Patents by Inventor Alfred Engel
Alfred Engel has filed for patents to protect the following inventions. This listing includes patent applications that are pending as well as patents that have already been granted by the United States Patent and Trademark Office (USPTO).
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Publication number: 20230095167Abstract: The present invention relates to a method for assessing atrial fibrillation in a subject, said method comprising the steps of determining the amount of BMP10 in a sample from the subject, and comparing the amount of BMP10 to a reference amount, whereby atrial fibrillation is to be assessed. Moreover, the present invention relates to a method for diagnosing heart failure based on the determination of BMP 10 in a sample from a subject. Further, the present invention relates to a method for predicting the risk of a subject of hospitalization due to heart failure based on the determination of a BMP10-type peptide in a sample from a subject. The present invention further pertains to antibodies which bind to one or more BMP10-type peptides such as NT-proBMP10.Type: ApplicationFiled: February 19, 2021Publication date: March 30, 2023Inventors: Alfred Engel, Michael Gerg, Ute Jucknischke, Johann Karl, Peter Kastner, Thomas Meier, Lars Hillringhaus, Ulrich Schotten, Vinzent Rolny, Ursula-Henrike Wienhues-Thelen, André Ziegler, Roberto Latini, Jennifer Marie Theresia Anna Meessen
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Patent number: 11397187Abstract: 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.Type: GrantFiled: April 2, 2018Date of Patent: July 26, 2022Assignee: Roche Diagnostics Operations, Inc.Inventors: Andrea Horsch, Birgit Klapperich, Dirk Block, Alfred Engel, Johann Karl, Rosemarie Kientsch-Engel, Ekaterina Manuilova, Christina Rabe, Sandra Rutz, Monika Soukupova, Ursula-Henrike Wienhues-Thelen, Peter Kastner, Edelgard Anna Kaiser
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Recombinant immunoglobulin heavy chains comprising a sortase conjugation loop and conjugates thereof
Patent number: 11136376Abstract: 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.Type: GrantFiled: March 23, 2018Date of Patent: October 5, 2021Assignee: Roche Diagnostics Operations, Inc.Inventors: Alfred Engel, Pavel Kubalec, Alfons Nichtl, Tobias Oelschlaegel, Rainer Schlecht -
Publication number: 20210061924Abstract: 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.Type: ApplicationFiled: October 13, 2020Publication date: March 4, 2021Inventors: Hartmut Duefel, Alfred Engel, Frank Kroner, Thomas Meier, Sandra Rutz, Michael Schraeml, Gloria Tabares, Ulrike Kurtkaya, Boris Pinchuk, Christina Zimmermann
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RECOMBINANT IMMUNOGLOBULIN HEAVY CHAINS COMPRISING A SORTASE CONJUGATION LOOP AND CONJUGATES THEREOF
Publication number: 20210009660Abstract: 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.Type: ApplicationFiled: March 23, 2018Publication date: January 14, 2021Applicant: Roche Diagnostics Operations, Inc.Inventors: Alfred Engel, Pavel Kubalec, Alfons Nichtl, Tobias Oelschlaegel, Rainer Schlecht -
Publication number: 20190137523Abstract: The present invention relates to a method for measuring the level of VEGF-A in the presence of a VEGF-A antagonist, kits comprising means for detecting VEGF-A in the presence of a VEGF-A antagonist, compositions of matter comprising a first and a second antibody suitable for detecting the level of VEGF-A in the presence of a VEGF-A antagonist, as well as methods of detecting a complex comprising human VEGF-A and a non-human or chimeric protein.Type: ApplicationFiled: January 10, 2019Publication date: May 9, 2019Applicant: Hoffmann-La Roche Inc.Inventors: Alfred Engel, Johann Karl, Christina Rabe, Michael Schraeml, Monika Soukupova, Peter Stegmueller, Norbert Wild
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Publication number: 20180231570Abstract: 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.Type: ApplicationFiled: April 2, 2018Publication date: August 16, 2018Applicant: Roche Diagnostics Operations, Inc.Inventors: Andrea Horsch, Birgit Klapperich, Dirk Block, Alfred Engel, Johann Karl, Rosemarie Kientsch-Engel, Ekaterina Manuilova, Christina Rabe, Sandra Rutz, Monika Soukupova, Ursula-Henrike Wienhues-Thelen, Peter Kastner, Edelgard Anna Kaiser
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Patent number: 9809835Abstract: 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.Type: GrantFiled: November 24, 2015Date of Patent: November 7, 2017Assignee: Roche Diagnostics Operations, Inc.Inventors: Alfred Engel, Michael Greif, Christine Jung, Sebastian Malik, Rainer Mueller, Harald Sobek, Bernhard Suppmann, Marco Thomann
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Patent number: 9481902Abstract: 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 ?-galactoside-?-2,6-sialyltransferase I (hST6Gal-I) exhibited different specific sialyltransferase enzymatic activities. In one example, under conditions wherein the first variant ?89 hST6Gal-I catalyzed formation of bi-sialylated target molecules the second variant ?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.Type: GrantFiled: December 16, 2015Date of Patent: November 1, 2016Assignee: Roche Diagnostics Operations, Inc.Inventors: Tibor Czabany, Alfred Engel, Michael Greif, Christine Jung, Christiane Luley, Sebastian Malik, Rainer Mueller, Bernd Nidetzky, Doris Ribitsch, Katharina Schmoelzer, Helmut Schwab, Harald Sobek, Bernhard Suppmann, Marco Thomann, Sabine Zitzenbacher
