Class / Patent application number | Description | Number of patent applications / Date published |
530381000 | Blood coagulation factors and fibrin, e.g., thromboplastin, etc. | 72 |
20080281080 | Purification of Recombinant Human Factor XIII - The present invention provides improved methods for the purification of factor XIII. In particular, the methods provide compositions containing 5% or less contaminating proteins. In particular embodiments of the present invention the methods provide purified factor XIII compositions comprising less than 1% activated factor XIII, less than 2% protein aggregates, and/or less than 5% charge isomers of factor XIII. The methods do not require the use a precipitation or crystallization step common to prior methods of isolating factor XIII. Instead, the method uses immobilized metal affinity chromatography to remove various contaminants common to recombinant expression of factor XIII. Further, a combination of various chromatography methods including ion exchange chromatography, hydrophobic affinity chromatography, and immobilized metal affinity chromatography comprise a simple and less expensive method to produce a pharmaceutical grade factor XIII product at high yield. | 11-13-2008 |
20090069543 | Factor IXa for the treatment of bleeding disorders - The invention provides a method of treating bleeding disorders in a subject by administration of a preparation enriched for Factor IXa. The Factor IXa can be produced by proteolytically activating recombinantly-produced Factor IX. The invention also provides an improved method for producing Factor IXa from a plasma fraction, which method results in a Factor IXa product containing little or no prekallikrein activity, thus reducing the incidence of undesired side effects in a subject. | 03-12-2009 |
20090093616 | IN-SOLUTION ACTIVATION OF FACTOR VII - The present invention is directed to a method for activation of Factor VII to FVIIa in solution. | 04-09-2009 |
20090281283 | METHOD FOR EXTRACTING A PROTEIN FROM MILK - The invention relates to a method for extracting a protein from milk, having at least one hydrophobic pocket and a negative charge to the natural pH of milk, that comprises the following steps: a) skimming and delipidation of the milk; b) passing the delipidated and skimmed fraction containing said protein on a chromatographic substrate on which is grafted a ligand having both a hydrophobic characteristic and a ionic characteristic in pH conditions enabling the protein to be retained on said substrate, the pH being higher than 4.6; c) elution of the protein; d) purification of the eluded fraction by removing the milk proteins from said eluded fraction; and e) recovering said protein. | 11-12-2009 |
20100022755 | PLATELET AGGREGATION INDUCING SUBSTANCE - A platelet aggregation inducing substance containing as an active ingredient a polypeptide having a peptide fragment represented by formula (1) (component A): | 01-28-2010 |
20100041872 | GLYCEROL LINKED PEGYLATED SUGARS AND GLYCOPEPTIDES - The present invention provides conjugates between peptides and PEG moieties through glycerol linkers. | 02-18-2010 |
20100113743 | GLYCOPEGYLATED FACTOR VII AND FACTOR VIIA - The present invention provides conjugates between Factor VII or Factor VIIa peptides and PEG moieties. The conjugates are linked via an intact glycosyl linking group that is interposed between and covalently attached to the peptide and the modifying group. The conjugates are formed from both glycosylated and unglycosylated peptides by the action of a glycosyltransferase. The glycosyltransferase ligates a modified sugar moiety onto either an amino acid or glycosyl residue on the peptide. Also provided are pharmaceutical formulations including the conjugates. Methods for preparing the conjugates are also within the scope of the invention. | 05-06-2010 |
20100121034 | Hydrolysable Polymeric FMOC-Linker - The invention relates to Fmoc (9-fluorenyl-methoxycarbonyl)-based polymeric conjugates. These conjugates are useful for extending the in-vivo circulation of protein and peptide drugs. | 05-13-2010 |
20100145020 | METHOD FOR PRODUCING HIGH-PURITY SOLUBLE THROMBOMODULIN - It is an object of the present invention to obtain a soluble thrombomodulin substantially not containing a denatured product of soluble thrombomodulin that may be generated under acidic conditions. The present invention provides a method for producing soluble thrombomodulin substantially not containing a denatured product of the soluble thrombomodulin that may be generated under acidic conditions, from a soluble thrombomodulin-containing material that contains or is suspected to contain the denatured product of the soluble thrombomodulin, which comprises; a step of subjecting the soluble thrombomodulin-containing material to an anion exchanger or hydroxyapatite; and a step of carrying out linear gradient elution, stepwise gradient elution, or gradient elution in which linear gradient elution is combined with stepwise gradient elution under separation conditions in which the denatured product of the soluble thrombomodulin can be separated, wherein said gradient is a gradient of salt concentration, so as to obtain an elution fraction containing soluble thrombomodulin that does not substantially contain the denatured product of the soluble thrombomodulin, either (a) after the position of a fraction has previously been confirmed, or (b) while confirming the elution fraction. | 06-10-2010 |
