Immunological Separation Or Affinity Chromatography Patents (Class 530/413)
-
Patent number: 8598337Abstract: This invention relates to improved methods for purifying polysaccharides from cellular components, such as a cell wall. The method relates to hydrolyzing and separating the polysaccharides, thereby resulting in purified polysaccharides useful for producing antigens, antibodies, and vaccines comprising the polysaccharides alone or conjugated to carrier molecules. This method is simple, rapid, efficient, scalable, and reproducible.Type: GrantFiled: January 12, 2007Date of Patent: December 3, 2013Assignees: Baxter International Inc., Baxter Healthcare S.A.Inventors: Francis Michon, Catherine Uitz
-
Publication number: 20130317198Abstract: The present disclosure provides methods for purifying products from a fluid. In some embodiments, provided purification methods use a combination of purification modes (e.g., protein A and ion exchange) operated in tandem, wherein at least one of the modes utilizes weak partitioning. In some embodiments, provided purification methods operate under robust conditions in which a degree of binding between a product and resin is maintained despite variations in operating parameters.Type: ApplicationFiled: July 29, 2011Publication date: November 28, 2013Applicant: Pfizer Inc.Inventors: Jonathan Lee Coffman, Ranganathan Godavarti, Michael Shamashkin
-
Patent number: 8592555Abstract: The present invention relates to modified immunoglobulin-binding proteins, e.g., Staphylococcus protein A, having improved binding specificity for immunoglobulins and methods of making and using the same.Type: GrantFiled: August 4, 2009Date of Patent: November 26, 2013Assignee: EMD Millipore CorporationInventor: Shari Spector
-
Publication number: 20130309691Abstract: The present invention relates to a solid support having a heat-resistant biotin-binding protein attached thereto. The present invention also relates to the use of the solid support of the present invention having a heat-resistant biotin-binding protein attached thereto. The present invention further relates to technical fields such as purification, concentration, detection and/or capture of a biotin-linked substance by means of a heat-resistant biotin-binding protein. Such a biotin-binding protein used in the solid support of the present invention is heat-resistant and is therefore useful for use in assay systems involving exposure to a temperature of 70° C. or more.Type: ApplicationFiled: July 11, 2013Publication date: November 21, 2013Applicant: JAPAN TOBACCO INC.Inventors: Yoshimitsu TAKAKURA, Satoru USAMI, Masako ICHIKAWA
-
Patent number: 8584869Abstract: The present invention provides an absorbent which can remove cells present in blood including activated leukocytes such as granulocytes and monocytes, and cancer cells as well as can remove cytokines which facilitate the activation of the remaining cells, and further has no concern for pressure loss and has high configuration stability. That is, the present invention provides an absorbent which absorbs the granulocytes and the monocytes in blood, an absorbent for cancer therapy which absorbs an immunosuppressive protein and an absorbent having a bilayer structure of a net and a nonwoven fabric, having a zeta potential of ?20 mV or more, as well as a blood circulation column containing any of the absorbents filled therein.Type: GrantFiled: March 31, 2006Date of Patent: November 19, 2013Assignee: Toray Industries, Inc.Inventors: Masaaki Shimagaki, Yasufumi Yamamura, Katsuhisa Sato, Kazuo Teramoto, Takeshige Oozeki, Shigehisa Wada
-
Publication number: 20130296538Abstract: Large-scale downstream processing of secreted recombinant proteins is provided in a single device, wherein the contents of a plurality of bioreactors are combined simultaneous to their harvesting and purification resulting in significant savings of time and the cost of manufacturing.Type: ApplicationFiled: July 12, 2013Publication date: November 7, 2013Inventor: Sarfaraz K. Niazi
-
Publication number: 20130295646Abstract: 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 the protein on a chromatographic substrate on which is grafted a ligand having both a hydrophobic characteristic and an ionic characteristic in pH conditions enabling the protein to be retained on the substrate, the pH being higher than 4.6; c) elution of the protein; d) purification of the eluted fraction by removing the milk proteins from the eluted fraction; and e) recovering the protein.Type: ApplicationFiled: June 5, 2013Publication date: November 7, 2013Applicant: LFB BIOTECHNOLOGIESInventors: Alain LEJARS, Michel Nogre, Monique Ollivier
