Patents by Inventor Sophia Hober
Sophia Hober 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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Patent number: 11820802Abstract: The present invention is within the field of protein engineering and purification. The invention relates to a target-binding polypeptide mutant of an IgG binding polypeptide, such as Protein A, Protein G, Protein L or Protein M, comprising a metal binding motif. More closely the invention relates to an Fc binding ligand comprising an engineered protein based on the Protein A derived Z domain, to which a calcium binding EF-loop has been introduced.Type: GrantFiled: September 5, 2017Date of Patent: November 21, 2023Assignee: Cytiva BioProcess R&D ABInventors: Sophia Hober, Sara Kanje, Johan Nilvebrant
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Publication number: 20230250160Abstract: The present disclosure provides for a bispecific protein that enables simultaneous binding of both albumin and a desired target to an ADAPT (ABD Derived Affinity ProTeins) molecule. The present disclosure provides for an ADAPT molecule wherein the proposed binding surface of the desired target is located on helix 1 and helix 2 of the ADAPT molecule.Type: ApplicationFiled: April 29, 2021Publication date: August 10, 2023Inventors: Sophia Hober, Sarah Lindbo, Emma von Witting
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Publication number: 20230165982Abstract: There is provided an imaging agent for use in a method of visualization of HER2 expression in a human patient, said method comprising administering the imaging agent to the patient in a dose of 400-700 ?g and subsequently a scanning of the patient to visualize HER2 expression, wherein the imaging agent is a conjugate comprising a radionuclide and a HER2-binding protein (HBP) of a certain amino acid sequence. Further there is provided a unit dose comprising the imaging agent in an amount of 400-700 ?g.Type: ApplicationFiled: April 30, 2020Publication date: June 1, 2023Inventors: Sophia Hober, Javad Garousi, Vladimir Tolmachev, Bragina Olga, Sarah Lindbo, Vladimir Chernov
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Publication number: 20230107890Abstract: There is provided a therapeutic conjugate comprising a fusion protein and a cytotoxic radionuclide, which cytotoxic radionuclide is bound to the fusion protein. The fusion protein comprises a certain HER2-binding region (HBR), a certain albumin-binding region (ABR) and a spacer region.Type: ApplicationFiled: March 9, 2021Publication date: April 6, 2023Inventors: Sophia Hober, Emma von Witting, Javad Garousi, Vladimir Tolmachev
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Patent number: 11505576Abstract: The disclosure provides a population of polypeptide variants based on a common scaffold, each polypeptide in the population comprising the scaffold amino acid sequence Xsc1AELDXsc2Xsc3GVG AXXIKXIXsc4XA XXVEXVQXXK QXILAX. The disclosure also provides methods for selecting and identifying polypeptides from the population, as well as such polypeptides themselves.Type: GrantFiled: March 12, 2019Date of Patent: November 22, 2022Assignee: AFFIBODY ABInventors: Caroline Ekblad, Elin Gunneriusson, Sophia Hober, Sarah Lindbo
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Publication number: 20210162319Abstract: The present invention relates to an immunoglobulin-binding protein, wherein at least one asparagine residue has been mutated to an amino acid other than glutamine or aspartic acid, which mutation confers an increased chemical stability at pH-values of up to about 13-14 compared to the parental molecule. The protein can for example be derived from a protein capable of binding to other regions of the immunoglobulin molecule than the complementarity determining regions (CDR), such as protein A, and preferably the B-domain of Staphylococcal protein A. The invention also relates to a matrix for affinity separation, which comprises an immunoglobulin-binding protein as ligand coupled to a solid support, in which protein ligand at least one asparagine residue has been mutated to an amino acid other than glutamine.Type: ApplicationFiled: January 20, 2021Publication date: June 3, 2021Inventor: Sophia Hober
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Publication number: 20210047372Abstract: The disclosure provides a population of polypeptide variants based on a common scaffold, each polypeptide in the population comprising the scaffold amino acid sequence Xsc1AELDXsc2Xsc3GVG AXXIKXIXsc4XA XXVEXVQXXK QXILAX. The disclosure also provides methods for selecting and identifying polypeptides from the population, as well as such polypeptides themselves.Type: ApplicationFiled: March 12, 2019Publication date: February 18, 2021Inventors: Caroline Ekblad, Elin Gunneriusson, Sophia Hober, Sarah Lindbo
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Patent number: 10918971Abstract: The present invention relates to an immunoglobulin-binding protein, wherein at least one asparagine residue has been mutated to an amino acid other than glutamine or aspartic acid, which mutation confers an increased chemical stability at pH-values of up to about 13-14 compared to the parental molecule. The protein can for example be derived from a protein capable of binding to other regions of the immunoglobulin molecule than the complementarity determining regions (CDR), such as protein A, and preferably the B-domain of Staphylococcal protein A. The invention also relates to a matrix for affinity separation, which comprises an immunoglobulin-binding protein as ligand coupled to a solid support, in which protein ligand at least one asparagine residue has been mutated to an amino acid other than glutamine.Type: GrantFiled: December 2, 2016Date of Patent: February 16, 2021Assignee: Cytiva BioProcess R&D ABInventor: Sophia Hober