20110040073 | Covalent Factor VII-Tissue Factor Complex - The present invention relates to novel covalent complexes of a Factor VII polypeptide and a Tissue Factor polypeptide, in particular to such complexes which are functionally active and which have an enhanced proteolytic activity towards Factor X compared to the corresponding free Factor VII polypeptide as well as methods for production of these novel complexes. | 02-17-2011 |
20110230645 | PURIFICATION OF FACTOR V - The invention provides methods for purifying blood coagulation Factor V from biological fluids. | 09-22-2011 |
20120178908 | TARGETING TISSUE FACTOR TO ACTIVATED PLATELETS - The current invention relates to procoagulant fusion proteins, polynucleotides that encode said fusion proteins and cells that expresses said fusion proteins. Furthermore, the current invention relates to fusion proteins for use as a medicament. Individuals that have a coagulopathy, such as haemophilia A and B with or without inhibitors, may be treated with fusions proteins of the current invention. | 07-12-2012 |
20130079498 | PROCESS FOR PURIFYING VITAMIN K DEPENDENT PROTEINS SUCH AS COAGULATION FACTOR IX - A process of manufacturing a prion-free Vitamin K dependent Protein in a purification sequence employing chromatography characterized in that
| 03-28-2013 |
20130289246 | INFLUENZA VIRUS ANTIBODIES AND IMMUNOGENS AND USES THEREFOR - The present invention is directed to particular monoclonal antibodies and fragments thereof that find use in the detection, prevention and treatment of influenza virus infections. In particular, these antibodies may neutralize or limit the replication of influenza virus. Also disclosed are improved methods for producing such monoclonal antibodies, including novel immunogens for use in vaccination and production of protective immune responses. | 10-31-2013 |
20130317197 | METHODS FOR CAPTURING VIRUS LIKE PARTICLES FROM PLANTS USING EXPANDED BED CHROMATOGRPAHY - The present invention relates to a method for capturing virus-like particles of interest from a mixture comprising the use of an expanded bed of adsorbent; suitably wherein said method comprises the steps of: (a) providing an expanded bed of adsorbent; (b) contacting the mixture with the adsorbent such that the constituents of the mixture contact the expanded bed of adsorbent; (c) optionally washing the adsorbent; and (d) optionally eluting the particle of interest from the adsorbent. | 11-28-2013 |
20140039160 | NOVEL PROCESS FOR THE PREPARATION OF A VIRUS-INACTIVATED FV CONCENTRATE STARTING FROM HUMAN PLASMA, SCALABLE TO INDUSTRIAL LEVEL - The present invention provides a process for purifying FV starting from human plasma or a fractionation intermediate thereof, that is simple, scalable to the industrial level and relatively inexpensive compared to the methods described in the literature to date. The invention consists of the use of two anion exchange chromatography steps, the first of which has the purpose of separating the FV from the PTC component factors, while the second has the purpose of isolating the protein of interest from the majority of plasma proteins by means of selective interaction with the weak anion exchange support used. The process developed has also had a viral inactivation step and a viral removal step included, contributing to the safety of the final product obtained, without however significantly altering the process total recovery of FV, and without necessitating the introduction of additional steps for eliminating the inactivating agents used, thanks to the order in which the various steps are conducted. The process described in the present invention also enables an FV concentrate to be obtained that is stable once frozen at −20° C. | 02-06-2014 |
20140046028 | 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. | 02-13-2014 |
530382000 | Fibrin or fibrin intermediates, e.g., fibrinogen, etc. | 17 |
20080207878 | Process for separating proteins fibrinogen, factor XIII and biological glue from a solubilized plasma fraction and for preparing lyophilised concentrates of said proteins - Process for separating proteins fibrinogen, Factor XIII and biological glue from a solubilized plasma fraction and for preparing lyophilised concentrates of said proteins | 08-28-2008 |
