Roche Diagnostics Operations, Inc.

Roche Diabetes Care, Inc.

Hoffmann-la Roche Inc.

Roche Molecular Systems, Inc.

Max-planck-gesellschaft Zur F&#xf6;rderung Der Wissenschaften E. V.

Roche Diagnostics Gmbh

F. Hoffmann-la Roche Ag

Thomas Meier

Dieter Heindl

Rainer Schmuck

Carina Horn

Hartmut Duefel

Bernd Schneidinger

Michael Schraeml

Joachim Hoenes

Hans-Peter Josel

Christoph Seidel

Michael Gerg

Michael Tacke

Michael Marquant

Wolfgang Petrich

Erasmus Huber

Roberto Falkenstein

Eva Hoess

Wilhelm Tischer

Klaus Reichert

Klaus Hirzel

Christopher J Nelson

Waltraud Ankenbauer

Arnulf Staib

Rolf Deeg

Alfred Engel

Christa Hubner-Parajsz

Bernhard Schaffar

Rolf Nagel

Zhixin Shao

Peter Kratzsch

Reinhold Mischler

Otto Gaa

Claudia Gaessler-Dietsche

Ulrich Schwaneberg

Christine Markert-Hahn

Leopold Von Proff

Michael Wiedmann

Friedrich Popp

Caroline Dorothea Hojer

Andreas Gallusser

Rosemarie Kientsch-Engel

Martin Kaufmann

Elmar Weinhold

Hartmut Schetters

Nelli Steinke

Peter Gebauer

Martin Hajnsek

Bernd Nidetzky

Wolfgang Roedel

Gloria Tabares

Frank Kroner

Lars Hillringhaus

Hemanshu Mundhada

Gabriele Pestlin

Edgar Voss

Stacy H Duvall

Wolfgang Rödel

Eberhard Russmann

Ulrike Kurtkaya

Sandra Rutz

Hannes Kirzinger

Gabriele Chemnitius

Marco Bocola

Erik Uwe Arango Gutierrez

Boris Pinchuk

Christina Zimmermann

Florian Huber

Tobias Graf

Nadine Bucci

Harald Peschel

Thomas Stoisser

Jessica Strey

Gisela Betzl

Annette Deufel

Hartmut Düfel

Claudia Gässler-Dietsche

Eberhard Russman

Uwe Wehnes

Johnny Staepels

Ranier Schmuck

Stefan Leitgeb

Karl Recht

Tarik Khan

Sanjay Gupta

Hartmut Dufel

Thomas Mag Rer Nat Stoisser

Thomas Nagel

Joachim Hönes

Michael Leiss

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 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

The present disclosure provides an aqueous composition comprising a purified thermostable polypeptide with biological activity, and a purified thermolabile water-soluble substance which in a functional conformation at a permissive temperature absorbs light and/or exhibits fluorescence, wherein the maximal permissive temperature of the polypeptide is above the maximal permissive temperature of the substance. The present disclosure further provides methods employing such a composition, and kits containing ingredients to form such a composition.

Compositions with thermolabile dyes

Novel glucose oxidase (GOx) variants are disclosed that have the substitutions of T30V and I94V set forth in SEQ ID NO:1, and additionally at least one further amino acid substitution in the enzyme sequence in any of the positions S53; A137; A173; A332; F414 and V560. The GOx variants herein exhibit specificity for glucose and significantly reduced oxygen consumption rates and/or increased enzyme activity for electron mediators other than oxygen. Also provided are assay devices incorporating at least one of the GOx variants herein for improved blood glucose measurements.

Glucose oxidase variants and methods of using the same

Azo compounds are disclosed that do not form azoxy dimers and that do not have any reactive nitroso groups. Also disclosed are use of the azo compounds as mediators in optical and electrochemical diagnostic methods, as well as detection reagents, kits and test elements that include such azo compounds and that can be used in the diagnostic methods.

Azo mediators and methods of use thereof

The invention also relates to compounds, which are useful for intra-molecular fluorescence resonance energy transfer (FRET), comprising the oxidized form of a carbaNADH-based first fluorophore and a second fluorophore that is excitable at a wave-length of between 445 to 540 nm and that has an emission maximum of greater than 560 nm, and methods, kits and compositions related thereto.

