Class / Patent application number | Description | Number of patent applications / Date published |
435226000 | Derived from animal tissue (e.g., rennin, etc.) | 45 |
20090053788 | MUSCULAR DYSTROPHY DRUG - The object of the present invention is to provide a drug having therapeutic effect on muscular dystrophy without lowering renal function. The therapeutic drug for muscular dystrophy of the present invention comprises a caldecrin or a caldecrin gene. | 02-26-2009 |
20100021987 | Compositions, Methods, and Kits for Enhancing Protein Expression - The inventive subject matter relates to novel compositions, methods, and kits for enhancing the expression, solubility, and isolation of heterologous proteins. Further, the inventive subject matter relates to methods for generating proteins with novel N-terminal amino acids, unlike wild-type proteins which always are translated from mRNA with methionine at the N-terminus. | 01-28-2010 |
20100144013 | OVER EXPRESSION OF FOLDASES AND CHAPERONES IMPROVES PROTEIN PRODUCTION - The present teachings provide methods for increasing protein secretion, e.g., chymosin in filamentous fungi by co-expressing certain chaperone(s) and/or foldase(s). The present teachings also provide filamentous fungi containing certain chaperone(s) and/or foldase(s) and a protein of interest for increased secretion. | 06-10-2010 |
20110263000 | A THROMBIN-LIKE ENZYME OF AGKISTRODON ACUTUS - A thrombin-like enzyme isolated from Agkistrodon acutus venom, comprising an alpha subunit having the sequence of SEQ ID No. 1 and a beta subunit having the sequence of SEQ ID No. 2, which are linked by seven disulfide bonds, is provided. The hemocoagulase of | 10-27-2011 |
20110287518 | Polypeptide Purification - The invention relates to the purification of different gamma carboxylated forms of a polypeptide using ion exchange chromatography. In particular, the invention provides a method for purifying a polypeptide having a desired content of gamma-carboxyglutamic acid from a sample comprising mixture of species of said polypeptide having different contents of gamma-carboxyglutamic acid, said method comprising the steps of: (a) loading said sample onto an anion exchange chromatography material; (b) eluting said polypeptide using a solution at a pH of less than pH 9.0 comprising at least one salt selected from ammonium acetate, ammonium chloride and sodium acetate; and (c) selecting a fraction obtained from said elution wherein the polypeptides in the fraction have the desired content of gamma-carboxyglutamic acids. | 11-24-2011 |
20110312059 | TAU PROTEASE COMPOSITIONS AND METHODS - Tau protein has a causative role in Alzheimer's disease and multiple other neurodegenerative disorders exhibiting tau histopathology collectively termed tauopathies. The primary function of tau protein is to facilitate assembly and maintenance of microtubules in neuronal axons. In the disease process tau protein becomes modified, loses its affinity to microtubules and accumulates in the cell body where it forms aggregates. The large neurofibrillary tangles formed from tau protein assembled into filaments were thought to be the pathological structure of tau. However, more recent work indicates that smaller, soluble oligomeric forms of tau are best associated with neuron loss and memory impairment. A novel and unexpected protease activity has been discovered to be associated with tau in oligomeric but not monomeric structures. Methods have been developed to form and purify tau protease and to assay its activity. Tau protease activity constitutes a totally novel mechanism for tau-mediated neurodegenerative disease by causing tau loss of function, as it cleaves itself, and gain of toxic function as it can cleave other proteins and facilitate cell death through apoptotic and/or senescence pathways. Tau protease presents a novel and unique target for the development of therapeutics that may be achieved by several strategies including by inhibiting the tau oligomer enzymatic activity. | 12-22-2011 |
20120034674 | METHOD OF PRODUCING RECOMBINANT ADAMTS13 IN CELL CULTURE - Among other aspects, the present invention relates to cell culture conditions for producing high molecular weight vWF, in particular, highly multimericWF with a high specific activity and ADAMTS13 with a high specific activity. The cell culture conditions of the present invention can include, for example, a cell culture medium with an increased copper concentration and/or cell culture supernatant with a low ammonium (NH | 02-09-2012 |
