Chromatography Or By Septum Selective As To Material, E.g., Gel Filtration, Molecular Sieve Dialysis, Etc. Patents (Class 530/417)
  • Patent number: 10160964
    Abstract: Disclosed is a method for the isolation of extracellular vesicles, including exosomes, from a liquid sample, the method comprising the steps of: adjusting the pH of a liquid sample comprising extracellular vesicles to a preselected, binding pH; contacting the liquid sample with silicon carbide, wherein at the preselected, binding pH, the extracellular vesicles bind to the silicon carbide; and eluting the bound extracellular vesicles from the silicon carbide. The liquid samples can comprise bodily fluids. Further disclosed is a method for producing a liquid sample, substantially depleted of extracellular vesicles, including exosomes.
    Type: Grant
    Filed: May 6, 2016
    Date of Patent: December 25, 2018
    Assignee: Norgen Biotek Corp.
    Inventor: Yousef Haj-Ahmad
  • Patent number: 9994612
    Abstract: Processes are provided for recovering and purifying refolded recombinant proteins produced in heterologous host cells, which includes the step of refolding the protein in a high pH buffer.
    Type: Grant
    Filed: October 26, 2015
    Date of Patent: June 12, 2018
    Assignee: Genentech, Inc.
    Inventors: Shelly Pizarro, Ailen Sanchez, Charles H. Schmelzer
  • Patent number: 9422329
    Abstract: Herein is reported a method for the purification of an antibody directly captured from clarified cell culture supernatants using Streamline CST and/or Capto MMC, wherein especially product related (aggregates and fragments) and process related impurities (host cell protein, media components) could efficiently be removed, resulting in a preparation with a purity comparable to classical protein A affinity chromatography.
    Type: Grant
    Filed: November 2, 2011
    Date of Patent: August 23, 2016
    Assignee: Hoffmann-La Roche Inc.
    Inventors: Roberto Falkenstein, Thorsten Lemm, Markus Strasser, Hidenari Yamada
  • Patent number: 9206227
    Abstract: Herein is reported a method for the purification of an antibody directly captured from clarified cell culture supernatants using Streamline CST and/or Capto MMC, wherein especially product related (aggregates and fragments) and process related impurities (host cell protein, media components) could efficiently be removed, resulting in a preparation with a purity comparable to classical protein A affinity chromatography.
    Type: Grant
    Filed: November 2, 2011
    Date of Patent: December 8, 2015
    Assignee: Hoffmann-La Roche Inc.
    Inventors: Roberto Falkenstein, Thorsten Lemm, Markus Strasser, Hidenari Yamada
  • Patent number: 9200030
    Abstract: Processes are provided for recovering and purifying refolded recombinant proteins produced in heterologous host cells, which includes the step of refolding the protein in a high pH buffer.
    Type: Grant
    Filed: November 2, 2012
    Date of Patent: December 1, 2015
    Assignee: Genentech, Inc.
    Inventors: Shelly Pizarro, Ailen Sanchez, Charles H. Schmelzer
  • Patent number: 9029517
    Abstract: Adsorptive media for chromatography, particularly ion-exchange chromatography, derived from a shaped fiber. In certain embodiments, the functionalized shaped fiber presents a fibrillated or ridged structure which greatly increases the surface area of the fibers when compared to ordinary fibers. Also disclosed herein is a method to add surface pendant functional groups that provides cation-exchange or anion-exchange functionality to the high surface area fibers. This pendant functionality is useful for the ion-exchange chromatographic purification of biomolecules, such as monoclonal antibodies (mAbs).
    Type: Grant
    Filed: July 27, 2011
    Date of Patent: May 12, 2015
    Assignee: EMD Millipore Corporation
    Inventors: David Yavorsky, John Amara, Joaquin Umana, William Cataldo, Mikhail Kozlov, Matthew Stone
  • Publication number: 20150125929
    Abstract: The present invention relates to novel and improved methods for the purification of biomolecules. In particular, the present invention relates to methods of protein purification which employ a porous solid support modified with a charged fluorocarbon composition.
    Type: Application
    Filed: March 18, 2013
    Publication date: May 7, 2015
    Inventors: Mikhail Kozlov, Wilson Moya, Jad Jaber, William Cataldo, Ajish Potty, Christopher Gillespie
  • Publication number: 20150105542
    Abstract: The present invention provides a method and automated system for the purification of polypeptides including the direct filtration of solutions containing the polypeptides after purification.
