Inventor
Hans-Peter Schwarz
Inventor
Vienna, AT
Overview
Patents· 117 as inventor
Public. Assignee & technology derived from the patent record. Each patent links to its LexDana page.
A61Kprimary
A61KPreparations for medical, dental or toiletry purposes22%
A61PSpecific therapeutic activity of chemical compounds or medicinal preparations22%
C07KPeptides16%
C12YEnzymes9%
C12NMicroorganisms or enzymes8%
G01NInvestigating or analysing materials by determining their chemical or physical properties5%
B01DSeparation4%
C12QMeasuring or testing processes involving enzymes, nucleic acids or microorganisms3%
Y02ATechnologies for adaptation to climate change2%
Y10STechnical subjects covered by former uspc cross-reference art collections [xracs] and digests2%
PatentTitleYear
10,875,906Removal of serine proteases by treatment with finely divided silicon dioxide202010,758,599Stabilized liquid and lyophilized ADAMTS13 formulations202010,738,107Methods to produce a human plasma-derived IgG preparation enriched in brain disease-related natural iggs202010,494,418IgG stimulated remyelination of peripheral nerves201910,238,720Stabilized liquid and lyophilized ADAMTS13 formulations201910,209,263Methods of measuring adamts 13 activity201910,208,106Removal of serine proteases by treatment with finely divided silicon dioxide201910,183,976Method for producing factor H from a plasma precipitation fraction201910,125,189Method to produce a highly concentrated immunoglobulin preparation for subcutaneous use20189,937,244Stabilized liquid and lyophilized ADAMTS13 formulations20189,896,501'Methods to produce a human plasma-derived IgG preparation enriched in brain disease-related natural IgGs'20189,855,331'Stabilization of immunoglobulins through aqueous formulation with histidine at weak acidic to neutral pH'20189,834,593IgG stimulated remyelination of peripheral nerves20179,783,792'Purification of butyrylcholinesterase using membrane adsorption'20179,782,477'Fraction I-IV-1 precipitation of immunoglobins from plasma'20179,708,391'Removal of serine proteases by treatment with finely divided silicon dioxide'20179,587,249'Models of thrombotic thrombocytopenic purpura and methods of use thereof'20179,572,778'Stabilized liquid and lyophilized ADAMTS13 formulations'20179,556,261'Methods to produce a human plasma-derived IgG preparation enriched in brain disease-related natural IgGs'20179,512,198'FVIII peptides for immune tolerance induction and immunodiagnostics'20169,512,172'Ethanol dependence of alpha1 antitrypsin C-terminal Lys truncation by basic carboxypeptidases'20169,488,651'Methods of measuring ADAMTS 13 activity'20169,468,675'Removal of serine proteases by treatment with finely divided silicon dioxide'20169,403,899'Method for reducing the thromboembolic potential of a plasma-derived immunoglobulin composition'20169,351,935'Stabilized liquid and lyophilized ADAMTS13 formulations'20169,309,506'Composition exhibiting a von Willebrand factor (vWF) protease activity comprising a polypeptide chain with the amino acid sequence AAGGILHLELLV'20169,175,068'Method to produce a highly concentrated immunoglobulin preparation for subcutaneous use'20159,109,044'Manufacture of factor H (FH) and FH-derivatives from plasma'20159,110,085'Methods of testing effectiveness of a treatment for thromobotic thrombocytopenic purpura by measuring ADAMTS13-mediated in vivo cleavage of von Willebrand factor'20159,084,743'Stable co-formulation of hyaluronidase and immunoglobulin, and methods of use thereof'20159,075,069'Measurement of autoantibodies at low conductivity with increased sensitivity'20158,993,734'Method to produce an immunoglobulin preparation with improved yield'20158,986,670'IgG stimulated remyelination of peripheral nerves'20158,986,607'Method for the validatable inactivation of pathogens in a biological fluid by irradiation'20158,969,524'FVIII peptides for immune tolerance induction and immunodiagnostics'20158,962,912'Transgenic non-human animals expressing human blood clotting factors and uses thereof'20158,940,877'Method to produce an immunoglobulin preparation with improved yield'20158,921,520'Removal of serine proteases by treatment with finely divided silicon