-
Patent number: 8574589Abstract: Bordetella pertussis p69 antigen is purified by immobilized metal affinity chromatography.Type: GrantFiled: May 10, 2010Date of Patent: November 5, 2013Assignee: Novartis AGInventor: Christian A. Lease
-
Patent number: 8568594Abstract: Embodiments of the present invention are directed to articles of manufacture, devices, methods and apparatus for performing liquid chromatography featuring a chromatographic sorbent having one or more pentafluorophenyl groups, wherein said one or more pentafluorophenyl groups are a bonded phase on a sorbent selected from the group comprising silica, organic polymers or hybrid organic silane material and said pentafluorophenyl groups are in a mono-, bi-, and tridentate forms.Type: GrantFiled: July 10, 2012Date of Patent: October 29, 2013Assignee: Waters Technologies CorporationInventors: Martin Gilar, Ying-Qing Yu, Jennifer Fournier, John E. O'Gara
-
Patent number: 8569464Abstract: The present invention relates to a selectively soluble polymer capable of binding to a desired molecules in an unclarified mixture containing various biological materials and the methods of using such a polymer to purify a molecule from such a mixture. The polymer is soluble in the mixture under a certain set of process conditions such as pH or temperature and/or salt concentration and is rendered insoluble and precipitates out of solution upon a change in the process conditions. The polymer is capable of binding to the desired molecule (protein, polypeptide, etc) and remains capable of binding to that molecule even after the polymer is precipitated out of solution. The precipitate can then be filtered out from the remainder of the stream and the desired biomolecule is recovered such as by elution and further processed.Type: GrantFiled: December 16, 2008Date of Patent: October 29, 2013Assignee: EMD Millipore CorporationInventors: Wilson Moya, Jad Jaber
-
Publication number: 20130280788Abstract: The present invention is directed to a continuous affinity chromatography method and to an apparatus to be used in such method. The method allows the use of high operational velocity while maintaining high binding capacities.Type: ApplicationFiled: April 19, 2013Publication date: October 24, 2013Applicant: Merck Patent GmbHInventor: Romas SKUDAS
-
Publication number: 20130274178Abstract: The invention provides a peptide triazole conjugate and derivatives thereof, and methods of its use. The invention also provides an antibody to the peptide triazole conjugate. The invention further provides a method of identifying an HIV-1 entry inhibitor candidate.Type: ApplicationFiled: March 27, 2013Publication date: October 17, 2013Applicant: Philadelphia Health & Education Corporation d/b/a Drexel University College of MedicineInventor: Philadelphia Health & Education Corporation d/b/a Drexel University College of Medicine
-
Publication number: 20130261290Abstract: The invention relates to a method for preparative in vitro protein synthesis in a cell-free transcription/translation system, comprising the following steps: a) in a reaction vessel, a reaction solution is prepared, comprising the following synthesis substances: components of the transcription/translation apparatus for a defined-protein, amino acids, and metabolic components supplying energy and being necessary for the synthesis of the defined protein, b) the synthesis is performed in the reaction vessel in a defined period of time, c) after expiration of the defined period of time, the reaction solution is subjected to a separation step, in which generated low-molecular metabolic products are separated from the solution (and extracted).Type: ApplicationFiled: April 19, 2013Publication date: October 3, 2013Inventors: JAN STREY, HELMUT MERK, WOLFGANG STIEGE
-
Patent number: 8546548Abstract: The present invention relates to a new and improved method for preparing a highly concentrated immunoglobulin composition from pooled plasma for subcutaneous injection. A composition comprising 20% or more immunoglobulin suitable for subcutaneous use is also described.Type: GrantFiled: May 27, 2010Date of Patent: October 1, 2013Assignees: Baxter International Inc., Baxter Healthcare S.A.Inventors: Wolfgang Teschner, Harald Arno Butterweck, Azra Pljevljakovic, Theresa Friederike Bauer, Bernhard Koelbl, Hans-Peter Schwarz, Nebojsa Nikolic, Gerhard Poelsler, Johanna Kindermann