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Publication number: 20160102333Abstract: 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 ?-galactoside-?-2,6-sialyltransferase I (hST6Gal-I) exhibited different specific sialyltransferase enzymatic activities. In one example, under conditions wherein the first variant ?89 hST6Gal-I catalyzed formation of bi-sialylated target molecules the second variant ?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.Type: ApplicationFiled: December 16, 2015Publication date: April 14, 2016Inventors: Tibor Czabany, Alfred Engel, Michael Greif, Christine Jung, Christiane Luley, Sebastian Malik, Rainer Mueller, Bernd Nidetzky, Doris Ribitsch, Katharina Schmoelzer, Helmut Schwab, Harald Sobek, Bernhard Suppmann, Marco Thomann, Sabine Zitzenbacher
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Publication number: 20160102298Abstract: The present disclosure is directed to glycosyltransferase variants having N-terminal truncation deletions. Contrary to previous findings certain truncations comprising the conserved amino acid motif (“QVWxKDS”) were found to be compatible with glycosyltransferase enzymatic activity, particularly in a human sialyltransferase (hST6Gal-I). 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 terminal acceptor groups of glycan moieties being part of glycoproteins such as immunoglobulins.Type: ApplicationFiled: December 16, 2015Publication date: April 14, 2016Inventors: Tibor Czabany, Alfred Engel, Michael Greif, Christine Jung, Christiane Luley, Sebastian Malik, Rainer Mueller, Bernd Nidetzky, Doris Ribitsch, Katharina Schmoelzer, Helmut Schwab, Harald Sobek, Bernhard Suppmann, Marco Thomann, Sabine Zitzenbacher
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Publication number: 20160076068Abstract: 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.Type: ApplicationFiled: November 24, 2015Publication date: March 17, 2016Inventors: Alfred Engel, Michael Greif, Christine Jung, Sebastian Malik, Rainer Mueller, Harald Sobek, Bernhard Suppmann, Marco Thomann
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Publication number: 20150355199Abstract: The present invention relates to an assay for specific detection of complement factor H-related protein 1 (CFHR1) in a sample from a subject, as well as kits and agents related thereto.Type: ApplicationFiled: August 26, 2015Publication date: December 10, 2015Inventors: Alfred Engel, Andreas Gallusser, Johann Karl, Peter Kastner, Wolfgang Obermeier, Monika Soukupova
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Patent number: 8551696Abstract: 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.Type: GrantFiled: June 3, 2010Date of Patent: October 8, 2013Assignee: Roche Diagnostics Operations, Inc.Inventors: Christian Scholz, Ralf Bollhagen, Alfred Engel, Elke Faatz, Peter Schaarschmidt, Barbara Upmeier, Toralf Zarnt
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Patent number: 8426167Abstract: The present invention relates to the cloning and expression of foreign protein or polypeptides in bacteria, such as Escherichia coli. 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.Type: GrantFiled: April 13, 2007Date of Patent: April 23, 2013Assignee: Roche Diagnostics Operations, Inc.Inventors: Christian Scholz, Herbert Andres, Elke Faatz, Alfred Engel, Urban Schmitt, Ariuna Bazarsuren, Peter Schaarschmidt
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Publication number: 20110059552Abstract: 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.Type: ApplicationFiled: June 3, 2010Publication date: March 10, 2011Inventors: CHRISTIAN SCHOLZ, RALF BOLLHAGEN, ALFRED ENGEL, ELKE FAATZ, PETER SCHAARSCHMIDT, BARBARA UPMEIER, TORALF ZARNT
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Patent number: 7604935Abstract: 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.Type: GrantFiled: October 23, 2006Date of Patent: October 20, 2009Assignee: Roche Diagnostics Operations, Inc.Inventors: Barbara Upmeier, Ralf Bollhagen, Alfred Engel, Elke Faatz, Peter Schaarschmidt, Christian Scholz, Toralf Zarnt
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Publication number: 20090028893Abstract: The present invention relates to the cloning and expression of foreign protein or polypeptides in bacteria, such as Escherichia coli. 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.Type: ApplicationFiled: April 13, 2007Publication date: January 29, 2009Inventors: Christian Scholz, Herbert Andres, Elke Faatz, Alfred Engel, Urban Schmitt, Ariuna Bazarsuren, Peter Schaarschmidt
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Patent number: 7244819Abstract: The present invention relates to the cloning and expression of foreign protein or polypeptides in bacteria, such as Escherichia coli. 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.Type: GrantFiled: June 24, 2002Date of Patent: July 17, 2007Assignee: Roche Diagnostics Operations, Inc.Inventors: Christian Scholz, Herbert Andres, Elke Faatz, Alfred Engel, Urban Schmitt, Ariuna Bazarsuren, Peter Schaarschmidt
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Patent number: 7244575Abstract: 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.Type: GrantFiled: March 24, 2005Date of Patent: July 17, 2007Assignee: Roche Diagnostics CorporationInventors: Christian Scholz, Herbert Andres, Elke Faatz, Alfred Engel, Dorothea Sizmann