20120231523 | RECOMBINANT FACTOR X WITH NO GLYCOSYLATION AND METHOD FOR PREPARING THE SAME - A Factor X (hereinafter referred to as “FX”) with a high activity is provided. The present invention relates to a method for efficiently preparing a recombinant, two-chain FX which comprises intervening glycosylation at such an amino acid sequence that is essential for glycosylation in FX to thereby allow for expression of a recombinant FX with no glycosylation, and the recombinant FX with no glycosylation obtained by said method. | 09-13-2012 |
20120252097 | Therapeutic Agents Comprising Pro-Apoptotic Proteins - The present invention relates to targeted killing of a cell utilizing a chimeric polypeptide comprising a cell-specific targeting moiety and a signal transduction pathway factor. In a preferred embodiment, the signal transduction pathway factor is an apoptosis-inducing factor, such as granzyme B, granzyme A, or Bax. | 10-04-2012 |
20120270299 | TISSUE PLASMINOGEN ACTIVATOR VARIANT USES - A method is disclosed for using tenecteplase to restore function in dysfunctional hemodialysis catheters, which have a blood flow rate of less than 300 mL/minute. Kits are also provided with instructions to direct the user to administer tenecteplase in a total dose of about 3 to 4 mg locally into all catheter lumens and allow the tenecteplase to dwell in the catheter for from about one hour to about 72 hours. | 10-25-2012 |
20120270300 | PRODUCTION OF RECOMBINANT FACTOR IX IN A HUMAN HEPATOCYTE CELL LINE - The invention relates to a recombinant human factor IX (FIX) characterized in that said factor is obtained by a preparation method comprising, or even consisting of, the steps which consist in causing the genetic material encoding the FIX to be expressed in vitro in a human hepatocyte cell line Huh7, recovering the cellular supernatant in which the FIX was secreted and, optionally, purifying the synthesized FIX. | 10-25-2012 |
20130071906 | CELL CULTURE MEDIUM FOR ADAMTS PROTEIN EXPRESSION - The present invention provides culture mediums that are useful for the expression of ADAMTS proteins, such as ADAMTS13. Methods for the expression and purification of ADAMTS proteins are also provided. In some embodiments, the mediums and methods of the invention are useful for the expression of ADAMTS proteins having high specific activities. Also provided are ADAMTS, e.g., ADAMTS13, protein compositions with high specific activities, which are expressed and purified according to the methods provided herein. | 03-21-2013 |
20130095555 | Hyperglycosylated Human Coagulation Factor IX - The invention relates to hyperglycosylated human coagulation factor IX polypeptides, to processes for preparing said polypeptides, to pharmaceutical compositions comprising said polypeptides and to the use of the compounds for the treatment of diseases alleviated by human coagulation factor IX, in particular, but not exclusively hemophilia. | 04-18-2013 |
20130143302 | METHOD FOR PURIFYING GLA-DOMAIN COAGULATION PROTEINS - A method for purifying GLA-domain coagulation proteins, includes the following steps: a) bringing a sample containing one or more GLA-domain coagulation proteins into contact with an affinity substrate on which nucleic aptamers which bind specifically to the GLA-domain coagulation proteins are immobilized, in order to form complexes between (i) the nucleic aptamers and (ii) the GLA-domain coagulation protein(s), b) releasing the GLA-domain coagulation protein(s) from the complexes formed in step a), and c) recovering the GLA-domain coagulation protein(s) in a purified form. | 06-06-2013 |
20130260439 | Method for the Production of Proteins - The present invention relates to a process for the purification of a protease. | 10-03-2013 |
20130273634 | METHOD FOR MASS PRODUCTION OF FACTOR VII/VIIA - A method for the mass production of human coagulation factor VII. The method includes a) providing an expression vector carrying i) a dihydrofolate reductase promoter devoid of one or more CCGCC repeat sequences from the GC-rich region thereof and a dihydrofolate reductase (DHFR) gene operably linked thereto and ii) a cytomegalovirus (CMV) promoter and a human coagulation factor VII gene operably linked thereto; b) obtaining a transformed a host cell line containing the expression vector; and c) culturing the transfected host cell in the presence of a dihydrofolate reductase inhibitor to select cells which express human coagulation factor VII with high efficiency; and d) adding sodium butyrate to the selected host cells. | 10-17-2013 |
