Patents by Inventor Marco Thomann
Marco Thomann 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: 20240101643Abstract: Herein is reported a method for producing an antibody comprising the steps of forming an antibody-antibody light chain affinity ligand complex, wherein the antibody light chain affinity ligand is immobilized on a solid phase, by applying a solution comprising the antibody to the immobilized antibody light chain affinity ligand, and incubating the complex formed in the previous step with one or more enzymes to modify the glycosylation of the antibody, thereby producing the antibody.Type: ApplicationFiled: May 16, 2023Publication date: March 28, 2024Applicant: Hoffmann-La Roche Inc.Inventors: Roberto FALKENSTEIN, Heiko WALCH, Sebastian MALIK, Marco THOMANN, Matthias FREIHERR VON ROMAN, Ingrid GRUNERT, Roland DORN, Michael HINGAR
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Patent number: 11788108Abstract: The properties of certain glycosyltransferase variants having N-terminal truncation deletions or internal deletions are disclosed. Particularly, mutants that exhibit ?-2,6-sialyltransferase enzymatic activity in the presence of CMP-activated sialic acid as co-substrate, and in the presence of a suitable acceptor site, are disclosed. A fundamental finding documented in the present disclosure is that enzymes are not only capable of catalyzing transfer of a sialidyl moiety but they are also capable of catalyzing hydrolytic cleavage of terminally bound sialic acid from a glycan.Type: GrantFiled: June 23, 2021Date of Patent: October 17, 2023Assignee: Roche Diagnostics Operations, Inc.Inventors: Harald Sobek, Michael Greif, Marco Thomann, Sebastian Malik
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Patent number: 11767342Abstract: Herein is reported a method for the enzymatic production of an antibody with a modified glycosylation in the Fc-region comprising the steps of incubating the antibody light chain affinity ligand-bound monoclonal antibody with a glycosylation in the Fc-region with a first enzyme for a time sufficient and under conditions suitable to modify the glycosylation of the Fc-region, recovering the antibody from the antibody light chain affinity ligand, incubating the recovered antibody in solution with a second enzyme for a time sufficient and under conditions suitable to modify the glycosylation of the Fc-region to a defined form, separating the antibody with the modified glycosylation in the Fc-region from the second enzyme in a cation exchange chromatography, and thereby producing the antibody with a modified glycosylation in the Fc-region.Type: GrantFiled: June 20, 2019Date of Patent: September 26, 2023Assignee: Hoffmann-La Roche Inc.Inventors: Thomas Dams, Roberto Falkenstein, Sebastian Malik, Ingrid Grunert, Marco Thomann, Matthias Freiherr Von Roman, Heiko Walch
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Patent number: 11718653Abstract: The present invention relates to a method for the production of in vitro glycoengineered erythropoiesis stimulating protein, comprising the steps of providing sialic acid free erythropoiesis stimulating protein, treating the erythropoiesis stimulating protein with N-Acetyl-Glucosamin-transferase B3GNT2, treating the erythropoiesis stimulating protein with galactosyltransferase, and treating the erythropoiesis stimulating protein with sialyltransferase.Type: GrantFiled: December 16, 2020Date of Patent: August 8, 2023Assignee: Hoffmann-La Roche Inc.Inventors: Maria Maier, Marco Thomann
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Publication number: 20210340585Abstract: The present disclosure is directed to the properties of certain glycosyltransferase variants having N-terminal truncation deletions or internal deletions. Any of the mutants disclosed in here exhibit ?-2,6-sialyltransferase enzymatic activity in the presence of CMP-activated sialic acid as co-substrate, and in the presence of a suitable acceptor site. A fundamental finding documented in the present disclosure is that such enzyme are not only capable of catalyzing transfer of a sialidyl moiety but they are also capable of catalyzing hydrolytic cleavage of terminally bound sialic acid from a glycan.Type: ApplicationFiled: June 23, 2021Publication date: November 4, 2021Inventors: Harald SOBEK, Michael GREIF, Marco THOMANN, Sebastian MALIK
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Patent number: 11078511Abstract: The present disclosure is directed to the properties of certain glycosyltransferase variants having N-terminal truncation deletions or internal deletions. Any of the mutants disclosed in here exhibit alpha-2,6-sialyltransferase enzymatic activity in the presence of CMP-activated sialic acid as co-substrate, and in the presence of a suitable acceptor site. A fundamental finding documented in the present disclosure is that these enzymes are not only capable of catalyzing transfer of a sialidyl moiety but they are also capable of catalyzing hydrolytic cleavage of terminally bound sialic acid from a glycan.Type: GrantFiled: June 21, 2017Date of Patent: August 3, 2021Assignee: Roche Diagnostics Operations, Inc.Inventors: Harald Sobek, Michael Greif, Marco Thomann, Sebastian Malik
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Publication number: 20210101950Abstract: The present invention relates to a method for the production of in vitro glycoengineered erythropoiesis stimulating protein, comprising the steps of providing sialic acid free erythropoiesis stimulating protein, treating the erythropoiesis stimulating protein with N-Acetyl-Glucosamin-transferase B3GNT2, treating the erythropoiesis stimulating protein with galactosyltransferase, and treating the erythropoiesis stimulating protein with sialyltransferase.Type: ApplicationFiled: December 16, 2020Publication date: April 8, 2021Applicant: Hoffmann-La Roche Inc.Inventors: Maria MAIER, Marco THOMANN