    Type: Application
    Filed: October 28, 2014
    Publication date: April 16, 2015
    Applicant: Lonza Biologics PLC
    Inventors: Mark R. Whickman, Sam Mansoor
  • Patent number: 9005996
    Abstract: The current invention is a capture-particle comprising: a) a molecular sieve portion; and b) an analyte binding portion; wherein the molecular sieve portion, analyte binding portion or both further comprise a cross-linked region having modified porosity. Capture particles wherein the molecular sieve portion, analyte binding portion or both comprise pore dimensions sufficient to exclude molecules larger than about 60 kDa. These particles are useful in purification and diagnostic methods. Kits comprising the capture particles are also described.
    Type: Grant
    Filed: September 27, 2006
    Date of Patent: April 14, 2015
    Assignee: George Mason Research Foundation
    Inventors: Lance Liotta, Emanuel Petricoin, David Geho
  • Patent number: 8993350
    Abstract: The present invention relates generally to a novel method using HPLC and fluorescence detection of free PEG-mal in PEGylated proteins and PEG-mal raw materials by adding a fluorescent label to the free PEG-mal.
    Type: Grant
    Filed: January 29, 2010
    Date of Patent: March 31, 2015
    Assignee: Bristol-Myers Squibb Company
    Inventors: Mei Lin, Anulfo Valdez
  • Publication number: 20150087816
    Abstract: A material for reverse phase chromatography comprises surface modifying apolar and charged groups bound to a solid support, said charged groups being present in amounts of about 0.25 to about 22% of the surface modifying groups, or in amounts of about 0.01 ?mol/m2 to 0.8 ?mol/m2 referred to the surface of the solid support for a material with a total amount of surface modifying groups of 3.6 ?mol/m2. Such material and suitable purification conditions for active pharmaceutical ingredients (APIs) like peptides can be evaluated by (a) determining the isoelectric point (pI) of the API of interest, (b) choosing a pH in a range where the solid phase material is stable, (c) determining the difference pI-pH and (d) if the difference pI-pH is positive, choosing an anion exchange (AIEX) material, or if the difference pI-pH is negative, choosing an cation exchange (CIEX) material.
    Type: Application
    Filed: March 21, 2013
    Publication date: March 26, 2015
    Applicant: ZEOCHEM AG
    Inventors: Nicola Forrer, Mandy Erdmann, David Gétaz, Massimo Morbidelle, Susanna Bernardi, Rushd Khalaf
  • Publication number: 20150065696
    Abstract: The invention is directed to an apparatus and method for purifying a protein. The apparatus involves the use of a capture chromatography resin, a depth filter arranged after the capture chromatography resin, and a mixed-mode chromatography resin arranged after the depth filter. The method involves providing a sample containing the protein, processing the sample through a capture chromatography resin, a depth filter, and a mixed-mode chromatography resin. A membrane adsorber or monolith may be substituted for the mixed-mode chromatography column.
    Type: Application
    Filed: June 4, 2014
    Publication date: March 5, 2015
    Inventors: Chen Wang, Robert K. Hickman, I, Edwin O. Lundell, Roy D. Hegedus
  • Patent number: 8969532
    Abstract: The present invention provides processes for the manufacturing of polypeptide conjugates. In particular, the invention provides methods for the purification of polypeptide conjugates, which include at least one polymeric modifying groups, such as a poly(alkylene oxide) moiety. Exemplary poly(alkylene oxide) moieties include poly(ethylene glycol) (PEG) and poly(propylene glycol). In an exemplary process, hydrophobic interaction chromatography (HIC) is used to resolve different glycoforms of glycoPEGylated polypeptides.
    Type: Grant
    Filed: October 3, 2007
    Date of Patent: March 3, 2015
    Assignee: Novo Nordisk A/S
    Inventors: Shawn DeFrees, Kyle Kinealy
  • Patent number: 8945872
    Abstract: Expression vector systems are provided for increased production of a recombinant GDF-5 (rhGDF-5) protein. Also provided are transformed host cells that were engineered to produce and express high levels of rhGDF-5 protein. Methods for production and high expression of rhGDF-5 protein are disclosed herein. The methods of enhancing production and protein expression of rhGDF-5 protein as disclosed are cost-effective, time-saving and are of manufacturing quality.
