Roche Diagnostics Operations, Inc.

Roche Diagnostics Gmbh

Hoffmann-la Roche Inc.

F. Hoffmann-la Roche Ag

Alfred Engel

Elke Faatz

Christian Scholz

Herbert Andres

Peter Schaarschmidt

Urban Schmitt

Barbara Upmeier

Rainer Mueller

Harald Sobek

Toralf Zarnt

Michael Greif

Dorothea Sizmann

Marco Thomann

Ralf Bollhagen

Bernhard Suppmann

Sebastian Malik

Christine Jung

Ariuna Bazarsuren

Sandra Rutz

Johann Karl

Michael Schraeml

Andrea Horsch

Dirk Block

Ursula-Henrike Wienhues-Thelen

Thomas Meier

Rainer Schmuck

Helmut Schwab

Wilhelm Tischer

Christa Hubner-Parajsz

Michael Tacke

Reinhard Franze

Hartmut Duefel

Alfons Nichtl

Rosemarie Kientsch-Engel

Josef Burg

Beatus Ofenloch-Hahnle

Edelgard Anna Kaiser

Hartmut Ernst Schurig

Monika Soukupova

Tobias Oelschlaegel

Wojtek Steffen

Rainer M&uuml;ller

Gloria Tabares

Frank Kroner

Bernd Nidetzky

Pavel Kubalec

Peter Kastner

Christiane Luley

Harald Weisser

Manfred Wozny

Bernd Hilger

Ulrike Kurtkaya

Christina Zimmermann

Kerstin Kr&uuml;ger

Susanne Schmolke

Boris Pinchuk

Birgit Klapperich

Sabine Zitzenbacher

Katharina Schmoelzer

Doris Ribitsch

Tibor Czabany

Ekaterina Manuilova

Christina Rabe

Rainer Schlecht

Romina Eisenhauer

Anna Edelgard Kaiser

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 describes a method for predicting the risk of a patient to suffer from acute kidney injury (AKI) during or after a surgical procedure or after administration of a contrast medium. The method is based on the determination of the level of the biomarker IGFBP7 (Insulin-like Growth Factor Binding Protein 7) in a body fluid sample obtained from the patient prior to the surgical procedure or prior to the administration of a contrast medium. Further, the present disclosure describes a method for predicting the risk of a patient to suffer from acute kidney injury (AKI) based on the determination of the amount of the biomarker IGFBP7 (Insulin-like Growth Factor Binding Protein 7) and Cystatin C in a body fluid sample obtained from the patient. The present disclosure further encompasses kits and devices adapted to carry out the methods of the disclosed methods.

IGFBP7 for prediction of risk of AKI when measured prior to surgery

The disclosure describes a recombinant immunoglobulin heavy chain comprising a sortase conjugation loop, methods for conjugating and/or labeling such recombinant immunoglobulin heavy chains by use of the enzyme sortase and to the conjugates/labeled products obtained via the method.

Recombinant immunoglobulin heavy chains comprising a sortase conjugation loop and conjugates thereof

The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. Contrary to previous findings certain truncations were found to exhibit sialidase enzymatic activity, particularly a variant of human sialyltransferase (hST6Gal-I) with a truncation deletion involving the first 89 N-terminal amino acids of the respective wild-type polypeptide. A fundamental finding documented in the present disclosure is that there exists a variant of this enzyme which is capable of catalyzing transfer of a glycosyl moiety as well as hydrolysis thereof. Thus, disclosed is a specific exemplary variant of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variant of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.

Quantitative control of sialylation

The present disclosure is directed to the use of certain glycosyltransferase variants having N-terminal truncation deletions. It was found that the combination of two different truncation variants of human &#x3b2;-galactoside-&#x3b1;-2,6-sialyltransferase I (hST6Gal-I) exhibited different specific sialyltransferase enzymatic activities. In one example, under conditions wherein the first variant &#x394;89 hST6Gal-I catalyzed formation of bi-sialylated target molecules the second variant &#x394;108 hST6Gal-I catalyzed formation of mono-sialylated target molecules. Thus, disclosed are variants of mammalian glycosyltransferase, nucleic acids encoding the same, methods and means for recombinantly producing the variants of mammalian glycosyltransferase and use thereof, particularly for sialylating in a quantitatively controlled manner terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.

Quantitative control of sialylation and specific mono-sialylation

The invention relates to soluble rubella E1 antigens and variants of these antigens. The antigens contain amino acids 201 to 432 or 169 to 432 and are lacking amino acids 453 to 481 as well as at least the amino acids 143 to 164. They further contain a region spanning two disulfide-bridges. The invention also relates to a recombinant DNA molecule encoding the rubella E1 antigens, the expression of rubella E1 antigens as chaperone fusion proteins and their use in a method of detecting antibodies against rubella in a sample.