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Publication number: 20200325245Abstract: The present invention relates to galactoengineered recombinant antibodies of IgG1 isotype, methods for the production of said antibodies and uses thereof.Type: ApplicationFiled: June 25, 2020Publication date: October 15, 2020Applicants: Genentech, Inc., Hoffmann-La Roche Inc.Inventors: Sebastian Malik, Dietmar Reusch, Alfred Schnüriger, Max L. Tejada, Marco Thomann
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Publication number: 20200165321Abstract: Herein is reported a method for the enzymatic preparation/production of an antibody with a modified glycosylation in the Fc-region comprises the steps of incubating an antibody that has a glycosylation in the Fc-region with one or more enzymes for a time sufficient and under conditions suitable to modify the glycosylation of the Fc-region to a defined form, separating in one or more chromatography steps the antibody with a modified glycosylation in the Fc-region from the one or more enzymes and thereby producing the antibody with a modified glycosylation in the Fc-region and one or more recycled enzymes, and repeating the incubating step with the one or more recycled enzymes at least once.Type: ApplicationFiled: June 20, 2019Publication date: May 28, 2020Applicant: Hoffmann-La Roche Inc.Inventors: Roberto Falkenstein, Sebastian Malik, Ingrid Grunert, Marco Thomann, Matthias Freiherr Von Roman, Heiko Walch
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Publication number: 20200165320Abstract: Herein is reported a method for producing an antibody comprising the steps of forming an antibody-antibody light chain affinity ligand complex, wherein the antibody light chain affinity ligand is immobilized on a solid phase, by applying a solution comprising the antibody to the immobilized antibody light chain affinity ligand, and incubating the complex formed in the previous step with one or more enzymes to modify the glycosylation of the antibody, thereby producing the antibody.Type: ApplicationFiled: June 20, 2019Publication date: May 28, 2020Applicant: Hoffmann-La Roche Inc.Inventors: Roberto FALKENSTEIN, Heiko WALCH, Sebastian MALIK, Marco THOMANN, Matthias FREIHERR VON ROMAN, Ingrid GRUNERT, Roland DORN, Michael HINGAR
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Publication number: 20200165296Abstract: Herein is reported a method for the enzymatic production of an antibody with a modified glycosylation in the Fc-region comprising the steps of incubating the antibody light chain affinity ligand-bound monoclonal antibody with a glycosylation in the Fc-region with a first enzyme for a time sufficient and under conditions suitable to modify the glycosylation of the Fc-region, recovering the antibody from the antibody light chain affinity ligand, incubating the recovered antibody in solution with a second enzyme for a time sufficient and under conditions suitable to modify the glycosylation of the Fc-region to a defined form, separating the antibody with the modified glycosylation in the Fc-region from the second enzyme in a cation exchange chromatography, and thereby producing the antibody with a modified glycosylation in the Fc-region.Type: ApplicationFiled: June 20, 2019Publication date: May 28, 2020Applicant: Hoffmann-La Roche Inc.Inventors: Thomas DAMS, Roberto FALKENSTEIN, Sebastian MALIK, Ingrid GRUNERT, Marco Thomann, Matthias FREIHERR VON ROMAN, Heiko Walch
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Publication number: 20200148735Abstract: The present invention relates to a method for the production of in vitro glycoengineered erythropoiesis stimulating protein, comprising the steps of providing sialic acid free erythropoiesis stimulating protein, treating the erythropoiesis stimulating protein with N-Acetyl-Glucosamin-transferase B3GNT2, treating the erythropoiesis stimulating protein with galactosyltransferase, and treating the erythropoiesis stimulating protein with sialyltransferase.Type: ApplicationFiled: September 18, 2019Publication date: May 14, 2020Applicant: Hoffmann-La Roche Inc.Inventors: Maria MAIER, Marco THOMANN
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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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Publication number: 20170298405Abstract: The present disclosure is directed to the properties of certain glycosyltransferase variants having N-terminal truncation deletions or internal deletions. Any of the mutants disclosed in here exhibit ?-2,6-sialyltransferase enzymatic activity in the presence of CMP-activated sialic acid as co-substrate, and in the presence of a suitable acceptor site. A fundamental finding documented in the present disclosure is that suchs enzyme are not only capable of catalyzing transfer of a sialidyl moiety but they are also capable of catalyzing hydrolytic cleavage of terminally bound sialic acid from a glycan.Type: ApplicationFiled: June 21, 2017Publication date: October 19, 2017Inventors: Harald Sobek, Michael Greif, Marco Thomann, Sebastian Malik
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Publication number: 20170253661Abstract: The present invention relates to galactoengineered recombinant antibodies of IgG1 isotype, methods for the production of said antibodies and uses thereof.Type: ApplicationFiled: March 10, 2017Publication date: September 7, 2017Applicants: Hoffmann-La Roche Inc., Genentech, Inc.Inventors: Sebastian Malik, Dietmar Reusch, Alfred Schnüriger, Max L Tejada, 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