20130330808 | NOVEL PROCESS FOR THE PURIFICATION OF TISSUE PLASMINOGEN ACTIVATOR - The present invention provides process of purification of tissue plasminogen activator (tPA) from a crude mixture or a partially purified mixture containing tPA protein and impurities by using hydrophobic interaction column chromatography, optionally in combination with ion exchange column chromatography. | 12-12-2013 |
20140087443 | OVER EXPRESSION OF FOLDASES AND CHAPERONES IMPROVES PROTEIN PRODUCTION - The present teachings provide methods for increasing protein secretion, e.g., chymosin in filamentous fungi by co-expressing certain chaperone(s) and/or foldase(s). The present teachings also provide filamentous fungi containing certain chaperone(s) and/or foldase(s) and a protein of interest for increased secretion. | 03-27-2014 |
20140186923 | COMPOUNDS AND METHODS FOR PURIFICATION OF SERINE PROTEASES - Disclosed herein are compounds, compositions, methods and kits for purifying a serine protease and serine proteases purified with the compounds, compositions and methods. | 07-03-2014 |
20140193880 | MODIFIED FACTOR VIII AND FACTOR IX GENES AND VECTORS FOR GENE THERAPY - The present invention relates to a modified and optimized Factor VIII or Factor IX nucleic acid for inclusion in a chimeric virus vector. Use of such vector can be used for treatment of hemophilia. | 07-10-2014 |
20140193881 | NOVEL ADAMTS-13 MUTANT - An enhanced disintegrin-like domain, and metalloprotease, with an isolated human thrombospondin type 1 motif, member 13 (ADAMTS-13) that includes substitutions at one or more positions in the isolated human ADAMTS-13. | 07-10-2014 |
20140212949 | METHOD FOR PREPARING MICROVESICULAR ADAM15 - The present invention relates to a method for preparing microvesicular ADAM15, comprising: (a) a step of activating protein kinase C (PKC) of separated mammalian cells; and (b) a step of separating microvesicle-containing ADAM15 from the mammalian cells. According to the present invention, a method for preparing microvesicular ADAM15 from mammalian cells is provided, and a novel cell regulation mechanism mediated by ADAM proteins is provided by the study of the function of the microvesicular ADAM15. Further, the present invention may provide a novel anti-cancer drug using microvesicular ADAM15, which inhibits adhesion, proliferation and migration of tumor cells. | 07-31-2014 |
20140248686 | THERAPEUTIC POLYPEPTIDES WITH INCREASED IN VIVO RECOVERY - The present invention relates to the field of modified therapeutic polypeptides with increased in vivo recovery compared to their non-modified parent polypeptide. For example, the invention relates to fusions of therapeutic polypeptides with recovery enhancing polypeptides connected directly or optionally connected by a linker peptide. | 09-04-2014 |
20140302591 | PROTEIN PURIFICATION BY ANION EXCHANGE CHROMATOGRAPHY - The present invention relates to a two-step method for the purification of divalent cation binding proteins with high yield and high purity on anion exchange resin materials, to divalent cation binding proteins obtainable by said method, and to a kit comprising means for carrying out said method. | 10-09-2014 |
20140302592 | PROTEIN PURIFICATION BY ANION EXCHANGE CHROMATOGRAPHY - The present invention relates to a two-step method for the purification of divalent cation binding proteins with high yield and high purity on anion exchange resin materials, to divalent cation binding proteins obtainable by said method, and to a kit comprising means for carrying out said method. | 10-09-2014 |
20140329294 | CELL CULTURE MEDIUM FOR ADAMTS PROTEIN EXPRESSION - The present invention provides culture mediums that are useful for the expression of ADAMTS proteins, such as ADAMTS13. Methods for the expression and purification of ADAMTS proteins are also provided. In some embodiments, the mediums and methods of the invention are useful for the expression of ADAMTS proteins having high specific activities. Also provided are ADAMTS, e.g., ADAMTS13, protein compositions with high specific activities, which are expressed and purified according to the methods provided herein. | 11-06-2014 |
