Hoffmann-la Roche Inc.

Bristol-myers Squibb Compnay

Engmab Ag

F. Hoffmann-la Roche Ag

Engmab Sarl

Engmab Beta Holdings LLC

Stefan Klostermann

Christian Klein

Wolfgang Schaefer

Pablo Umana

Joerg Thomas Regula

Michael Molhoj

Marina Bacac

Oliver Ast

Ekkehard Moessner

Sabine Imhof-Jung

Christiane Neumann

Tanja Fauti

Lydia Jasmin Hanisch

Pablo Umaña

Hubert Kettenberger

Ralf Hosse

Kay-Gunnar Stubenrauch

Stefan Dengl

Anne Freimoser-Grundschober

Georg Tiefenthaler

Jens Fischer

Ulrich Kohnert

Joerg Benz

Rudolf Vogel

Uwe Wessels

Ulrich Essig

Klaus Strein

Guy Georges

Erhard Kopetzki

Joerg Moelleken

Alexander Haas

Sebastian Fenn

Sabine Hoves

Tina Weinzierl

Sonja Offner

Johannes Auer

Apollon Papadimitriou

Alexander Bujotzek

Samuel Moser

Wei Xu

Minh Diem Vu

Johannes Sam

Sylvia Herter

Frank Kowalewsky

Sebastian Neumann

Meher Majety

Ramona Murr

Sabine Jung-Imhof

Claudia Kirstenpfad

Francesca Ros

Christiane Jaeger

Friederike Jung

Ursula Schwarz

Estelle Marrer-Berger

Esther Koenigsberger

Alejandro Carpy Gutierrez Cirlos

Jasmin Sydow-Andersen

Simon Patrick Keiser

Andreas Hinz

Florian Lipsmeier

Anne Freimoser-grundschober

Frederic Schultz

Clemens Wrzodek

Jasmin Sydow-andersen

Alain Tissot

Herein is reported an antibody binding to rabbit CD19 comprising (a) a HVR-H1 comprising the amino acid sequence of SEQ ID NO: 32 or 33 or 34, (b) a HVR-H2 comprising the amino acid sequence of SEQ ID NO: 35 or 36, (c) a HVR-H3 comprising the amino acid sequence of SEQ ID NO: 37, (d) a HVR-L1 comprising the amino acid sequence of SEQ ID NO: 38, (e) a HVR-L2 comprising the amino acid sequence of SEQ ID NO: 39, and (f) a HVR-L3 comprising the amino acid sequence of SEQ ID NO: 40, as well as methods of using the same, especially in the identification and selection of antibody producing rabbit B-cells.

Anti-rabbit CD19 antibodies and methods of use

The present invention relates to anti-HLA-G antibodies and methods of using the same.

Anti-HLA-G antibodies and methods of use thereof

The present invention generally relates to antibodies that bind to HLA-A2/WT1, including bispecific antigen binding molecules e.g. for activating T cells. In addition, the present invention relates to polynucleotides encoding such antibodies, and vectors and host cells comprising such polynucleotides. The invention further relates to methods for producing the antibodies, and to methods of using them in the treatment of disease.

Antibodies binding to HLA-A2/WT1

The present invention generally relates to antibodies that bind to HLA-A2/MAGE-A4, including multispecific antibodies e.g. for activating T cells. In addition, the present invention relates to polynucleotides encoding such antibodies, and vectors and host cells comprising such polynucleotides. The invention further relates to methods for producing the antibodies, and to methods of using them in the treatment of disease.

Antibodies binding to HLA-A2/MAGE-A4

Anti-HLA-G antibodies and use thereof

The present invention relates to bispecific antibodies against ROR1 and CD3, their manufacture and use.

Bispecific antibodies against CD3EPSILON and ROR1

Herein is reported a method for the humanization of non-human antibodies using a structure-based scoring matrix. With the scoring matrix it is possible to determine (the requirement for and) the suitability of specific (back)mutations of amino acid residues at defined positions of a selected human germline sequence. The scoring matrix takes into account the topology, the three-dimensional structure and the interactions of the respective residue and change. Thereby the influence on antigen binding of a specific amino acid residue change can be determined.

Three-dimensional structure-based humanization method

The present invention generally relates to novel bispecific antigen binding molecules for T cell activation and re-direction to specific target cells. In addition, the present invention relates to polynucleotides encoding such bispecific antigen binding molecules, and vectors and host cells comprising such polynucleotides. The invention further relates to methods for producing the bispecific antigen binding molecules of the invention, and to methods of using these bispecific antigen binding molecules in the treatment of disease.

Bispecific T cell activating antigen binding molecules

Herein is reported a method for selecting or deselecting an antibody comprising a) determining for each Asp and Asn residue in an antibody Fv region the conformational flexibility of the C-atom using a homology model ensemble, b) determining for each Asp and Asn residue in an antibody Fv region the size of the amino acid residue C-terminal to the Asp or Asn residue, and c) selecting an antibody in which the C-atom is conformationally inflexible and/or the Asp or Asn has a big C-terminal amino acid residue, or deselecting an antibody in which the C-atom has a moderate to high conformational flexibility and/or the Asp or Asn has a small C-terminal amino acid residue.

Method for improving antibody stability

A bispecific bi- or trivalent antibody specifically binding to the two targets which are extracellular domain of human B cell maturation antigen (BCMA) and human CD3&#x3b5;, wherein the variable domains VL and VH in a light chain and the respective heavy chain are replaced by each other, characterized in comprising a constant domain CL wherein the amino acid at position 124 is substituted independently by lysine (K), arginine (R) or histidine (H) (numbering according to Kabat), and in the respective constant domain CH1 the amino acid at position 147 and the amino acid at position 213 is substituted independently by glutamic acid (E), or aspartic acid (D) (numbering according to EU index of Kabat). Also the manufacture and use of said antibody.

Bispecific antibodies against CD3&#x3f5; and BCMA

Herein is reported a method for reducing the aggregation of an immunoglobulin in solution comprising the steps of i) comparing the amino acid sequence of the fourth framework region of the heavy chain of an antibody with a reference or germline sequence and determining whether one or more threonine residues and/or serine residues have been replaced by a different amino acid residue, and ii) modifying the amino acid sequence of the immunoglobulin by reverting the exchanged threonine residues and/or serine residues back to threonine or serine of the reference or germline sequence and thereby reducing the aggregation of an immunoglobulin in solution.

Sequence dependent aggregation

Growing community of inventors

Neuried, Germany

Stefan Klostermann