-
Patent number: 8541178Abstract: Methods to detect, characterize, and quantitate biological samples after administration of antibody conjugates, antibody-drug conjugates of Formula I, antibodies, and fragments and metabolites thereof, by immunoaffinity bead separation, chromatography, and mass spectrometry are disclosed; Ab-(L-D)p??I wherein Ab is an antibody; D is a drug moiety; L is a linker covalently attached to Ab, and covalently attached to D; and p is 1, 2, 3, 4, 5, 6, 7, or 8.Type: GrantFiled: May 12, 2009Date of Patent: September 24, 2013Assignee: Genentech, Inc.Inventors: Surinder Kaur, Ola Saad, Keyang Xu
-
Publication number: 20130245139Abstract: The present invention provides novel compositions and methods for removal of protein aggregates from a sample in a flow-through mode.Type: ApplicationFiled: March 4, 2013Publication date: September 19, 2013Applicant: EMD Millpore CorporationInventors: Mikhail Kozlov, William Cataldo, Ajish Potty, Kevin Galipeau, James Hamzik, Joaquin Umana, Lars Peeck
-
Patent number: 8536316Abstract: The present invention relates, at least in part, to improved methods of protein purification. In particular, the present invention relates, at least in part, to methods for purifying an Fc region containing protein from a composition comprising the Fc region containing protein and one or more impurities, where the methods eliminate the need for a holding tank and/or a buffer exchange step.Type: GrantFiled: August 5, 2010Date of Patent: September 17, 2013Assignee: EMD Millipore CorporationInventors: Neil Soice, John Dana Hubbard, Yu Zhang, James Hamzik
-
Patent number: 8524470Abstract: The current invention comprises a method for producing an immunoglobulin or immunoglobulin fragment with defined glycostructure comprising the following steps: a) providing an affinity chromatography column eluate containing the immunoglobulin or immunoglobulin fragment, b) incubating the affinity chromatography column eluate with (?1,3)galactosidase of plant origin, e.g. from green coffee beans (EC 3.2.1.22), c) applying the incubated affinity chromatography column eluate to a protein A chromatography material and recovering the immunoglobulin or immunoglobulin fragment from the protein A chromatography material and thereby producing an immunoglobulin or immunoglobulin fragment with defined glycostructure.Type: GrantFiled: July 28, 2010Date of Patent: September 3, 2013Assignee: Hoffman-La Roche, Inc.Inventors: Markus Haberger, Christine Jung, Dietmar Reusch
-
Publication number: 20130225796Abstract: Problems to be Solved: The present invention provides a simpler and less expensive method for purifying physiologically active proteins, especially antibodies, which can ensure removal of impurities such as DNA contaminants and viruses, and which can minimize a loss of physiologically active proteins. Means for Solving the Problems: A method for removing impurities in a physiologically active protein-containing sample, which comprises the following steps: 1) allowing the physiologically active protein-containing sample to be converted into an aqueous solution of low conductivity at a pH below the isoelectric point of the physiologically active protein; and 2) removing the resulting particles.Type: ApplicationFiled: March 20, 2013Publication date: August 29, 2013Applicant: Chugai Seiyaku Kabushiki KaishaInventor: Chugai Seiyaku Kabushiki Kaisha
-
Patent number: 8513393Abstract: The invention relates to a process for reducing the concentration of free Fc-moieties in a fluid comprising an Fc-containing protein comprising a cation exchange chromatography step.Type: GrantFiled: August 27, 2007Date of Patent: August 20, 2013Assignee: Ares Trading S.A.Inventors: Alex Eon-Duval, Alain Lamproye
-
Patent number: 8506797Abstract: Large-scale downstream processing of secreted recombinant proteins is provided in a single device, wherein the contents of a plurality of bioreactors are combined simultaneous to their harvesting and purification resulting in significant savings of time and the cost of manufacturing.Type: GrantFiled: February 21, 2012Date of Patent: August 13, 2013Assignee: Therapeutic Proteins International, LLCInventor: Sarfaraz Khan Niazi
-
