Abstract: 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a reference or germline sequence and determining whether one or more threonine residues and/or serine residues have been replaced by a different amino acid residue, and ii) modifying the amino acid sequence of the immunoglobulin by reverting the exchanged threonine residues and/or serine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.

Abstract: The present invention relates to antigen binding proteins comprising two Fc parts, methods for their production, pharmaceutical compositions containing said antigen binding proteins, and uses thereof.

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

Abstract: The present invention relates to monovalent antigen binding proteins with a CH1-CL domain exchange, methods for their production, pharmaceutical compositions containing said antibodies, and uses thereof.

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

Abstract: The present invention relates to bispecific antibodies against human VEGF and against human ANG-2, methods for their production, pharmaceutical compositions containing said antibodies, and uses thereof.

Abstract: Herein are reported anti-ANG2 antibodies. A specific anti-ANG2 antibody comprises (a) a HVR-H1 comprising the amino acid sequence of SEQ ID NO: 29, (b) a HVR-H2 comprising the amino acid sequence of SEQ ID NO: 30, and (c) a HVR-H3 comprising the amino acid sequence of SEQ ID NO: 32.

Abstract: 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.

Abstract: The present invention relates to bispecific, bivalent antibodies against human vascular endothelial growth factor (VEGF/VEGF-A) and against human angiopoietin-2 (ANG-2), methods for their production, pharmaceutical compositions containing said antibodies, and uses thereof.

Abstract: 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.

Abstract: Herein is reported a method for selecting a full length antibody comprising the steps of a) generating from a parent full length antibody a plurality of full length antibodies by randomizing one or more amino acid residues selected from the amino acid residues at positions 1-23 in the heavy chain variable domain (numbering according to Kabat), at positions 55-83 in the light chain variable domain (numbering according to Kabat), at positions 145-174 in the first heavy chain constant domain (numbering according to EU index), and at positions 180-97 in the first heavy chain constant domain (numbering according to EU index), b) determining the binding strength of each of the full length antibodies from the 10 plurality of antibodies to the human neonatal Fc receptor (FcRn), and c) selecting a full length antibody from the plurality of full length antibodies that has a different binding strength to the FcRn than the parent full length antibody.

Abstract: The present invention relates to Bispecific antibodies against human TWEAK and human IL17 (bispecific TWEAK-IL17 antibodies), methods for their production, pharmaceutical compositions containing said antibodies, and uses thereof.

Abstract: The present invention relates to bispecific antibodies against human VEGF and against human ANG-2, methods for their production, pharmaceutical compositions containing said antibodies, and uses thereof.

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

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

Abstract: Herein is reported the use of a binding assay of a bivalent, bispecific antibody that has the smaller kD value (dissociation constant) for the interaction with its antigen for the immobilization of the bivalent, bispecific antibody to a solid surface for the determination of the biological activity of the bivalent, bispecific antibody.

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

Abstract: 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.

Abstract: 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.

Abstract: 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.