20080281081 | Polyvinyl Pyrollidone Cryoprecipitate Extraction of Clotting Factors - Blood collection, processing and transfer leads to the separation of discrete fractions by adding additional citrate (trisodium citrate) to bring the citrate concentration to 10%-15% w/v thereby leading to enhanced yield and purity of cryoprecipitate. The improved cryoprecipitate then yields concentrated clotting factors by an improved extraction process which uses polyvinyl pyrollidone to reduce the extraction of fibrinogen. Following extraction the remaining cryoprecipitate can advantageously be formed into a fibrin fabric used in surgeries and in the treatment of wounds | 11-13-2008 |
20090018313 | ENHANCED PRODUCTION OF BLOOD CLOTTING FACTORS AND FIBRIN FABRIC - The blood collection, processing and transfer by separation of discrete components containing additional citrate (at least about trisodium citrate 9% w/v) in one or other of collection or processing bag provides for enhanced yield and purity of cryoprecipitate. Inhibiting the activation or denaturation of blood components including blood cells and plasma proteins and with the removal of the activated and denatured components thereby improving safety and efficacy of end products. The inventive process is particularly suited to an improved extraction process to yield concentrated clotting factors from single donors or limited pools without use of chromatography. Following extraction the remaining cryoprecipitate can advantageously be formed into a fibrin fabric used in surgeries and in the treatment of wounds. | 01-15-2009 |
20090099338 | Novel Protein Highly Producing Recombinant Animal Cell, Method for Preparing the Same, and Method for Mass-Producing Protein Using the Same - A gene encoding a production amount-potentiating factor is introduced into an animal cell to transform the cell. Alternatively, a protein production gene and the gene encoding the production amount-potentiating factor are introduced into the animal cell to transform the cell. Herein, as the production amount potentiating factor, there is used a factor having caspase activity inhibiting activity and/or protein biosynthesis activity potentiating action, for example, baculovirus P35. Further, the animal cell is cultured by a culturing method under a condition that apoptosis is not induced, so that a protein is mass-produced. | 04-16-2009 |
20090326201 | Affinity Adsorbents for Fibrinogen - For the separation, removal, isolation, purification, characterisation, identification or quantification of fibrinogen or a protein that is a fibrinogen analogue, an affinity adsorbent is used that is a compound of formula II wherein one X is N and the other is N, C—Cl or C—CN; Y is O, S or NR | 12-31-2009 |
20100069613 | IMPLANTABLE MATERIALS AND COMPOSITIONS - A method of concentrating proteins from whole blood comprising exposing whole blood to a covalently crosslinked hydrogel to remove water from the blood into the hydrogel to thereby concentrate the proteins in the whole blood. The hydrogel may absorb, for example, 50% or 90% of the water from the blood while excluding proteins with a weight of more than about 15,000 Daltons. In some embodiments, the hydrogels are dry, sterile, and spherical. | 03-18-2010 |
20100145021 | PROCESS FOR ENHANCING PROTEIN RECOVERY YIELDS - A process for enhancing the recovery yield of proteins, especially plasma proteins, from sources containing the proteins, wherein the sources containing the proteins are frozen at temperatures of ≦−70° C., and the proteins from a frozen source after thawing are further processed in a per se known manner. | 06-10-2010 |
20100197893 | METHOD TO PRODUCE FIBRIN MONOMER IN ACID MEDIA FOR USE AS TISSUE SEALANT - ClotFoam is an hemostatic agent designed for use in cases of non-compressible hemorrhage. It can be applied outside the operating room through a mixing needle and/or a spray injection method following abdominal, chest, extremities or other intracavitary severe trauma to promote hemostasis, or it can be used in the operating room for laparoscopic procedures or other surgical procedures in which compression is not possible or recommended. Its crosslinking technology generates an adhesive three-dimensional polymeric network or scaffold that carries a fibrin sealant required for hemostasis. When mixed, Clotfoam produces a foam that spreads throughout a body cavity reaching the lacerated tissue to seal tissue and promote the coagulation cascade. The viscoelastic attachment properties of the foam as well as the rapid formation of a fibrin clot that ensure that the sealant remains at the site of application without being washed away by blood or displaced by movement of the target tissue. The fibrin components are produced by a novel method which does not present thrombin to immune system and can be maintained in solution for six weeks without significant proteolytic degradation. | 08-05-2010 |