Publication number: 20130203101Abstract: A method is provided for purifying a protein comprising the steps of providing a heme tag with an open coordination site and tagging the recombinant protein of interest with the heme tag. A resin framework is used, wherein a base that binds to heme is immobilized to the resin, and the open coordination site of the heme tag is capable of reversibly binding to the base immobilized to the resin. The tagged protein is reversibly bound to the resin, then eluted from the resin and quantified. The method enables the tagged protein to be tracked during protein expression or purification, and can be used to identify secretion of a protein to the periplasm or to tag proteins in the cytoplasm.Type: ApplicationFiled: January 28, 2011Publication date: August 8, 2013Applicant: UNIVERSITY OF ROCHESTERInventors: Kara L. Bren, Wesley B. Asher
-
Patent number: 8501918Abstract: The present invention provides a method for enhancing an immune response in a mammal to facilitate the elimination of a chronic pathology. The method involves the removal of immune system inhibitors such as soluble TNF receptor from the circulation of the mammal, thus, enabling a more vigorous immune response to the pathogenic agent. The removal of immune system inhibitors is accomplished by contacting biological fluids of a mammal with one or more binding partner(s) such as TNF? muteins capable of binding to and, thus, depleting the targeted immune system inhibitor(s) from the biological fluids. Particularly useful in the invention is an absorbent matrix composed of an inert, biocompatible substrate joined covalently to a binding partner, such as a TNF? mutein, capable of specifically binding to a targeted immune system inhibitor such as soluble TNF receptor.Type: GrantFiled: February 11, 2009Date of Patent: August 6, 2013Assignee: Cytologic, Inc.Inventor: Mark Douglas Howell
-
Publication number: 20130197200Abstract: The present invention provides novel and improved protein purification processes which incorporate certain types of carbonaceous materials and result in effective and selective removal of certain undesirable impurities without adversely effecting the yield of the desired protein product.Type: ApplicationFiled: August 2, 2012Publication date: August 1, 2013Applicant: EMD Millipore CorporationInventors: Nanying Bian, Christopher Gillespie, Matthew T. Stone, Mikhail Kozlov, Jie Chen, Martin Siwak
-
Patent number: 8497358Abstract: Provided is a purification method that purifies an antibody to a high purity, effectively removes antibody polymer (or aggregate), and improves antibody recovery rate. An antibody purification method including a step for treating a solution containing an antibody by mixed mode chromatography in the presence of an amino acid is provided.Type: GrantFiled: December 18, 2009Date of Patent: July 30, 2013Assignee: Takeda Pharmaceutical Company LimitedInventors: Masato Suenaga, Takeshi Hayakawa, Takuya Muramoto
-
Publication number: 20130190254Abstract: Polypeptides which bind to the helical transmembrane region of membrane proteins are disclosed, as are methods for the design of polypeptides that bind to the transmembrane region of membrane proteins. Also provided are methods for the use of the disclosed polypeptides in various applications, as well as products made through the practice of the instant methods.Type: ApplicationFiled: December 5, 2012Publication date: July 25, 2013Applicant: THE TRUSTEES OF THE UNIVERSITY OF PENNSYLVANIAInventor: The Trustees of the University of Pennsylvania
-
Publication number: 20130190478Abstract: The current invention reports a method for the purification of a non-glycosylated, heterologous polypeptide, which has been recombinantly produced in a prokaryotic cell, wherein the method comprises three chromatography steps of which the first chromatography step selected from i) hydrophobic charge induction chromatography, or ii) hydrophobic interaction chromatography, or iii) affinity chromatography, or iv) ion exchange chromatography, the second chromatography step is selected from i) anion exchange chromatography, or ii) cation exchange chromatography, or iii) hydroxylapatite chromatography, or iv) hydrophobic interaction chromatography, and the a third chromatography step is selected from i) hydrophobic charge induction chromatography, or ii) anion exchange chromatography, or iii) cation exchange chromatography, or iv) hydrophobic interaction chromatography, whereby the first chromatography step is an affinity chromatography in case of polypeptides capable of interacting with metal ligands, the second cType: ApplicationFiled: September 21, 2012Publication date: July 25, 2013Inventor: Hoffmann-La Roche Inc.
