FcRn) and beta-2-microglobulin (b2m) as affinity chromatography ligand in general and, for example, for the determination of the in vivo half-live of an antibody by determining the ratio of the retention times of the antibody and a reference antibody.

Fc-receptor based affinity chromatography

Humanized anti-Tau(pS422) antibodies and methods of use

Fc-region variants with improved protein A-binding

The present invention relates to modified antibodies. In particular, the present invention relates to recombinant monoclonal antibodies having altered ability to induce direct cell death and effector function. In addition, the present invention relates to nucleic acid molecules encoding such antibodies, and vectors and host cells comprising such nucleic acid molecules. The invention further relates to methods for producing the antibodies of the invention, and to methods of using these antibodies in treatment of disease.

Antibody fab and Fc variants

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

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Penzberg, Germany

Tilman Schlothauer