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Publication number: 20190218265Abstract: The present invention is within the field of protein engineering and purification. The invention relates to a target-binding polypeptide mutant of an IgG binding polypeptide, such as Protein A, Protein G, Protein L or Protein M, comprising a metal binding motif. More closely the invention relates to an Fc binding ligand comprising an engineered protein based on the Protein A derived Z domain, to which a calcium binding EF-loop has been introduced.Type: ApplicationFiled: September 5, 2017Publication date: July 18, 2019Inventors: Sophia Hober, Sara Kanje, Johan Nilvebrant
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Publication number: 20170080358Abstract: The present invention relates to an immunoglobulin-binding protein, wherein at least one asparagine residue has been mutated to an amino acid other than glutamine or aspartic acid, which mutation confers an increased chemical stability at pH-values of up to about 13-14 compared to the parental molecule. The protein can for example be derived from a protein capable of binding to other regions of the immunoglobulin molecule than the complementarity determining regions (CDR), such as protein A, and preferably the B-domain of Staphylococcal protein A. The invention also relates to a matrix for affinity separation, which comprises an immunoglobulin-binding protein as ligand coupled to a solid support, in which protein ligand at least one asparagine residue has been mutated to an amino acid other than glutamine.Type: ApplicationFiled: December 2, 2016Publication date: March 23, 2017Inventor: Sophia Hober
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Patent number: 9534023Abstract: The present invention relates to an immunoglobulin-binding protein, wherein at least one asparagine residue has been mutated to an amino acid other than glutamine or aspartic acid, which mutation confers an increased chemical stability at pH-values of up to about 13-14 compared to the parental molecule. The protein can for example be derived from a protein capable of binding to other regions of the immunoglobulin molecule than the complementarity determining regions (CDR), such as protein A, and preferably the B-domain of Staphylococcal protein A. The invention also relates to a matrix for affinity separation, which comprises an immunoglobulin-binding protein as ligand coupled to a solid support, in which protein ligand at least one asparagine residue has been mutated to an amino acid other than glutamine.Type: GrantFiled: September 4, 2015Date of Patent: January 3, 2017Assignee: GE Healthcare BioProcess R&D ABInventor: Sophia Hober
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Publication number: 20160152668Abstract: The present invention relates to an immunoglobulin-binding protein, wherein at least one asparagine residue has been mutated to an amino acid other than glutamine or aspartic acid, which mutation confers an increased chemical stability at pH-values of up to about 13-14 compared to the parental molecule. The protein can for example be derived from a protein capable of binding to other regions of the immunoglobulin molecule than the complementarity determining regions (CDR), such as protein A, and preferably the B-domain of Staphylococcal protein A. The invention also relates to a matrix for affinity separation, which comprises an immunoglobulin-binding protein as ligand coupled to a solid support, in which protein ligand at least one asparagine residue has been mutated to an amino acid other than glutamine.Type: ApplicationFiled: September 4, 2015Publication date: June 2, 2016Applicant: GE Healthcare Bio-Sciences ABInventor: Sophia Hober
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Patent number: 9296791Abstract: The present invention relates to an immunoglobulin-binding protein, wherein at least one asparagine residue has been mutated to an amino acid other than glutamine or aspartic acid, which mutation confers an increased chemical stability at pH-values of up to about 13-14 compared to the parental molecule. The protein can for example be derived from a protein capable of binding to other regions of the immunoglobulin molecule than the complementarity determining regions (CDR), such as protein A, and preferably the B-domain of Staphylococcal protein A. The invention also relates to a matrix for affinity separation, which comprises an immunoglobulin-binding protein as ligand coupled to a solid support, in which protein ligand at least one asparagine residue has been mutated to an amino acid other than glutamine.Type: GrantFiled: January 14, 2013Date of Patent: March 29, 2016Assignee: GE Healthcare Bio-Sciences ABInventors: Sophia Hober, Hans J. Johansson
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Patent number: 9156892Abstract: The present invention relates to an immunoglobulin-binding protein, wherein at least one asparagine residue has been mutated to an amino acid other than glutamine or aspartic acid, which mutation confers an increased chemical stability at pH-values of up to about 13-14 compared to the parental molecule. The protein can for example be derived from a protein capable of binding to other regions of the immunoglobulin molecule than the complementarity determining regions (CDR), such as protein A, and preferably the B-domain of Staphylococcal protein A. The invention also relates to a matrix for affinity separation, which comprises an immunoglobulin-binding protein as ligand coupled to a solid support, in which protein ligand at least one asparagine residue has been mutated to an amino acid other than glutamine.Type: GrantFiled: June 5, 2012Date of Patent: October 13, 2015Assignee: GE Healthcare Bio-Sciences Corp.Inventor: Sophia Hober