20150050716 | NOVEL ADAMTS-13 MUTANT - An enhanced disintegrin-like domain, and metalloprotease, with an isolated human thrombospondin type 1 motif, member 13 (ADAMTS-13) that includes substitutions at one or more positions in the isolated human ADAMTS-13. | 02-19-2015 |
20150104849 | METHODS OF PURIFYING RECOMBINANT ADAMTS13 AND OTHER PROTEINS AND COMPOSITIONS THEREOF - Provided herein are methods for purifying recombinant A Disintegrin-like and Metallopeptidase with Thrombospondin Type 1 Motif 13 (ADAMTS13) protein from a sample. The method comprises enriching for ADAMTS13 protein by chromatographically contacting the sample with hydroxyapatite under conditions that allow ADAMTS13 protein to appear in the eluate or supernatant from the hydroxylapatite. The methods may further comprise tandem chromatography with a mixed mode cation exchange/hydrophobic interaction resin that binds ADAMTS13 protein. Additional optional steps involve ultrafiltration/diafiltration, anion exchange chromatography, cation exchange chromatography, and viral inactivation. Also provided herein are methods for inactivating virus contaminants in protein samples, where the protein is immobilized on a support. Also provided herein are compositions of ADAMTS13 prepared according to said methods. | 04-16-2015 |
20150132826 | CHIMERIC TRUNCATED TISSUE PLASMINOGEN ACTIVATOR (t-PA) RESIATANT TO PLASMINOGEN ACTIVATOR INHIBITOR-1 AND IMPROVED BIOCHEMICAL PROPERTIES - The present invention discloses a thrombolytic therapy for acute myocardial infarction by t-PA. A chimeric truncated form of t-PA is designed and expressed in | 05-14-2015 |
20150299685 | Virus Filtration of Liquid Factor VII Compositions - The present invention relates to a novel method for improving the viral safety of liquid Factor VII compositions, in particular those comprising active Factor VII polypeptides (a Factor VIIa polypeptide). | 10-22-2015 |
20150329848 | CELL CULTURE MEDIUM FOR ADAMTS PROTEIN EXPRESSION - The present invention provides culture mediums that are useful for the expression of ADAMTS proteins, such as ADAMTS13. Methods for the expression and purification of ADAMTS proteins are also provided. In some embodiments, the mediums and methods of the invention are useful for the expression of ADAMTS proteins having high specific activities. Also provided are ADAMTS, e.g., ADAMTS13, protein compositions with high specific activities, which are expressed and purified according to the methods provided herein. | 11-19-2015 |
20150337285 | COMPOUNDS AND METHODS FOR PURIFICATION OF SERINE PROTEASES - Disclosed herein are compounds, compositions, methods and kits for purifying a serine protease and serine proteases purified with the compounds, compositions and methods. | 11-26-2015 |
20150337286 | CATHEPSIN L INHIBITORS AND PROBES COMPRISING VINYL SULFONATE MOIETY AND METHODS OF USING SAME - Human cathepsin L inhibitors and probes containing a vinyl sulfonate ester moiety are described. The inhibitors are highly potent (low nM affinity), selective, and cell permeable, and can inhibit ultra-low concentration of active cathepsin L. The developed probes are highly sensitive and can detect an ultra-low amount of probe-labeled active cathespin L. | 11-26-2015 |
20150344862 | COAGULATION FACTOR IX COMPOSITIONS AND METHODS OF MAKING AND USING SAME - The present invention relates to compositions comprising factor IX coagulation factors linked to extended recombinant polypeptide (XTEN), isolated nucleic acids encoding the compositions and vectors and host cells containing the same, and methods of making and using such compositions in treatment of coagulation factor-related diseases, disorders, and conditions. | 12-03-2015 |
20160002618 | IMPROVED PURIFICATION OF PROTEINS VIA A DEGLYCOSYLATION STEP - A method for purifying a polypeptide of interest by use of a deglycosylation step. | 01-07-2016 |
20160024488 | METHOD FOR PREPARING A CONCENTRATE OF FACTOR XI - The invention concerns a concentrate of human Factor XI having high specific activity prepared using a method comprising a filtration-adsorption step and a chromatography step on cation exchange resin. The concentrate obtained is fully adapted for therapeutic use as substitution therapy in cases of Factor XI deficiency. | 01-28-2016 |