Compounds useful for FRET and methods related thereto

Compositions, devices, kits and methods are disclosed for assaying glucose with a glycosylated, modified flavin adenine dinucleotide-dependent glucose dehydrogenase (FAD-GDH), variant thereof or an active fragment thereof, where at least one asparagine residue at positions N2, N168 and N346 of mature, wild-typeFAD-GDH according to SEQ ID NO:2 is substituted by one or more amino acids not suitable for glycosylation, thereby eliminating or inactivating, respectively, a potential glycosylation site at this position.

Glycosylated modified flavin adenine dinucleotide-dependent glucose dehydrogenases, compositions thereof as well as methods of making and using the same

Methods for stabilizing an enzyme by storing the enzyme in the presence of a stabilized coenzyme are disclosed. In addition, an enzyme stabilized with a stabilized coenzyme as well as the use thereof in test elements for detecting analytes are also disclosed. Other aspects include unique compositions, methods, techniques, systems and devices involving enzyme stabilization.

Stabilization of enzymes with stable coenzymes

The present invention concerns a method for determining an analyte as well as a diagnostic element suitable therefore. In one particular form, a method for determining an analyte includes contacting a sample containing the analyte with a diagnostic element comprising a dry reagent layer. The dry reagent layer contains a mutated dehydrogenase which is specific for the analyte and an artificial coenzyme. The method also includes determining at least one of analyte presence and an amount of the analyte.

Fast reaction kinetics of enzymes having low activity in dry chemistry layers

The disclosure concerns a high efficiency electrochemical sensor with high signal yield for determining an analyte in a fluid medium comprising, at least one reference electrode, at least one working electrode having particles of an electrocatalyst in an electrode matrix, and an enzyme that is suitable for determining an analyte is selectively covalently bound to the particles of the electrocatalyst. The disclosure also describes a process for producing the electrochemical sensor and a method for determining an analyte in a fluid medium using the electrochemical sensor. have a high efficiency and thus achieve a high signal yield.

Continuous monitor sensor with covalently bound enzyme

The present disclosure relates to a mutant lactate oxidase having increased stability, a nucleic acid encoding the mutant lactate oxidase, an expression vector comprising the nucleic acid, a host cell comprising the nucleic acid or the expression vector, a method of determining lactate in a sample, the use of the mutant lactate oxidase for determining lactate, a device for determining lactate in a sample using the mutant lactate oxidase and a kit for determining lactate comprising the mutant lactate oxidase.

Mutant lactate oxidase with increased stability and product, methods and uses involving the same

The disclosure concerns the enzymatic synthesis of stable analogues of nicotinamide adenine dinucleotide NAD/NADH and nicotinamide adenine dinucleotide phosphate NADP/NADPH, the so-called 'carba-NADs', i.e. analogues of NAD/NADH or NADP/NADPH, respectively, comprising a carbacyclic sugar instead of ribose.

Enzymatic synthesis of carba-NAD

A method for detecting sequence specific methylation in a biomolecule, comprising: (a) contacting the biomolecule with an S-adenosyl-L-methionine-dependent methyltransferase in the presence of a detectable cofactor of said methyltransferase; and (b) detecting whether the recognition sequence of said methyltransferase has been modified with the cofactor or a derivative thereof, wherein modification of the recognition sequence of said methyltransferase is indicative of an absence of methylation at said recognition sequence. Also disclosed is a cofactor specific for S-adenosyl-L-methionine-dependent methyltransferases, wherein said cofactor is an N-adenosylaziridine derivative with a reporter group attached to the 6 or 7 position of the adenine ring or attached to the aziridine ring. A complex of the cofactor and a methyltransferase a composition comprising the cofactor or the complex and the use of the cofactor or the complex for detecting sequence-specific methylation in DNA molecules are also disclosed.

Sequence-specific detection of methylation in biomolecules

It was found that a fragment of nativeDNA polymerase (TaqWT) lacking 288 N-terminal amino acids (Taq&#x394;288) possesses an increased thermostability over TaqWT, Taq&#x394;279, and Taq&#x394;289. The present invention therefore provides Taq&#x394;288, recombinant expression vectors encoding the same or derivatives thereof, as well as purification protocols for Taq&#x394;288. The invention also encompasses kits containing Taq&#x394;288 as well as the use of Taq&#x394;288 and kits containing Taq&#x394;288. In addition, the invention encompasses methods for the sequencing a nucleic acid template and methods for amplifying a target nucleic acid.

Thermostable Taq polymerase fragment

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Munich, Germany

Thomas Meier