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Patent number: 8916689Abstract: The present invention relates to site-specific labeling of antibodies or fragments thereof with one or more reporter group(s) in a way that does not affect antigen binding. The method for labeling antibodies and/or fragments thereof, comprises the following steps a) providing an IgG binding protein, which comprises ?-helix structures, with a photoactivatable group and at least one label; b) forming a mixture of said IgG binding protein and the antibodies and/or fragments to be labeled; and c) UV illuminating said mixture for site-specific labeling of said antibodies and/or fragments thereof. The IgG binding protein is preferably the Z domain of Protein A.Type: GrantFiled: September 5, 2011Date of Patent: December 23, 2014Assignee: GE Health Bio-Sciences ABInventors: Sophia Hober, Amelie Eriksson Karlstrom, Anna Konrad
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Publication number: 20130184442Abstract: The present invention relates to site-specific labeling of antibodies or fragments thereof with one or more reporter group(s) in a way that does not affect antigen binding. The method for labeling antibodies and/or fragments thereof, comprises the following steps a) providing an IgG binding protein, which comprises ?-helix structures, with a photoactivatable group and at least one label; b) forming a mixture of said IgG binding protein and the antibodies and/or fragments to be labeled; and c) UV illuminating said mixture for site-specific labeling of said antibodies and/or fragments thereof. The IgG binding protein is preferably the Z domain of Protein A.Type: ApplicationFiled: September 5, 2011Publication date: July 18, 2013Applicant: GE HEALTHCARE BIO-SCIENCES ABInventors: Sophia Hober, Amelie Eriksson Karlstrom, Anna Konrad
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Patent number: 8354510Abstract: The present invention relates to an immunoglobulin-binding protein, wherein at least one asparagine residue has been mutated to an amino acid other than glutamine or aspartic acid, which mutation confers an increased chemical stability at pH-values of up to about 13-14 compared to the parental molecule. The protein can for example be derived from a protein capable of binding to other regions of the immunoglobulin molecule than the complementarity determining regions (CDR), such as protein A, and preferably the B-domain of Staphylococcal protein A. The invention also relates to a matrix for affinity separation, which comprises an immunoglobulin-binding protein as ligand coupled to a solid support, in which protein ligand at least one asparagine residue has been mutated to an amino acid other than glutamine.Type: GrantFiled: September 29, 2009Date of Patent: January 15, 2013Assignee: GE Healthcare Bio-Sciences ABInventors: Sophia Hober, Hans J. Johansson
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Publication number: 20120238724Abstract: The present invention relates to an immunoglobulin-binding protein, wherein at least one asparagine residue has been mutated to an amino acid other than glutamine or aspartic acid, which mutation confers an increased chemical stability at pH-values of up to about 13-14 compared to the parental molecule. The protein can for example be derived from a protein capable of binding to other regions of the immunoglobulin molecule than the complementarity determining regions (CDR), such as protein A, and preferably the B-domain of Staphylococcal protein A. The invention also relates to a matrix for affinity separation, which comprises an immunoglobulin-binding protein as ligand coupled to a solid support, in which protein ligand at least one asparagine residue has been mutated to an amino acid other than glutamine.Type: ApplicationFiled: June 5, 2012Publication date: September 20, 2012Applicant: GE HEALTHCARE BIO-SCIENCES ABInventor: SOPHIA HOBER
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Patent number: 8198404Abstract: The present invention relates to an immunoglobulin-binding protein, wherein at least one asparagine residue has been mutated to an amino acid other than glutamine or aspartic acid, which mutation confers an increased chemical stability at pH-values of up to about 13-14 compared to the parental molecule. The protein can for example be derived from a protein capable of binding to other regions of the immunoglobulin molecule than the complementarity determining regions (CDR), such as protein A, and preferably the B-domain of Staphylococcal protein A. The invention also relates to a matrix for affinity separation, which comprises an immunoglobulin-binding protein as ligand coupled to a solid support, in which protein ligand at least one asparagine residue has been mutated to an amino acid other than glutamine.Type: GrantFiled: October 8, 2010Date of Patent: June 12, 2012Assignee: GE Healthcare Bio-Sciences ABInventor: Sophia Hober
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Publication number: 20110112276Abstract: The present invention relates to an immunoglobulin-binding protein, wherein at least one asparagine residue has been mutated to an amino acid other than glutamine or aspartic acid, which mutation confers an increased chemical stability at pH-values of up to about 13-14 compared to the parental molecule. The protein can for example be derived from a protein capable of binding to other regions of the immunoglobulin molecule than the complementarity determining regions (CDR), such as protein A, and preferably the B-domain of Staphylococcal protein A. The invention also relates to a matrix for affinity separation, which comprises an immunoglobulin-binding protein as ligand coupled to a solid support, in which protein ligand at least one asparagine residue has been mutated to an amino acid other than glutamine.Type: ApplicationFiled: October 8, 2010Publication date: May 12, 2011Applicant: GE HEALTHCARE BIO-SCIENCES ABInventor: SOPHIA HOBER