dioxide'20148,889,838'Removal of serine proteases by treatment with finely divided silicon dioxide'20148,852,874'Anti-amyloid β activity of intravenous immunoglobulin (IVIG) in vitro'20148,828,676'Methods for differentiating plasma-derived protein from recombinant protein in a sample'20148,822,656'Manufacture of factor H (FH) and FH-derivatives from plasma'20148,795,658'Stabilization of immunoglobulins through aqueous formulation with histidine at weak acidic to neutral pH'20148,796,430'Method to produce an immunoglobulin preparation with improved yield'20148,785,139'Modification-dependent activity assays'20148,772,462'Removal of serine proteases by treatment with finely divided silicon dioxide'20148,772,240'Ethanol dependence of alpha1 antitrypsin C-terminal lys truncation by basic carboxypeptidases'20148,735,086'Kit for measuring the thrombin generation in a sample of a patient\'s blood or plasma'20148,703,426'Composition exhibiting a von Willebrand Factor (vWF) protease activity with the amino acid sequence AAGGILHLELLV'20148,703,429'Composition exhibiting a von Willebrand Factor (vWF) protease activity comprising a polypeptide chain with the amino acid sequence AAGGILHLELLV'20148,652,793'Solid phase-bound elastase-binding assay for the measurement of alpha1-antitrypsin activity'20148,623,352'Stabilized liquid and lyophilized ADAMTS13 formulations'20148,623,612'Method for testing treatment of ADAMTS13 deficiency'20148,603,830'Method for the determination of polysorbate 80'20138,546,548'Method to produce a highly concentrated immunoglobulin preparation for subcutaneous use'20138,546,332'Factor VIII polypeptide having factor VIII:C activity'20138,415,114'Methods of measuring ADAMTS13-mediated in vivo cleavage of von Willebrand factor and uses thereof'20138,377,375'Methods for the inactivation of microorganisms in biological fluids, flow through reactors and methods of controlling the light sum dose to effectively inactivate microorganisms in batch reactors'20138,343,748'Preparative purification process for human furin'20138,304,524'Manufacture of factor H (FH) and FH-derivatives from plasma'20128,216,793'Detection of antibody that binds to water soluble polymer-modified polypeptides'20128,173,597'Modified recombinant factor VIII and von Willebrand factor and methods of use'20128,114,633'Methods for differentiating plasma-derived protein from recombinant protein in a sample'20127,993,580'Methods for the inactivation of microorganisms in biological fluids, flow through reactors and methods of controlling the light sum dose to effectively inactivate microorganisms in batch reactors'20117,968,293'IVIG modulation of chemokines for treatment of multiple sclerosis, alzheimer\'s disease, and parkinson\'s disease'20117,910,094'Composition exhibiting a von willebrand factor (vWF) protease activity comprising a polypeptide chain with the amino acid sequence AAGGILHLELLV'20117,807,435'Method for the purification of alpha-1 proteinase inhibitor (a1PI)'20107,557,188'Methods of treating blood coagulation disorders using a pharmaceutical preparation comprising vWF propeptide'20097,544,660'Factor VIII polypeptide having factor VIII:C activity'20097,501,117'Composition exhibiting a von Willebrand factor (vWF) protease activity comprising a polypeptide chain with the amino acid sequence AAGGILHLELLV'20097,279,161'Factor IX/factor IXa activating antibodies and antibody derivatives'20077,033,590'Factor IX/factor IXa activating antibodies and antibody derivatives'20067,005,502'Pharmaceutical preparation comprising vWF propeptide'20066,926,894'Composition exhibiting a von willebrand factor (vWF) protease activity comprising a polypeptide chain with the amino acid sequence AAGGILHLELLV'20056,919,311'Factor VII polypeptide having factor VII:C activity'20056,777,390'Stable blood coagulation inhibitor-free factor vii preparation and method for preparing same'20046,670,116'Methods for the detection, quantification and differentiation of infectious versus non-infectious pathogens in a sample'20036,414,125'Method of chromatographically purifying or fractionating, respectively, von Willebrand factor from a VWF-containing starting material'20026,403,556'Pharmaceutical preparation