Hoffmann-La Roche Inc.

Roche Diagnostics Operations, Inc.

Roche Sequencing Solutions, Inc.

Roche Molecular Systems, Inc.

Ventana Medical Systems, Inc.

Scil Proteins Gmbh

Roche Diagnostics Oeprations, Inc.

Roche Diagnostics Gmbh

F. Hoffmann-La Roche Ag

Dynamic Biosensors Gmbh

Michael Schraeml

Michael Gerg

Birgit Bossenmaier

Christian Scholz

Gerhard Niederfellner

Guy Georges

Leopold Von Proff

Victor I Lyamichev

Dieter Heindl

Frank Bergmann

Jigar Patel

Thomas J Albert

Hartmut Duefel

Herbert Andres

Olaf Mundigl

Ulrich Goepfert

Thomas Meier

Fiona Grueninger

Bernd Bohrmann

Wolfgang Schaefer

Hans-Peter Josel

Hubert Kettenberger

Joerg Benz

Michael Tacke

Markus Roessler

Christian Klein

Herbert Von Der Eltz

Christoph Seidel

Alfred Mertens

Erasmus Huber

Stefan Dengl

Hans-Willi Krell

Erik Fiedler

Martin Lanzendoerfer

Alfred Engel

Valeria Lifke

Claudio Sustmann

Ulrich Rant

Sonja Offner

Manfred Watzele

Walter Huber

Andreas Langer

Andreas Gallusser

Patrick C Roche

Sebastian Dziadek

Volker Schmid

David Casagolda Vallribera

Wojtek Steffen

Thomas Streidl

Frank Kroner

Carmen Peess

Richard John Buick

Monika Soukupova

Tobias Oelschlaegel

Klaus Hirzel

Caroline Dorothea Hojer

Mohamed Yosry Hassan Mohamed

Ralf Strasser

Frank Kowalewsky

Gloria Tabares

Edgar Voss

Lars Hillringhaus

Laurence Ozmen

Johannes Stoeckel

Sandra Rutz

Thomas Albert

Ulrike Kurtkaya

Boris Pinchuk

Christina Zimmermann

Florian Huber

Sarah Liedke

Dorothee Ambrosius

Jan Van Dieck

Steffen Wojtek

Richard Buick

Christoph Rutz

Romina Eisenhauer

The present invention relates to a monoclonal antibody capable of binding to biotin. In one embodiment the monoclonal antibody according to the invention also does not bind to a biotin moiety on a biotinylated molecule, wherein the biotin moiety is attached to the molecule via the carbon atom of the carboxyl function of the valeric acid moiety of biotin. Also disclosed is a method for generation of an antibody as discloed herein. The monoclonal antibody according to the invention is of specific use in a method for measuring an analyte in a sample, wherein a (strept)avidin/biotin pair is used to bind a biotinylated analyte specific binding agent to a (strept)avidin coated solid phase.

Biotin-specific monoclonal antibody and use thereof

The present invention relates to improved variant monoclonal antibodies binding to cardiac troponin T and having a better Kthan the monoclonal antibody 12.1A11.11-7, produced by hybridoma clone 7.1 A 12.2-22 (ECACC 89060901) as deposited with European Collection of Animal Cell Cultures, GB.

Anti-troponin T antibodies

The present invention relates to a method for determining the total amount and/or concentration of an analyte in the presence of a binding molecule as well as kits, compositions and uses relating thereto.

Method for determining the total amount and/or concentration of an analyte in the presence of a binding molecule as well as kits, compositions and uses relating thereto

The present invention relates to a novel monoclonal antibody that specifically binds to a conformation dependent epitope on human thymidine kinase 1 (hTK-1; SEQ ID NO:1), to methods for quantifying hTK-1 employing the antibody and to the use of the anti-hTK-1 antibody in quantifying hTK-1.

Anti-thymidine kinase antibodies

Herein is reported a polypeptide-polynucleotide-complex as therapeutic agent and its use as tool for the targeted delivery of an effector moiety. The polynucleotide part of the complex is essentially resistant to proteolytic and enzymatic degradation in vivo. Additionally the polypeptide part specifically binds to a compound or structure such as a tissue or organ, a process or a disease. Thus, one aspect as reported herein is a polypeptide-polynucleotide-complex comprising a) a polypeptide specifically binding to a target and conjugated to a first member of a binding pair, b) a polynucleotide linker conjugated at its first terminus to the second member of the binding pair, and c) an effector moiety conjugated to a polynucleotide that is complementary to at least a part of the polynucleotide linker.