    Type: Grant
    Filed: January 25, 2013
    Date of Patent: February 3, 2015
    Assignee: Warsaw Orthopedic, Inc.
    Inventors: David S. Scher, Roger E. Harrington
  • Patent number: 8933205
    Abstract: The invention provides a process for preparing a cell-binding agent chemically coupled to a drug. The process comprises covalently attaching a linker to a cell-binding agent, a purification step, conjugating a drug to the cell-binding agent and a subsequent purification step.
    Type: Grant
    Filed: February 25, 2013
    Date of Patent: January 13, 2015
    Assignee: ImmunoGen, Inc.
    Inventors: Yong Dai, Yong Wang, Shengjin Jin, Deborah H. Meshulam, Godfrey W. Amphlett
  • Patent number: 8921518
    Abstract: The present invention provides a method for industrial-scale protein separation by reverse phase chromatography by use of a buffer system and an additional salt.
    Type: Grant
    Filed: December 21, 2006
    Date of Patent: December 30, 2014
    Assignee: Novo Nordisk A/S
    Inventors: Daniel E. Rasmussen, Arne Staby, John Strikart Nielsen, Ole Schou
  • Patent number: 8916387
    Abstract: Methods are provided for the prevention, treatment and diagnosis of Alzheimer's disease, based on the glycosylation pattern of amyloid-beta peptides in body fluids and tissues.
    Type: Grant
    Filed: October 28, 2011
    Date of Patent: December 23, 2014
    Inventors: Jonas Nilsson, Adnan Halim, Göran Larson, Kaj Blennow, Gunnar Brinkmalm, Erik Portelius, Henrik Zetterberg
  • Patent number: 8906231
    Abstract: The present invention provides a method and automated system for the purification of polypeptides including the direct filtration of solutions containing the polypeptides after purification.
    Type: Grant
    Filed: September 10, 2010
    Date of Patent: December 9, 2014
    Assignee: Lonza Biologics PLC
    Inventors: Mark R. Whickman, Sam Mansoor
  • Patent number: 8906648
    Abstract: A process for recovering and purifying refolded heparin binding proteins produced in heterologous host cells includes the step of incubation of the solubilized protein with a polyanionic species such as dextran sulfate.
    Type: Grant
    Filed: March 26, 2013
    Date of Patent: December 9, 2014
    Assignee: Genentech, Inc.
    Inventors: Michelle D. Butler, Jeffrey L. Cleland, David W. Kahn, Shelly Pizarro, Charles H. Schmelzer, Marjorie E. Winkler
  • Patent number: 8895710
    Abstract: The present invention relates to a chromatography ligand defined by the following formula R1—R2—N(R3)—R4—R5 wherein R1 is a substituted or non-substituted phenyl group; R2 is a hydrocarbon chain comprising 0-4 carbon atoms; R3 is a hydrocarbon chain comprising 1-3 carbon atoms; R4 is a hydrocarbon chain comprising 1-5 carbon atoms; and R5 is OH or H. The invention also comprises a separation matrix, comprising the described ligands coupled to a porous support, such as particles or a membrane. The ligand and matrix according to the invention is useful for purification of biomolecules or organic compounds, such as proteins, polypeptides, DNA etc. An advantageous use according to the invention is the purification of antibodies.
    Type: Grant
    Filed: January 4, 2011
    Date of Patent: November 25, 2014
    Assignee: GE Healthcare Bio-Sciences AB
    Inventors: Carina Engstrand, Annika Forss, Gunnar Glad, Bo-Lennart Johansson, Hans J. Johansson, Jean-Luc Maloisel
  • Patent number: 8889837
    Abstract: The invention is a method for the purification of mono-PEGylated erythropoietin using two cation exchange chromatography steps wherein the same type of cation exchange material is used in both cation exchange chromatography steps and a method for producing a mono-PEGylated erythropoietin in substantially homogeneous form.
    Type: Grant
    Filed: January 24, 2011
    Date of Patent: November 18, 2014
    Assignee: Hoffman-La Roche Inc.
