Roche Diagnostics Operations, Inc.

Hoffmann-la Roche Inc.

Roche Diabetes Care, Inc.

Roche Diagnostics Gmbh

F. Hoffmann-la Roche Ag

Hartmut Duefel

Christian Scholz

Michael Schraeml

Michael Gerg

Herbert Andres

Thomas Meier

Dieter Heindl

Michael Tacke

Frank Kowalewsky

David Casagolda Vallribera

Carina Horn

Urban Schmitt

Uwe Kobold

Roberto Falkenstein

Rainer Schmuck

Wilhelm Tischer

Peter Schaarschmidt

Alfred Engel

Ulrich Schwaneberg

Andreas Leinenbach

Gloria Tabares

Frank Kroner

Alexander Riedel

Hemanshu Mundhada

Ulrike Kurtkaya

Michael Schraemi

Sandra Rutz

Boris Pinchuk

Marco Bocola

Erik Uwe Arango Gutierrez

Christina Zimmermann

Iris Lein

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 is directed at an antibody conjugate having an antibody and a tag, wherein one or more element(s) present in the antibody exhibit an isotope ratio which differs from the naturally occurring isotope ratio of the one or more element(s), wherein the amount of the isotope which is less-common in nature, is increased to at least 4% of the atoms of the respective element in the antibody, as well as uses thereof.

Methods of protecting the sequence of an antibody conjugate from being determined

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

Isolated antibodies that specifically bind to an epitope comprised in the stretch of amino acids ranging from amino acid 76 to amino acid 84 of human insulin-like growth factor-1 precursor (SEQ ID NO:1). Use of the novel antibodies for the sensitive and specific detection of insulin-like growth factor-1, in some embodiments while in the presence of high excess concentration of insulin-like growth factor-2, for example in a bodily fluid sample.

Antibody specifically binding to insulin-like growth factor-1

The invention concerns a fusion polypeptide including several molecules of folding helper polypeptides, including one multimerization domain, in particular Skp, and at least one molecule of SlyD or SlpA, wherein no further target polypeptide sequences are fused to the fusion polypeptide. The invention further concerns an immunoassay and the use of the fusion polypeptide in an immunoassay for reduction of interferences or minimizing false positive results or for stabilizing proteinaceous assay reagents. Further the invention concerns a reagent kit for use in an immunoassay comprising the fusion polypeptide.

Chaperone-chaperone fusion polypeptides for reduction of interference and stabilization of immunoassays

Herein is reported a fusion polypeptide according to formula INH&#x2014;S&#x2014;X&#x2014;S&#x2014;COOH&#x2003;&#x2003;(formula I)wherein

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

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

Herein is reported a fusion polypeptide according to formula (I): NH&#x2014;S&#x2014;X&#x2014;S&#x2014;COOH, wherein Xcomprises 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 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.

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

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Schlehdorf, Germany

Hartmut Duefel