-
Publication number: 20130178370Abstract: Methods and compositions for identification of candidate antigen-specific variable regions as well as generation of antibodies or antigen-binding fragments that could have desired antigen specificity are provided. For example, in certain aspects, methods for determining amino acid sequences of serum antibody CDR3 and abundancy levels are described. In some aspects, methods for determining nucleic acid sequences of antibody variable region sequences and the frequency thereof in biological samples are provided. Furthermore, the invention provides methods for identification and generation of antibodies or antigen-binding fragments that comprise highly-represented CDR domains.Type: ApplicationFiled: November 23, 2012Publication date: July 11, 2013Applicant: The Board of Regents of the University of Texas SystemInventor: The Board of Regents of the University of Texas S
-
Patent number: 8481693Abstract: Methods for purifying human Calciviruses are disclosed, including Noroviruses and Sapoviruses.Type: GrantFiled: March 14, 2008Date of Patent: July 9, 2013Assignee: Takeda Vaccines (Montana), Inc.Inventors: Thomas S. Vedvick, Bryan Steadman, Charles Richardson, Thomas R. Foubert, Charles R. Petrie
-
Publication number: 20130172538Abstract: The objective of the present invention is to provide a method for easily producing a porous cellulose particle which can be used as an adsorbent for various substances in a safe manner without using a highly toxic solvent such as a calcium thiocyanate solution. In addition, the objective of the present invention is to provide a porous particle produced by the production method, an adsorbent which contains the porous particle and by which a highly pure protein can be efficiently purified in a safe manner, and a method for purifying a protein by using the adsorbent.Type: ApplicationFiled: September 12, 2011Publication date: July 4, 2013Applicant: Kaneka CorporationInventors: Masaru Hirano, Yasuyuki Suzuki, Kento Kanaya, Akihisa Kanda, Takuma Suzuki, Yoshikazu Kawai, Ken-Ichiro Morio
-
Publication number: 20130164860Abstract: Methods and apparatuses for detection of target molecules are provided.Type: ApplicationFiled: November 5, 2012Publication date: June 27, 2013Applicants: TECHNION RESEARCH & DEVELOPMENT FOUNDATION LTD., BIO-RAD LABORATORIES, INC.Inventors: BIO-RAD LABORATORIES, INC., TECHNION RESEARCH & DEVELOPMENT FOUNDATION LTD.
-
Publication number: 20130164766Abstract: Methods for obtaining highly pure native, recombinant or modified BAD-1 protein include the steps of culturing a population of microbes expressing BAD-1 protein in a culture medium, collecting the population of microbes from the culture medium, obtaining a BAD-1 protein-containing solution, and purifying the BAD-1 protein from the solution by combining the BAD-1 protein-containing solution with a nickel-chelating resin, washing the nickel-chelating resin to remove unbound matter, and eluting the BAD-1 protein from the nickel-chelating resin. Highly pure native BAD-1 protein may be used in diagnostic kits for detecting Blastomyces dermatitidis infections in animals.Type: ApplicationFiled: December 19, 2012Publication date: June 27, 2013Inventors: Bruce Klein, Theodore Brandhorst
-
Patent number: 8466265Abstract: A method of preparing anti-b amyloid immunoglobulin involves treating human plasma anti-b amyloid immunoglobulin under alkaline conditions, such as at pH 10.25 to 11.75 using diethylamine HCl, to dissociate b amyloid protein therefrom. Typically, the anti-b amyloid immunoglobulin is present in human immunoglobulin preparations obtained from plasma or serum. Anti-b amyloid immunoglobulin prepared by the method is substantially free of b amyloid protein and has therapeutic activity in compositions and/or methods for treating a disease or condition associated with b amyloid plaques, such as Alzheimer's disease.Type: GrantFiled: October 2, 2008Date of Patent: June 18, 2013Assignee: CSL LimitedInventor: John Cox