    Inventors: Josef Burg, Klaus Reichert, Axel Schroth, Hartmut Schurig, Axel Wessner
  • Patent number: 8852435
    Abstract: An assembly capable of capturing and purifying expressed biological products during or at the end of a bioreaction cycle is disclosed wherein a binding resin is kept separated from the contents of the bioreactor allowing capturing, harvesting and purification of biological products in a bioreactor; the invention additionally provides means of removing undesirable metabolic products as well as provides for efficient loading of chromatography columns.
    Type: Grant
    Filed: November 29, 2011
    Date of Patent: October 7, 2014
    Assignee: Therapeutics Proteins International, LLC
    Inventor: Sarfaraz Niazi
  • Patent number: 8846878
    Abstract: A novel method for recovering nucleic acids and proteins from a biological sample having the steps of mixing a biological sample with a nucleic acid binding solution and contacting the mixture with a first porous silica compound configured to reversibly bind a nucleic acid. The fluid remainder of the mixture is gathered for protein extraction. The first silica compound is contacted with a nucleic acid elution solution which causes a majority of the nucleic acid bound to the first porous silica compound to unbind and enter the solution phase. The solution is collected, which contains isolated nucleic acid. The fluid gathered for protein extraction is mixed with a protein binding solution and contacted with a protein binding porous silica compound configured to reversibly bind a protein. The fluid remainder is separated from the protein binding porous silica compound.
    Type: Grant
    Filed: January 22, 2010
    Date of Patent: September 30, 2014
    Assignee: CUBRC Corporation
    Inventors: Richard J. Karalus, David R. Pawlowski
  • Publication number: 20140288283
    Abstract: The invention relates to a truncated L1 protein of the Human Papillomavirus Type 6, a virus-like particle consisting of the protein, a vaccine comprising said virus-like particle, and the use of the vaccine in the prevention of condyloma acuminatum or HPV infections.
    Type: Application
    Filed: April 8, 2014
    Publication date: September 25, 2014
    Applicants: BEIJING WANTAI BIOLOGICAL PHARMACY ENTERPRISE CO., LTD., XIAMEN UNIVERSITY
    Inventors: Shaowei Li, Huirong Pan, Bo Liu, Jun Zhang, Ji Miao, Ningshao Xia
  • Publication number: 20140288272
    Abstract: Processes for producing and purifying recombinant proteins are disclosed. In particular, the present disclosure provides processes of producing and purifying multi-subunit proteins expressed in yeast or filamentous fungal cells. The production and/or purification of such proteins are monitored for impurities, preferably using lectin binding assays, such that one or more process parameters may be adjusted to maximize the amount of desired recombinant protein and minimize the amount of glycosylated impurities. The processes can also be monitored for other undesired product-associated impurities, such as aggregates and nucleic acids. In exemplary embodiments, the recombinant proteins are multi-subunit proteins, such as antibodies, the host cell is a yeast, such as Pichia pastoris, and the glycosylated impurity is a glycovariant of the desired recombinant polypeptide, such as an N-linked and/or O-linked glycovariant.
    Type: Application
    Filed: March 17, 2014
    Publication date: September 25, 2014
    Applicant: ALDERBIO HOLDINGS LLC
    Inventors: Daniel S. ALLISON, Steven D. DAVIN, Hoa Binh DO, Leon F. GARCIA-MARTINEZ, Geoffrey F. LEE, Ethan W. OJALA, Mark YOUNG, John A. LATHAM
  • Publication number: 20140220633
    Abstract: The current invention reports a method for the purification of a not-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 c
    Type: Application
    Filed: April 7, 2014
    Publication date: August 7, 2014
    Applicant: HOFFMANN-LA ROCHE INC.
    Inventors: Roberto Falkenstein, Birgit Weydanz, Nicole Fuehrler, Claudia Giessel, Sybille Gabel, Adelbert Grossmann, Friederike Hesse, Marc Pompiati, Andreas Schaubmar, Brigitte Kraemer
  • Patent number: 8779110
    Abstract: The invention provides an efficient method of purification of a modified cytokine. The process includes the use of a chromatographic technique for the purification of the desired cytokine. The purified cytokine can be used as a therapeutic composition.
    Type: Grant
    Filed: June 23, 2009
    Date of Patent: July 15, 2014
    Assignees: Dr. Reddy's Laboratories Limited, Dr. Reddy's Laboratories, Inc.