20110112278 | NOVEL TUMOR MARKER FOR PANCREATIC CANCER - A novel protein and a fragment thereof useful as a tumor marker of pancreatic cancer are disclosed. This protein or a fragment thereof is a modified α-fibrinogen protein containing an oxidized amino acid residue(s) or a fragment thereof containing said oxidized amino acid residue(s). The oxidized amino acid residue(s) is one or more amino acid residues selected from the group consisting of (a) a proline residue corresponding to the proline residue at the position of 530 in SEQ ID NO: 2, and (b) a proline residue corresponding to the proline residue at the position of 565 in SEQ ID NO: 2. | 05-12-2011 |
20120165510 | NOVEL APPLICATION OF FIBRINOGEN-420 AND ITS ACTIVE DOMAIN - The invention discloses a novel application of fibrinogen-420 and its active domain (alpha EC domain), and a separate alpha EC domain protein has the same or similar function with fibrinogen-420. Fibrinogen-420 and its active domain can be widely used in inhibiting protein aggregation, helping protein refolding, drugs which can prevent and/or treat protein conformation disease, detecting denatured protein in quality control and protect protein from denaturation. | 06-28-2012 |
20130005947 | METHOD FOR REMOVING A LYTIC ENZYME FROM A HETEROGENEOUS MIXTURE - The invention relates to purification of an intact, non-degraded macromolecule from a biological mixture comprising the macromolecule in the presence of its lytic enzyme. The method comprises providing the biological mixture as a heterogeneous mixture comprising the lytic enzyme, at least partially, in soluble form and the macromolecule, at least partially, in non-soluble form; batch-wise contacting the heterogeneous mixture with an immobilized inhibitor of the lytic enzyme; increasing the solubility of the macromolecule in the mixture; and removing the immobilized inhibitor from the mixture. | 01-03-2013 |
20130053546 | Use of Anticoagulants in the Production of Recombinant Proteins in the Milk of Transgenic Animals - The invention relates to the production of recombinant human fibrinogen (rhFib) in the milk of transgenic mammalian animals. This production and subsequent purification process is generally hampered by the occurrence of so-called ‘clots’ and ‘flakes’ in the milk which, in severe cases, may prevent the cow from being milked at all, resulting in a halt of lactation. These clots and flakes occur because of the expression of the fibrinogen protein, which is a factor that is normally involved in blood clotting. The invention relates to solving this milk clotting problem by treating the (lactating) animals with anticoagulants such as coumarins. A preferred anticoagulant that is used in the methods of the present invention is warfarin. | 02-28-2013 |
20130144039 | ADSORBENT FOR BLOOD COAGULATION FACTOR OR CELL ADHESION FACTOR AND METHOD FOR PURIFYING THE FACTOR - An objective of the invention is to provide an adsorbent allowing purification of a blood coagulation factor or a cell adhesion factor under mild conditions, according to simple procedures, and at a low cost and safely while having a high affinity and a high resistance to deterioration, and a method for purifying the blood coagulation factor or the cell adhesion factor; a solution is to apply a polypeptide having peptide fragments represented by formula (1) as the adsorbent for the blood coagulation factor or the cell adhesion factor, and to purify the blood coagulation factor or the cell adhesion factor using the adsorbent: | 06-06-2013 |
20130274444 | PROCESS FOR PRODUCTION OF FIBRINOGEN - The present invention relates to a method or process for the manufacture of a virus and prion save native fibrinogen concentrate of high purity and low amounts of fibrinopeptide A and fibronectin. | 10-17-2013 |
20130345401 | FIBRINOGEN-PRODUCING TRANSGENIC SILKWORM - Disclosed is a novel means that enables mass production of highly safe fibrinogen at low cost. The transgenic silkworm of the present invention expresses the fibrinogen subunit Aα, Bβ and γ chains in the silk gland cells and produces fibrinogen having coagulation activity in the cocoon filament. Preferably, the transgenic silkworm expresses the subunits in the middle silk gland cells and produces fibrinogen in the sericin layer of the cocoon filament. By recovering fibrinogen from the cocoon of the transgenic silkworm of the present invention, highly safe fibrinogen can be mass-produced at low cost. | 12-26-2013 |
20140148580 | PROCESS FOR SEPARATING PROTEINS FIBRINOGEN, FACTOR XIII AND BIOLOGICAL GLUE FROM A SOLUBILIZED PLASMA FRACTION AND FOR PREPARING LYOPHILISED CONCENTRATES OF SAID PROTEINS - Process for separating proteins fibrinogen, Factor XIII and biological glue from a solubilized plasma fraction and for preparing lyophilised concentrates of said proteins. | 05-29-2014 |