-
Publication number: 20130150566Abstract: The invention belongs to the field of genetic engineering and biotechnology, and specifically discloses a design, preparation and pharmic application of a tumor-targeted TNF-related apoptosis-inducing ligand's variant. The tumor-targeted TNF-related apoptosis-inducing ligand's variant is generated by a fused protein which is consisted of the ligand of CD13, the connecting peptide and TNF-related apoptosis-inducing ligand's variant, and which is by the construction of coding gene of the variant according to the technology of genetic engineering and clone, soluble recombinant expression and ordinary separation and purification. The variant, produced by the method of preparation of the tumor-targeted TNF-related apoptosis-inducing ligand's variant, has favorable tumor-targeting characteristics and the significant enhancement of the anti-tumor effect.Type: ApplicationFiled: July 6, 2011Publication date: June 13, 2013Applicant: TARGETPHARMA LABORATORIES (CHANGZHOU) CO., LTDInventors: Zichun Hua, Lin Cao, Bo Tang
-
Patent number: 8461302Abstract: 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.Type: GrantFiled: November 23, 2005Date of Patent: June 11, 2013Assignee: Zymogenetics, Inc.Inventors: Carol Jewell, Hardarshan Cheema, Deborah Hogg, Wenmao Meng, Ray O'Donnell, Ewan Robertson, Andrew Topping
-
Publication number: 20130137112Abstract: Provided are dyes and compositions which are useful in a number of applications, such as the detection and monitoring protein aggregation, kinetic studies of protein aggregation, neurofibrillary plaques analysis, evaluation of protein formulation stability, and analysis of molecular chaperone activity.Type: ApplicationFiled: November 30, 2010Publication date: May 30, 2013Inventors: Wayne Forrest Patton, Sergiy M. Yarmoluk, Praveen Pande, Vladyslava Kovalska, Lijun Dai, Kateryna Volkova, Jack Coleman, Mykhaylo Losytskyy, Anthony Ludlam, Anatoliy Balanda, Dee Shen
-
Patent number: 8450465Abstract: The present invention, referred to as Surface-Free Affinity Purification (SFAP), relates to a system and method for purifying low abundance peptides, including digested plasma proteins. SFAP combines the components and processes of Surface-Free Isolation, Specific Competitive Elution, Dual Epitope Isolation and Protective Solvents in the purification of low abundance proteins, all of which may be performed in a single column. This column is a constant volume Diafiltration Column equipped with stirring that can be driven by an HPLC. Digested plasma may be injected into the Diafiltration Column by the HPLC. Immunoglobulins, Specific Competitive Elutants, Protective Solvents are injected in a series of injections that result in the purified peptides bound to the surfaces of a very-low volume hydrophobic reversed phase trap from which they can be easily injected into mass spectrometry detection instruments.Type: GrantFiled: October 5, 2011Date of Patent: May 28, 2013Assignee: Wellspring Clinical Lab, Inc.Inventor: Calvin Wiese
-
Publication number: 20130130248Abstract: The present disclosure provides variant Csy4 endoribonucleases, nucleic acids encoding the variant Csy4 endoribonucleases, and host cells genetically modified with the nucleic acids. The variant Csy4 endoribonucleases find use in a variety of applications, which are also provided. The present disclosure also provides methods of detecting a specific sequence in a target polyribonucleotide; and methods of regulating production of a target RNA in a eukaryotic cell.Type: ApplicationFiled: November 7, 2012Publication date: May 23, 2013Applicant: THE REGENTS OF THE UNIVERSITY OF CALIFORNIAInventor: THE REGENTS OF THE UNIVERSITY OF CALIFORNIA
-