    Inventors: Chaiti Roy, Darshan Koticha, Vivek Arthanari
  • Patent number: 8778653
    Abstract: A method for purification of viral compositions is provided. In particular, a method for reduction of unwanted residual DNA in a viral composition while retaining the immunogenicity of the virus itself is provided. The resulting immunogenic viral composition is substantially free of residual DNA, and is useful for the manufacture of medical products, such as vaccines designed for human or animal.
    Type: Grant
    Filed: August 12, 2010
    Date of Patent: July 15, 2014
    Assignee: Yisheng Biopharma Holdings Ltd.
    Inventors: Yi Zhang, Jinming Dai, Yajin Ni
  • Patent number: 8753897
    Abstract: Nanoporous materials can be used to enrich samples for subsequent analysis of substances contained in the sample. The method is shown to enrich the yield of species in the low molecular weight proteome, allowing detection of small peptides in the low nanomolar range.
    Type: Grant
    Filed: December 20, 2006
    Date of Patent: June 17, 2014
    Assignees: The Board of Regents of The University of Texas System, The Ohio State Research Foundation
    Inventors: Mauro Ferrari, Mark Ming-Cheng Cheng, Giovanni Cuda, Marco Gaspari, David Geho, Lance Liotta, Emmanuel Petricoin, Fredika Robertson, Rosa Terracciano
  • Publication number: 20140162248
    Abstract: The present disclosure relates to the use of aptamers in solid phase extraction, chromatography and chromatography-mass spectrometry systems. More specifically, the present disclosure relates to the use of aptamers in SPE and chromatography systems to selectively retain, extract and/or pre-concentrate target molecule(s) having a specific affinity for the particular aptamer(s). The target molecule(s) can be further analyzed by mass spectrometry with limited interferences and/or enhanced sensitivity.
    Type: Application
    Filed: December 10, 2013
    Publication date: June 12, 2014
    Applicant: Waters Technologies Corporation
    Inventors: Steven A. Cohen, Martin Gilar
  • Patent number: 8735122
    Abstract: Recombinant purified DnaK—having a ATPase activity without the addition of an other chaperone protein—essentially free of T-cell stimulating impurities.
    Type: Grant
    Filed: October 12, 2007
    Date of Patent: May 27, 2014
    Assignee: Biotech Tools S.A.
    Inventors: Frederic Henot, Thierry Legon, Sabine Pirotton, Gael Placier
  • Patent number: 8703123
    Abstract: Provided is a method of obtaining biologically active recombinant human G-CSF from inclusion bodies, wherein the solubilization and refolding process can be performed at ambient temperature and the purification step comprises reversed phase chromatography (RP), in particular RP-HPLC. The G-CSF preparation so obtained is characterized by high purity and homogeneity.
    Type: Grant
    Filed: March 17, 2011
    Date of Patent: April 22, 2014
    Assignee: BioGeneriX GmbH
    Inventors: Walter Hinderer, Christian Scheckermann
  • Patent number: 8697847
    Abstract: The present invention provides methods for purifying proteins. In particular, the methods employ a two-step non-affinity chromatography process without the use of an in-process tangential flow filtration step.
    Type: Grant
    Filed: March 2, 2012
    Date of Patent: April 15, 2014
    Assignee: Medarex, L.L.C.
    Inventors: Alahari Arunakumari, Gisela M. Ferreira
  • Patent number: 8685923
    Abstract: A method for inhibiting survival of cancer cells in a subject is disclosed. The method comprises administering to a subject in need thereof a therapeutically effective amount of fibrillar albumin. The preparation of the fibrillar albumin comprises: (i) forming a solution comprising an isolated and/or purified globular albumin; (ii) adding a detergent to the solution containing the isolated and/or purified globular albumin, wherein the detergent is one selected from the group consisting of sodium dodecyl sulfate (SDS) and n-tetradecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate; (iii) applying the solution to a molecular sizing column with a pore size that permits separation of a protein with a molecular weight of at least about 70 kDa so as to promote column-induced formation of the fibrillar albumin from the isolated and/or purified globular albumin; and (iv) eluting the fibrillar albumin from the column, wherein the eluted albumin has a fibrillar structure.