20150045539 | PROCESS FOR PRODUCTION OF FIBRINOGEN AND FIBRINOGEN PRODUCED THEREBY - A process for purifying fibrinogen from a fibrinogen containing source by precipitation of fibrinogen by a precipitating agent from a fibrinogen containing solution in the presence of one or more chelating agent(s) and removal of the supernatant from the fibrinogen paste, characterised in that fibrinogen is extracted from the paste forming a liquid fraction containing fibrinogen, and an undissolved residue, which is separated from the liquid. | 02-12-2015 |
530383000 | Blood coagulation factor VIII, AHF | 32 |
20080200651 | Selective Reduction and Derivatization of Engineered Proteins Comprising at Least One Non-Native Cysteine - The present invention relates to method for selective reduction and derivatization of recombinantly prepared engineered proteins comprising at least one non-native cysteine, wherein the reduction reaction is conducted in the presence of a redox buffer or in the presence of a triarylphosphine reducing agent. | 08-21-2008 |
20100113744 | Stabilization Of Liquid Solutions Of Recombinant Protein For Frozen Storage - The invention relates to a method for stabilizing a bulk solution of recombinant protein for frozen storage, which comprises providing a partially-purified solution of recombinant protein which has a monovalent salt concentration of at least 100 mM, and adding a carbohydrate to said solution in an amount sufficient that, upon freezing, the solution has a glass transition temperature of −56° C. or higher. | 05-06-2010 |
20100168391 | Pegylated Factor VIII - The invention is a proteinaceous construct comprising a Factor VIII molecule having at least a portion of the B domain intact, which is conjugated to a water-soluble polymer such as polyethylene glycol having a molecular weight of greater than 10,000 Daltons. The construct has a biological activity of at least 80% of the biological activity of native Factor VIII, and the in vivo half-life of the construct is increased by at least 1.5 fold as compared to the in vivo half-life of native factor FVIII. | 07-01-2010 |
20100204452 | Purification of Factor VIII Using a Mixed-Mode or Multimodal Resin - A method for purifying a recombinant protein using a multimodal or mixed mode resin containing ligands which comprise a hydrophobic part and a negatively charged part is described. The invention is advantageous in that it is a single step chromatographic process which does not require adjustment of pH or conductivity during loading step and results in high yield and potency. The process is used for the purification of recombinant compositions of coagulation factor, particularly recombinant Factor VIII. | 08-12-2010 |
20100305305 | METHOD FOR PURIFYING FACTOR VIII AND VON WILLEBRAND FACTOR - The purification method includes, starting from a solution selected from (i) a solution containing a mixture of FVIII and FvW, (ii) a solution containing FvW, (iii) a solution derived from a secretion of a non-human animal and (iv) a solution derived from a FVIII-containing plant extract, a step of absorption of FVIII or FvW on an ion-exchange chromatography filter-type membrane. | 12-02-2010 |
20110028693 | BLOOD COAGULATION PROTEIN CONJUGATES - The invention relates to materials and methods of conjugating a water soluble polymer to an oxidized carbohydrate moiety of a blood coagulation protein comprising contacting the oxidized carbohydrate moiety with an activated water soluble polymer under conditions that allow conjugation. More specifically, the present invention relates to the aforementioned materials and methods wherein the water soluble polymer contains an active aminooxy group and wherein an oxime linkage is formed between the oxidized carbohydrate moiety and the active aminooxy group on the water soluble polymer. In one embodiment of the invention the conjugation is carried out in the presence of the nucleophilic catalyst aniline. In addition the generated oxime linkage can be stabilized by reduction with NaCNBH | 02-03-2011 |
20110160435 | PROCESS OF PURIFYING COAGULATION FACTOR VIII - A process of purifying or enriching coagulation FVIII employing chromatography comprising the steps of providing a fraction containing FVIII in an aqueous solution having a high ionic strength; contacting the fraction containing FVIII with a multimodal resin; optionally washing the multimodal resin having FVIII adsorbed with an aqueous washing buffer; eluting FVIII containing fractions by an aqueous elution buffer comprising at least one amino acid which is positively charged at pH 6 to 8; and optionally collecting FVIII containing fractions in purified or enriched form. | 06-30-2011 |