20160039869 | PURIFICATION METHOD FOR VITAMIN K DEPENDENT PROTEINS BY ANION EXCHANGE CHROMATOGRAPHY - The present invention relates to a method for the purification of Vitamin K dependent proteins with high yield and high purity, particularly enriched in active protein, on anion exchange resin materials, to Vitamin K dependent proteins obtainable by said method, and to a kit comprising means for carrying out said method. | 02-11-2016 |
20160046922 | FACTOR X ACTIVATION - Methods and systems for activating Factor X are disclosed. | 02-18-2016 |
20160060612 | Method of Isolating and Purifying Fusion Protein Comprising Factor VII - The present invention provides a method of isolating and purifying a fusion protein comprising factor VII, and more specifically relates to a method of isolating and purifying a fusion protein comprising factor VII and transferrin, to a high degree of purity. Because the present invention provides a method whereby a recombinant fusion protein comprising factor VII can be isolated and purified to a high degree of purity, the invention is useful in producing a pharmaceutical preparation comprising factor VII that can be used in situations in which copious bleeding occurs such as surgery. | 03-03-2016 |
20160130573 | Method of Controlling a Polypeptide Modification Reaction - The invention relates to a method of controlling a polypeptide modification reaction, in particular but not exclusively, a method of controlling the activation of human factor VII (FVII) to produce human factor VII(a) (FVII(a)). The invention also relates to polypeptides obtainable by the polypeptide modification reaction and to pharmaceutical compositions comprising said polypeptides. | 05-12-2016 |
20160138001 | METHOD FOR PURIFYING ACTIVE GLA-DOMAIN COAGULATION PROTEINS - The invention relates to a method for purifying biologically active GLA-domain coagulation proteins, comprising the following steps: a) bringing a sample that contains one or more GLA-domain coagulation proteins and may contain biologically inactive molecules of GLA-domain protein(s), into contact with an affinity support on which nucleic aptamers that bind specifically to at least one biologically active GLA-domain coagulation protein are immobilized, in order to form complexes between (i) said nucleic aptamers and (ii) said GLA-domain coagulation protein(s), b) releasing the GLA-domain coagulation protein(s) from the complexes formed in step a), and c) recovering said biologically active GLA-domain coagulation protein(s) in a purified form. | 05-19-2016 |
20160145597 | HEPARIN AFFINITY TAG AND APPLICATIONS THEREOF - In one aspect, affinity tags for recombinant protein purification are described herein which, in some embodiments, can mitigate or overcome disadvantages of prior affinity tag systems. In some embodiments, for example, affinity tags described herein permit efficient elution of desired recombinant proteins with simplified solution systems, such as alkali metal salt solutions. An affinity tag described herein comprises an amino acid sequence including a repeating amino acid unit of BXXXBXX, wherein B is an amino acid selected from the group consisting of histidine, lysine and arginine and X is an amino acid selected from the group consisting of amino acids other than histidine, lysine and arginine. | 05-26-2016 |
20160160203 | COORDINATED COEXPRESSION OF THROMBIN - The present invention provides methods of producing thrombin using coordinated coexpression systems, and particularly inducible coexpression systems, capable of controlled induction of expression of each gene product required for the production of thrombin, and the thrombin produced by this method. | 06-09-2016 |
20160185816 | METHOD OF PURIFYING POLYPEPTIDES - The present invention relates to improved processes for purifying polypeptides of interest by increasing the amount of a polypeptide of interest bound to an ion-exchange matrix relative to the amount of one or more impurities bound to the ion-exchange matrix. This effect is achieved by adding a chemical compound in the process which by also binding to the ion-exchange matrix due to a charge that is opposite to the charge of the ion-exchange matrix, reduces the binding of impurities more than the binding of the polypeptide of interest. | 06-30-2016 |
20160194622 | FUSION PROTEIN HAVINGH FACTOR VII ACTIVITY | 07-07-2016 |