Publication number: 20130131321Abstract: The present invention relates to the use for affinity purification of an antibody or an fragment of an antibody, of a ligand-substituted matrix comprising a support material and at least one ligand covalently bonded to the support material, the ligand being represented by formula (I) wherein Sp is a spacer group; v is 0 or 1; Am is an amide group —NR1—C(O)—, and wherein either NR1 is attached to Ar1 and —C(O)— is attached to Ar2, or —C(O)— is attached to Ar1 and NR1 is attached to Ar2; and R1 is hydrogen or C1 to C4 alkyl, preferably hydrogen or methyl; and more preferably hydrogen; Ar1 is a divalent 5- or 6-membered substituted or unsubstituted aromatic ring; Ar2 is 5- or 6-membered heterocyclic aromatic ring which is (a) attached to a further 5- or 6-membered aromatic ring via a single bond; or (b) fused to a further 5- or 6-membered aromatic ring as part of a multicyclic ring system; or (c) attached to at least one substituent selected from C1 to C4 alkyl; C2 to C4 alkenyl; C2 to C4 alkynyl; aType: ApplicationFiled: August 3, 2011Publication date: May 23, 2013Applicant: GRAFFINITY PHARMACEUTICALS GMBHInventors: Holger Bittermann, Klaus Burkert, Marc Arnold, Oliver Keil, Thomas Neumann, Inge Ott, Kristina Schmidt, Daniel Schwizer, Renate Sekul
-
Patent number: 8440799Abstract: The present application provides methods of purifying A? binding proteins having a Fc region, for example, anti-A? antibodies or antibody fusions, by adsorbing the A? binding protein to a Fc binding agent, such as, for example, Protein A or Protein G, followed by a wash with a divalent cation salt buffer to remove impurities and subsequent recovery of the adsorbed A? binding protein. The present application also features methods of eluting the purified A? binding protein as well as the incorporation of the methods within a purification train. Kits comprising components for carrying out the methods and instructions for use are also provided.Type: GrantFiled: October 12, 2010Date of Patent: May 14, 2013Assignees: Janssen Alzheimer Immunotherapy, Wyeth LLCInventors: Ranganathan Godavarti, Timothy Iskra
-
Publication number: 20130115635Abstract: Described is an epitope tag useful in affinity-based applications. The invention further includes fusion proteins, methods for preparing fusion proteins, nucleic acid molecules encoding these fusion proteins and recombinant host cells that contain these nucleic acid molecules. The invention also relates to nanobodies and other affinity ligands specifically recognizing the epitope tag, and uses thereof in affinity-based applications.Type: ApplicationFiled: May 25, 2011Publication date: May 9, 2013Inventors: Els Pardon, Jan Steyaert, Lode Wyns
-
Patent number: 8435776Abstract: A method of separating a target biological species from a fluid is disclosed comprising contacting the fluid with a ligand-functionalized polymer comprising: a water soluble or water dispersible aminopolymer functionalized with guanidinyl groups; whereby a complex comprising the functionalized substrate and the target biological species is formed.Type: GrantFiled: February 14, 2011Date of Patent: May 7, 2013Assignee: 3M Innovative Properties CompanyInventors: Jerald K. Rasmussen, Kannan Seshadri, Robert T. Fitzsimons, Jr., James I. Hembre, Catherine A. Bothof, Erin A. Satterwhite, George W. Griesgraber, Yi He, Louis C. Haddad
-
Publication number: 20130102761Abstract: Proteins are purified by a mixed-mode chromatography system formed by attaching a ligand with cation exchange and hydrophobic functionalities to a large-pore support matrix, the only linkage between the ligand and the support matrix being a chain having a backbone of no more than three atoms between the hydrophobic group and the support matrix.Type: ApplicationFiled: October 18, 2012Publication date: April 25, 2013Applicant: Bio-Rad Laboratories, Inc.Inventor: Bio-Rad Laboratories, Inc.