20110282032 | PROCESS FOR HIGHLY SELECTIVE PURIFICATION OF TWO PLASMA PROTEINS: VON WILLEBRAND FACTOR (VWF) AND FIBRONECTIN (FN) - There is described a chromatographic purification process that allows highly purified von Willebrand factor (vWF) and Fibronectin (Fn) to be obtained, starting from a biological fraction enriched in vWF and Fn and easily scaled up to industrial level. Chromatographic purification was obtained by a strong anionic exchange resin. The concentrates obtained have a high specific activity and, given the low content of contaminant proteins, are particularly suitable for therapeutic use. | 11-17-2011 |
20120016105 | PURIFICATION OF PEPTIDE CONJUGATES BY HYDROPHOBIC INTERACTION CHROMATOGRAPHY - The present invention provides polypeptides that include an O-linked glycosylation site that is not present in the wild-type peptide. The polypeptides of the invention include glycoconjugates in which a species such as a water-soluble polymer, a therapeutic agent of a biomolecule is covalently linked through an intact O-linked glycosyl residue to the polypeptide. Also provided are methods of making a glycoconjugate, methods of isolating a glycoconjugate from a reaction mixture, pharmaceutical compositions containing a glycoconjugate, and methods of treating, ameliorating or preventing diseased in mammals by administering an amount of a glycoconjugate sufficient to achieve the desired response. | 01-19-2012 |
20120136139 | COUNTER-PRESSURE FILTRATION OF PROTEINS - A method is disclosed for filtering a protein in a liquid mixture in a manner that does not substantially damage or otherwise limit the recovery of the protein in the filtration filtrate. The method generally includes passing a liquid mixture containing a protein (e.g., an aqueous vWF mixture) through a filter while applying a counter pressure to the liquid mixture filtrate to accurately reduce and control the pressure differential across the filter. The disclosed method has the advantage that relatively high filtration flow rates can be achieved at relatively low pressure differentials, in contrast to high pressure differentials, which actually reduce the filtration flow rate of protein liquid mixtures. Further, the method can recover substantially all of the protein that is initially present in the liquid mixture. | 05-31-2012 |
20120149874 | METHOD FOR PREPARING RECOMBINANT GLYCOPROTEINS WITH HIGH SIALIC ACID CONTENT - The present disclosure relates to a method for preparing recombinant glycoproteins with high sialic acid content. More specifically, for UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE/MNK) enzyme where point mutation was induced by substituting arginine at position 263 by leucine only or by further substituting arginine at position 266 by glutamine, epimerase activity is constantly maintained, and overexpressed cells thereof experience an increase in intracellular cytidine monophosphate (CMP)-sialic acid content, irrespective of CMP-sialic acid concentration. Particularly, since in an glycoprotein(such as, erythropoietin and thrombopoietin)-producing host cell where point mutationinduced GNE/MNK, human alpha-2,3-sialyltransferase and a CMP-sialic acid transporter gene are simultaneously overexpressed, intracellular content of CMP-sialic acid and sialic acid in glycoprotein increases in cells, overexpression in a host cell producing a sialylated recombinant glycoprotein the three genes above may be useful for preparing glycoprotein with increased sialic acid content. | 06-14-2012 |
20120184715 | Eluate Collection Using Conductivity Gradient - The present specification discloses methods of eluting a protein from a chromatography column. | 07-19-2012 |
20120208982 | Viral Inactivation Using Improved Solvent-Detergent Method - The present specification discloses methods of inactivating a lipid-coat containing virus and proteins essentially free of a lipid-coat containing virus obtained from such methods. | 08-16-2012 |
20120232252 | FACTOR VIII POLYMER CONJUGATES - The invention is a proteinaceous construct comprising a Factor VIII molecule which is conjugated to a water-soluble polymer via carbohydrate moieties of Factor VIII, and methods of preparing same. | 09-13-2012 |
20120271039 | METHOD FOR PURIFYING ACTIVE GLA-DOMAIN COAGULATION PROTEINS - A method for purifying biologically active GLA-domain coagulation proteins, includes 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 substrate 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) 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 biologically active GLA-domain coagulation protein(s) in a purified form. | 10-25-2012 |
20130274445 | FACTOR VIII CONJUGATES - This invention relates to Factor VIII muteins that are covalently bound, at a predefined site that is not an N-terminal amine, to one or more biocompatible polymers such as polyethylene glycol. The mutein conjugates retain FVIII procoagulant activity and have improved pharmacokinetic properties. | 10-17-2013 |