Rubella E1 envelope protein variants and their use in detection of anti-rubella antibodies

The present invention relates to the cloning and expression of foreign protein or polypeptides in bacteria, such as. In particular, this invention relates to expression tools comprising a FKBP-type peptidyl prolyl isomerase selected from the group consisting of FkpA, SlyD, and trigger factor; methods of recombinant protein expression, the recombinant polypeptides thus obtained, as well as to the use of such polypeptides.

Methods for producing fusion polypeptides or enhancing expression of fusion polypeptides

A soluble rubella E1 antigen variant is disclosed that comprises amino acids 334-409 of the native rubella E1 peptide, but lacks the C-terminal end and at least the transmembrane region and the anchor segment as well as at least the amino acids 143 to 164. Also described is a recombinant DNA molecule encoding the rubella E1 antigen variants which are recombinantly expressed as a chaperone fusion protein, refolded into a soluble and immunoreactive conformation, and further used for the serological detection of anti-rubella antibodies. In addition, also disclosed is a method for the detection, determination and quantification of anti-rubella antibodies of IgG and/or IgM subclass in a sample wherein the rubella E1 antigen is used as a capture reagent and/or binding partner for the antibodies.

Soluble rubella E1 envelope protein variants

The present invention relates to the cloning and expression of foreign protein or polypeptides in bacteria, such asIn particular, this invention relates to expression tools comprising a FKBP-type peptidyl prolyl isomerase selected from the group consisting of FkpA, SlyD, and trigger factor; methods of recombinant protein expression, the recombinant polypeptides thus obtained, as well as to the use of such polypeptides.

Fusion polypeptides, vaccines and compositions of FKBP chaperones and target polypeptides

The present invention relates to the diagnosis of HIV infections. It especially teaches the production of a soluble retroviral surface glycoprotein-(or transmembrane glycoprotein)-chaperone complex and the advantageous use of a chaperone-antigen complex especially in the detection of antibodies to HIV in immunoassays, preferably according to the double antigen bridge concept, or as an immunogen. The invention also discloses soluble complexes comprising a variant of HIV-1 gp41 or a variant of HIV-2 gp36, respectively, and a chaperone selected from the peptidyl-prolyl-isomerase class of chaperones. Variants comprising specific amino-acid substitutions in the N-helical domain of HIV-1 gp41 or of HIV-2 gp36, respectively, are also described.

Soluble complex comprising a retroviral surface glycoprotein

The present invention refers to conjugates of erythropoietin with poly(ethylene glycol) comprising an erythropoietin glycoprotein having an N-terminal &#x3b1;-amino group and having the in vivo biological activity of causing bone marrow cells to increase production of reticulocytes and red blood cells and selected from the group consisting of human erythropoietin and analogs thereof which have the sequence of human erythropoietin modified by the addition of from 1 to 6 glycosylation sites or a rearrangement of at least one glycosylation site; said glycoprotein being covalently linked to one poly(ethylene glycol) group of the formula&#x2014;CO&#x2014;(CH)&#x2014;(OCHCH)&#x2014;ORwherein the &#x2014;CO of the poly(ethylene glycol) group forms an amide bond with said N-terminal &#x3b1;-amino group; and wherein R is lower alkyl; x is 2 or 3; and m is from about 450 to about 1350.

Erythropoietin conjugates

The present invention relates to the diagnosis of HIV infections. It especially teaches the production of a soluble retroviral surface glycoprotein- (or transmembrane glycoprotein)-chaperone complex and the advantageous use of a chaperone-antigen complex especially in the detection of antibodies to HIV in immunoassays, preferably according to the double antigen bridge concept, or as an immunogen. The invention also discloses soluble complexes comprising a variant of HIV-1 gp41 or a variant of HIV-2 gp36, respectively, and a chaperone selected from the peptidyl-prolyl-isomerase class of chaperones. Variants comprising specific amino-acid substitutions in the N-helical domain of HIV-1 gp41 or of HIV-2 gp36, respectively, are also described.

Soluble complexes of target proteins and peptidyl prolyl isomerase chaperones and methods of making and using them

DNA molecule comprising a structural gene which codes for a bacterial protein with the enzymatic activity of 3-hydroxybutyrate dehydrogenase (3-HBDH), a recombinant DNA containing the DNA molecule, microorganisms transformed accordingly, a process for obtaining 3-HBDH by culturing a suitable transformed microorganism as well as a method for the determination of ketone bodies in the presence of the enzyme. A structural gene from Rhodobacter sphaeroides is preferred.

Recombinant microbial 3-hydroxybutyrate dehydrogenase a process for its production and the use thereof

The present invention concerns an antibody against a hepatitis G virus antigen as well as a fragment of this antibody. The invention additionally concerns hybridoma cell lines as well as a conjugate that contains this antibody or the antibody fragment coupled to a biological molecule. Finally the present invention concerns the use of the antibody for the diagnostic detection of hepatitis G virus.

Antibodies against hepatitis G virus and their use for the diagnostic

Growing community of inventors

Tutzing, Germany

Alfred Engel