-
Publication number: 20130096284Abstract: In large-scale purification of proteins such as antibodies, an economic high-purity purification method is required. The present invention relates to a method for purifying a protein, including one or more chromatographic processes, in which an amino acid; or a dipeptide, an oligopeptide, or a polyamino acid thereof is included in a buffer solution used in at least one chromatographic processes (equilibration buffer, wash buffer, and elution buffer), thereby purifying a high-purity protein with a very small quantity of the impurity (e.g., polymers or host cell proteins).Type: ApplicationFiled: June 20, 2011Publication date: April 18, 2013Applicant: KYOWA HAKKO KIRIN CO., LTD.Inventor: Takashi Ishihara
-
Publication number: 20130084648Abstract: The present disclosure provides methods and compositions for separating polypeptide glycoforms using a medium that includes an Fc receptor. In certain embodiments, a medium includes an Fc receptor which comprises an extracellular portion of an Fc gamma RIII receptor.Type: ApplicationFiled: July 20, 2012Publication date: April 4, 2013Applicant: ZEPTEON, INC.Inventors: Glen Reed Bolton, Austin Wayne Boesch
-
Publication number: 20130053271Abstract: A flexible method for making multiplexed assays for antigen-specific antibody responses is disclosed herein. The method of the present invention comprises incubation of a substrate or a set of beads coated with a dockerin or a cohesin protein with a cohesin or dockerin-antigen fusion proteins to attach the fusion protein essentially irreversibly by non-covalent interaction. The present invention enables the use of one dockerin- or cohesin-coated bead for multiple sets of cohesin- or dockerin-antigens, obviating the need to directly chemically couple new antigens to new beads.Type: ApplicationFiled: August 24, 2012Publication date: February 28, 2013Applicant: BAYLOR RESEARCH INSTITUTEInventors: Gerard Zurawski, Sandra Zurawski
-
Patent number: 8383782Abstract: This invention relates to a composite material that comprises a support member that has a plurality of pores extending through the support member and, located in the pores of the support member, and filling the pores of the support member, a macroporous cross-linked gel. The invention also relates to a process for preparing the composite material described above, and to its use. The composite material is suitable, for example, for separation of substances, for example by filtration or adsorption, including chromatography, for use as a support in synthesis or for use as a support for cell growth.Type: GrantFiled: October 30, 2009Date of Patent: February 26, 2013Assignee: Natrix Separations Inc.Inventors: Ronald F. Childs, Carlos Filipe, Raja Ghosh, Jinsheng Zhou, Elena N. Komkova, Marcus Y. Kim, Tapan K. Dey
-
Publication number: 20130046080Abstract: The present invention relates to a method to improve the sorbent efficiency of protein A chromatography using switching column with continuous feeding. In the chromatography method of the present invention, the increased usage efficiency of the absorbent (resin), the decreased processing time, the decreased operation cycle of column compared to that of single batch-type column, and the reduced amount of used resin are achieved and thus, the target protein can be purified at a high efficiency and a low cost.Type: ApplicationFiled: April 26, 2011Publication date: February 21, 2013Applicant: CELLTRION, INC.Inventors: Su Hi Jeon, Jin-Il kim
-
Publication number: 20130041139Abstract: The present invention provides methods for purifying a polypeptide comprising a CH2/CH3 region, comprising binding the polypeptide to Protein A and eluting with a pH gradient starting at a low pH.Type: ApplicationFiled: September 1, 2010Publication date: February 14, 2013Applicant: Genentech, IncInventors: Arick Brown, Christopher J. Dowd, Asha Nandini Radhamohan
-
Patent number: 8372959Abstract: Disclosed is a method for the production of a heterologous polypeptide of interest with a homogenous N-terminus, using a fusion polypeptide comprising the polypeptide of interest and N-terminally thereto a polypeptide exhibiting autoproteolytic function, said method comprises the steps of a) binding of the fusion polypeptide in a soluble, autoproteolytically inactive form by an affinity chromatography system, b) refolding of the fusion polypeptide, thereby activating the autoproteolytic function of the fusion polypeptide and causing cleavage of the heterologous polypeptide of interest, and c) subsequently eluting the heterologous polypeptide of interest, wherein the steps are conducted on one affinity chromatography system.Type: GrantFiled: January 11, 2012Date of Patent: February 12, 2013Assignees: Sandoz AG, Boehringer Ingelheim RCV GmbH & Co KGInventors: Alois Jungbauer, Rainer Hahn, Anne Tscheliessnig, Waltraud Kaar