20130281671 | Systems for Factor VIII Processing and Methods Thereof - The present invention provides methods of reducing nonprocessed Factor VIII or a chimeric polypeptide comprising Factor VIII comprising co-transfecting in a host cell a polynucleotide encoding Factor VIII with a polynucleotide encoding a protein convertase, where the endogenous processing enzymes of the host cell are insufficient to convert all of the Factor VIII to its processed isoform; expressing a proprotein convertase from a second polynucleotide in the host cell; and reducing the nonprocessed Factor VIII by processing with said proprotein convertase. | 10-24-2013 |
20130345402 | Devices and Methods for Integrated Continuous Manufacturing of Biological Molecules - The present invention relates to a process and apparatus for purifying a molecule of interest from a heterogeneous clarified fluid mixture. The apparatus of the invention generally comprises a continuous perfusion fermentation system, a continuous particle removal system integrated with the perfusion fermentation system; and a continuous purification system integrated with the particle removal system, which is maintained under sterile conditions. The process comprises filtering a heterogeneous clarified fluid mixture by continuous ultrafiltration at a specific flow rate below the transition point of the molecule of interest in the pressure-dependent region of the flux versus TMP curve, wherein the specific flow rate is maintained substantially constant throughout the continuous ultrafiltration. | 12-26-2013 |
20130345403 | AQUEOUS FACTOR VIII SOLUTION - The present invention relates to methods for stabilizing FVIII in aqueous solutions comprising a relatively high concentration of FVIII. The invention furthermore relates to such aqueous solutions as well as use thereof. | 12-26-2013 |
20140024808 | FACTOR VIII POLYMER CONJUGATES - The invention is a proteinaceous construct comprising a Factor VIII molecule which is conjugated to a water-soluble polymer via carbohydrate moieties of Factor VIII, and methods of preparing same. | 01-23-2014 |
20140051832 | METHOD FOR THE PRODUCTION OF RECOMBINANT HUMAN FACTOR VIII - The object of the present invention is to provide methods for the production of recombinant human Factor VIII, employing specific endoproteases, thus assuring full proteolytic processing of said factor even during its biosynthesis, consequently avoiding additional purification steps. Other objects of the present invention are the recombinant human Factor VIII as obtained by said methods, pharmaceutical compositions, related uses and therapeutic methods. | 02-20-2014 |
20140107320 | BLOOD COAGULATION PROTEIN CONJUGATES - The invention relates to materials and methods of conjugating a water soluble polymer to an oxidized carbohydrate moiety of a blood coagulation protein comprising contacting the oxidized carbohydrate moiety with an activated water soluble polymer under conditions that allow conjugation. More specifically, the present invention relates to the aforementioned materials and methods wherein the water soluble polymer contains an active aminooxy group and wherein an oxime linkage is formed between the oxidized carbohydrate moiety and the active aminooxy group on the water soluble polymer. In one embodiment of the invention the conjugation is carried out in the presence of the nucleophilic catalyst aniline. In addition the generated oxime linkage can be stabilized by reduction with NaCNBH | 04-17-2014 |
20140221618 | TARGETED COAGULATION FACTORS AND METHOD OF USING THE SAME - Targeted coagulation factors comprising a coagulation factor linked with at least one domain that specifically binds to a membrane protein on a blood cell is provided. The disclosed targeted coagulation factors increase the efficiency of coagulation factors and prolong their duration of action and thus, are an improvement for the treatment of hematological diseases such as hemophilia A. | 08-07-2014 |
20140329994 | BRANCHED POLYMERS - The present invention is directed to branched reactive water-soluble polymers comprising at least two polymer arms, such as poly(ethylene glycol), attached to a central aliphatic hydrocarbon core molecule through heteroatom linkages. The branched polymers bear at least one functional group for reacting with a biologically active agent to form a biologically active conjugate. The functional group of the branched polymer can be directly attached to the aliphatic hydrocarbon core or via an intervening linkage, such as a heteroatom, -alkylene-, —O-alkylene-O—, -alkylene-O-alkylene-, -aryl-O—, —O-aryl-, (—O-alkylene-) | 11-06-2014 |
20150018525 | METHOD OF PRODUCING RECOMBINANT HIGH MOLECULAR WEIGHT vWF 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 | 01-15-2015 |