Polypeptide-polynucleotide-complex and its use in targeted effector moiety delivery

The current invention reports a method for producing an antibody comprising the steps of a) providing a plurality of hybridoma cells each expressing an antibody, b) determining the time dependent amount of said antibody bound to the respective antigen by surface plasmon resonance at different temperatures and different antibody concentrations, c) calculating with the time dependent amount determined in b) based on equations (II) to (XIII) at least the thermodynamic parameters (i) standard association binding entropy (&#x394;S&#xb0;&#x2021;ass), (ii) standard dissociation binding entropy (&#x394;S&#xb0;&#x2021;diss), (iii) standard binding entropy (&#x394;S&#xb0;), (iv) free standard binding enthalpy (&#x394;G&#xb0;), (v) standard dissociation free binding enthalpy (&#x394;G&#xb0;&#x2021;diss), (vi) standard association free binding enthalpy (&#x394;G&#xb0;&#x2021;ass), (vii) &#x2212;T&#x394;S&#xb0;, (viii) dissociation rate constant k, (ix) equilibrium binding constant K, and (x) association rate constant k, d) selecting a hybridoma cell producing an antibody with at least two of the following: i) a standard association binding entropy of less than 10 J/K*mol, ii) an absolute standard dissociation binding entropy of 100 J/mol*K or more, iii) an absolute standard binding entropy of 100 J/mol*K or more, e) producing an antibody by cultivating said selected cell under conditions suitable for the expression of said antibody and recovering said antibody from the cells or/and the cultivation medium.

Method to screen high affinity antibody

In one aspect, the present disclosure provides a system and method for the identification and characterization of a transglutaminase. Further, the present disclosure provides transglutaminase enzymes for forming isopeptide bonds, methods of forming isopeptide bonds in the presence of transglutaminases, and substrate tags for use with transglutaminases. In another aspect, the present disclosure provides glutamine-containing substrates (or Q-tag substrates) that are more resistant to proteases/clipping and therefore, more stable, than other Q-tag substrates, and their uses in substrate tags for cross-linking to an amine-donor tag via an isopeptide bond mediated by a microbial transglutaminase.

System and method for identification and characterization of transglutaminase species

According to one aspect, the present disclosure provides a method of identifying a substrate of a transglutaminase using a peptide array comprising a plurality of peptides. The method includes the steps of contacting the peptides in the peptide array with the transglutaminase, allowing the transglutaminase to bind to the peptides, and identifying the substrate of the transglutaminase.

Identification of transglutaminase substrates and uses therefor

A bivalent binding agent having a first monovalent binder that binds to a polypeptide epitope of a target polypeptide, a second monovalent binder that binds to a posttranslational polypeptide modification on the target polypeptide and a linker. Further disclosed are methods for the detection of a posttranslationally modified target polypeptide, for making the disclosed bivalent binding agent, and for use of the disclosed bivalent binding agent in histological staining procedures.

Detection of a posttranslationally modified polypeptide by a bivalent binding agent

The current invention is directed to the velocity factor. Based on the velocity factor antibodies can be classified, i.e. antibodies can be characterized on their binding properties as e.g. entropic or enthalpic antigen binder. A velocity factor based classification does not require detailed thermodynamic determinations and/or calculations. The velocity factor is the ratio of the antigen-antibody complex association rate constants ka determined at 37&#xb0; C. and 13&#xb0; C. As only two experimental determinations are required to calculate the velocity factor this is a fast and high-throughput suited method.

Velocity factor

The invention relates to HER3/HER2 bispecific antibodies binding to the beta-hairpin of HER3 and domain II of HER2, their preparation and use as medicament.

HER3/HER2 bispecific antibodies binding to the beta-hairpin of HER3 and domain II of HER2

In one aspect, the present disclosure provides a system and method for the identification and characterization of a transglutaminase. Further, the present disclosure provides transglutaminase enzymes for forming isopeptide bonds, methods of forming isopeptide bonds in the presence of transglutaminases, and substrate tags for use with transglutaminases.

Herein is reported a fusion polypeptide according to formula INH&#x2014;S&#x2014;X&#x2014;S&#x2014;COOH&#x2003;&#x2003;(formula I)whereinXcomprises either a random amino acid sequence or an amino acid sequence derived from a first polypeptide,S2 and S1 are non-overlapping amino acid sequences derived from a second polypeptide, and&#x2014; denotes a peptide bond,wherein the second polypeptide is a polypeptide with peptidyl-prolyl cis/trans-isomerase activity (PPIase activity) or is derived from the FKBP-fold domain family, wherein Xis inserted in place of the insert-in-flap-domain of the second polypeptide.

Amino acid sequence presenting fusion polypeptide and its use

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Penzberg, Germany

Michael Schraeml