containing protein C and a thrombolytically active substance'20026,395,880'Method for purification of antithrombin III using an anion exchanger'20026,358,534'Immunotolerant prothrombin complex preparation'20026,270,672'Devices and methods for removing pathogens from biological fluids'20016,224,862'Pharmaceutical preparation for treating blood coagulation disorders'20016,165,974'Pharmaceutical preparation for treating blood coagulation disorders'20006,103,693'Method for isolation of highly pure von willebrand factor'20006,099,837'Pharmaceutical preparation for treating blood coagulation disorders'20006,068,838'Purified multimerase'20006,039,945'Pharmaceutical preparation for treating blood coagulation disorders'20006,017,891'Stable preparation for the treatment of blood coagulation disorders'20006,013,620'Pharmaceutical composition for the treatment of blood coagulation diseases, methods for the production thereof and its use'20006,005,077'Use of von willebrand factor and pharmaceutical formulation'19995,891,843'Pharmaceutical composition for the treatment of blood coagulation diseases, methods for the production thereof and its use'19995,880,265'Method for isolation of highly pure von willebrand factor'19995,877,152'Method for isolation of highly pure von Willebrand Factor'19995,866,122'Pharmaceutical preparation for treating blood coagulation disorders'19995,863,896'Evaluation of substances for altering and for increasing APC response'19995,854,403'Method for isolation of highly pure von Willebrand Factor'19985,830,467'Pharmaceutical preparation containing protein C and a thrombolytically active substance'19985,827,818'Agent for subcutaneous administration of protein C'19985,804,181'Pharmaceutical preparation for the prevention and treatment of blood coagulation disorders'19985,804,159'Antiplasma animal model'19985,776,452'Thrombosis agent'19985,698,677'Stable preparation for the treatment of blood coagulation disorders'19975,675,058'Bioassay for thrombogenesis and rabbit model'19975,643,739'Assay for determining sensitivity to activated protein C'19975,614,493'Use of human protein C for prevention and treatment of depositions of thrombocytes'19975,597,800'Treatment with lys-plasminogen of reperfusion injury and brain edema caused by ischemia'19975,593,968'Virus-inactivated factor Xa preparation'19975,580,962'Parenterally administrable drug having thrombolytic activity and containing protein C'19965,571,786'Use of protein C or the activation peptide of protein C for preparing a pharmaceutical preparation'19965,549,893'Use of protein C in the treatment of purpura fulminans'19965,520,912'Prevention and treatment of ischemic events and reperfusion injury resulting therefrom using lys-plasminogen'19965,478,558'Method of dissolving venous Thrombi using drug containing activated Protein C'19955,330,907'Method of preparing activated protein C'19945,304,383'Pharmaceutical preparation based on Lys-plasminogen'19945,254,532'Preparation for treating and preventing thromboses and thromboembolic complications, use of such a preparation and a method of producing the same'19935,143,901'Preparation for treating and preventing thromboses and thromboembolic complications, use of such a preparation and a method of producing the same'1992Career & activity timeline
Assembled from patent assignee/location history and declaration credentials.
1992–2020Based in Vienna, AT· patent location history
2010–2016Patents assigned to BAXTER HEALTHCARE SA (38)· patent assignee history
2010–2016Patents assigned to BAXTER INT (38)· patent assignee history
2012–2017Patents assigned to SCHWARZ HANS-PETER (30)· patent assignee history
2015–2020Patents assigned to BAXALTA INC (29)· patent assignee history
2015–2020Patents assigned to Baxalta GmbH (29)· patent assignee history
Inventor activity
Assignee and location history derived from the patent record.
Assignees
| Assignee | Patents | Span |
|---|---|---|
| BAXTER HEALTHCARE SA | 38 | 2010–2016 |
| BAXTER INT | 38 | 2010–2016 |
| SCHWARZ HANS-PETERself | 30 | 2012–2017 |
| BAXALTA INC | 29 | 2015–2020 |
| Baxalta GmbH | 29 | 2015–2020 |
Locations
| Location | Patents | Span |
|---|---|---|
| Vienna, AT | 117 | 1992–2020 |