20150315263 | MONOLITH-BASED PSEUDO-BIOAFFINITY PURIFICATION METHODS FOR FACTOR VIII AND APPLICATIONS THEREOF - The present disclosure relates to purification of Factor VIII protein and/or its fragments from various sources by employing monolith based pseudobioaffinity purification methods. In particular, L-histidine over CIM monolith [Histidine Ligand Affinity Chromatography (HLAC)] is used for the purification of wild-type factor VIII from plasma cryoprecipitate, recombinant B-domain deleted factor VIII (rBDD-FVIII) expressed in various host systems and recombinant factor VIII light chain expressed in | 11-05-2015 |
20160024180 | PURIFICATION OF VWF - The present invention provides a method of purifying multimeric von Willebrand Factor (VWF) from a solution comprising multimeric VWF and contaminants. The method comprises passing the solution through a chromatography column comprising beads of a mixed mode chromatography resin coated with a size-exclusion inactive shell and collecting the multimeric VWF which passes through the column without binding to the resin. | 01-28-2016 |
20160058842 | FACTOR VIII POLYMER CONJUGATES - The invention is a proteinaceous construct comprising a Factor VIII molecule which is conjugated to a water-soluble polymer via carbohydrate moieties of Factor VIII, and methods of preparing same. | 03-03-2016 |
20160175402 | POLYMER-FACTOR VIII MOIETY CONJUGATES | 06-23-2016 |
20160185817 | PURIFICATION OF CHIMERIC FVIII MOLECULES - The invention is directed to methods of purifying a chimeric protein comprising subjecting the chimeric protein to a factor VIII-specific affinity chromatography, and subjecting the chimeric protein to an AEX chromatography; wherein the chimeric protein comprises a factor VIII protein or a fragment thereof. The chimeric protein purified by the present methods shows improved factor VIII activity. | 06-30-2016 |
20160193353 | FACTOR VIII: REMODELING AND GLYCOCONJUGATION OF FACTOR VIII | 07-07-2016 |
20160200795 | FACTOR VIII: REMODELING AND GLYCOCONJUGATION OF FACTOR VIII | 07-14-2016 |
530384000 | Blood coagulation factor II or factor II + VII + IX + X, i.e., prothrombin complex or factor | 6 |
20080207879 | METHOD FOR THE PURIFICATION OF RECOMBINANT BLOOD COAGULATION FACTOR IX ENRICHED IN SULFATED AND/OR PHOSPHORYLATED MOLECULES - The present invention relates to a method for the purification of rFIX using anion exchange chromatography in the pseudo-affinity mode, wherein said method comprises a wash step with a wash buffer having a salt concentration of more than 200 mM. The purification according to the invention provides a method to enrich rFIX molecules which have been posttranslationally modified by sulfation and/or phosphorylation. The present invention further relates to purified rFIX compositions enriched in monosulfated and/or monophosphorylated rFIX molecules. | 08-28-2008 |
20090221800 | Method for the Production of Recombinant Proteins - The present invention relates to a process for the production of recombinant polypeptides in leukocytes. | 09-03-2009 |
20130150557 | METHOD FOR THE PURIFICATION OF RECOMBINANT BLOOD COAGULATION FACTOR IX ENRICHED IN SULFATED AND/OR PHOSPHORYLATED MOLECULES - The present invention relates to a method for the purification of rFIX using anion exchange chromatography in the pseudo-affinity mode, wherein said method comprises a wash step with a wash buffer having a salt concentration of more than 200 mM. The purification according to the invention provides a method to enrich rFIX molecules which have been posttranslationally modified by sulfation and/or phosphorylation. The present invention further relates to purified rFIX compositions enriched in monosulfated and/or monophosphorylated rFIX molecules. | 06-13-2013 |
20130296534 | FUSION PROTEIN HAVING FACTOR IX ACTIVITY - Disclosed is a fusion protein comprising blood coagulation factor IX (FIX) and transferrin. The fusion protein exhibits improved specific FIX activity, as compared to native FIX, and can be useful in the treatment of FIX deficiency-associated diseases. | 11-07-2013 |
20140303353 | METHODS FOR PROCESSING COAGULATION FACTORS - The present application relates to methods for purifying recombinant coagulation factor proteins, including for example, prothrombin (Factor II). In embodiments, the methods provide purified prothrombin that exhibit increased bioactivity and reduced levels of thrombin, thereby increasing the safety of the prothrombin. Also provided are purified recombinant coagulation factor proteins. | 10-09-2014 |
20140316112 | METHOD OF INCREASING THE HYDRODYNAMIC VOLUME OF POLYPEPTIDES BY ATTACHING TO GONADOTROPHIN CARBOXY TERMINAL PEPTIDES - This invention is directed to the use of a chorionic gonadotrophin carboxy terminal peptide (CTP) or fragments thereof for modifying a polypeptide or a fragment thereof in order to increase the hydrodynamic volume of the polypeptide or fragment thereof. | 10-23-2014 |