    Type: Grant
    Filed: August 12, 2012
    Date of Patent: April 1, 2014
    Assignee: Academia Sinica
    Inventors: Shu-Mei Liang, Chun-Yung Huang, Chi-Ming Liang
  • Patent number: 8685248
    Abstract: The present invention relates to a separation matrix comprised of a porous support to which ligands have been immobilized, wherein said ligands comprise at least one aliphatic sulphonamide. The nitrogen of the sulphonamide may be a secondary or tertiary amine. The invention also relates to a chromatography column that contains the described separation matrix, as well as to a method of isolating immunoglobulin-like compounds by adsorption to a separation matrix that comprises aliphatic sulphonamide ligands.
    Type: Grant
    Filed: February 22, 2010
    Date of Patent: April 1, 2014
    Assignee: GE Healthcare Bio-Sciences AB
    Inventors: Gunnar Glad, Bo-Lennart Johansson, Jean-Luc Maloisel, Nils Norrman
  • Patent number: 8670941
    Abstract: Provided herein are methods of diagnosing Alzheimer's disease (“AD”) based on characteristic changes of the levels of certain free amino acids or dipeptides (collectively termed as “AD diagnosis markers”) in the body fluid sample of an individual, carnosine synthesis activities in the plasma, and dopamine synthesis activities in the plasma. Also provided are methods of simultaneously determining the levels of at least two free amino acids or dipeptides in the biological fluid sample of an individual.
    Type: Grant
    Filed: August 17, 2007
    Date of Patent: March 11, 2014
    Assignee: Huntington Medical Research Institutes
    Inventors: Alfred N. Fonteh, Michael G. Harrington
  • Publication number: 20140065672
    Abstract: Provided is a separatome-based recombinant peptide, polypeptide, and protein expression and purification platform based on the juxtaposition of the binding properties of host cell genomic peptides, polypeptides, and proteins with the characteristics and location of the corresponding genes on the host cell chromosome, such as that of E. coli, yeast, Bacillus subtilis or other prokaryotes, insect cells, mammalian cells, etc. This platform quantitatively describes and identifies priority deletions, modifications, or inhibitions of certain gene products to increase chromatographic separation efficiency, defined as an increase in column capacity, column selectivity, or both, with emphasis on the former. Moreover, the platform provides a computerized knowledge tool that, given separatome data and a target recombinant peptide, polypeptide, or protein, intuitively suggests strategies leading to efficient product purification.
    Type: Application
    Filed: October 17, 2013
    Publication date: March 6, 2014
    Applicant: BOARD TRUSTEES OF THE UNIVERSITY OF ARKANSAS
    Inventors: Ellen M. Brune, Robert R. Beitle, JR., Mohammad M. Ataai, Patrick R. Bartlow, Ralph L. Henry
  • Patent number: 8658773
    Abstract: Disclosed are methods, compositions and uses of high concentration antibody or immunoglobulin formulations for subcutaneous, intramuscular, transdermal or other local (regional) administration, in a volume of than 3, less than 2 or less than 1 ml. Preferably, the formulation contains a high concentration formulation (HCF) buffer comprising phosphate, citrate, polysorbate 80 and mannitol at a pH of about 5.2. The formulation more preferably comprises at least 100, 150, 200, 250 mg/ml or 300 mg/ml of antibody. The methods for preparing the high concentration formulation include ultrafiltration and diafiltration to concentrate the antibody and exchange the medium for HCF buffer. Other embodiments concern use of non-G1m1 (nG1m1) allotype antibodies, such as G1m3 and/or a nG1m1,2 antibodies. The nG1m1 antibodies show decreased immunogenicity compared to G1m1 antibodies.
    Type: Grant
    Filed: May 1, 2012
    Date of Patent: February 25, 2014
    Assignee: Immunomedics, Inc.
    Inventors: Li Zeng, Rohini Mitra, Edmund A. Rossi, Hans J. Hansen, David M. Goldenberg
  • Patent number: 8653032
    Abstract: Disclosed is a pharmaceutical composition for preventing or treating TRPV1 activity-related or inflammation-related, diseases or conditions, containing a Maillard peptide separated from well-aged traditional soy sauce as an active ingredient. The Maillard peptide in the present invention functions both as a TRPV1 agonist and a TRPV1 antagonist, and further functions as a TRPV1 activity modulator. Therefore, the Maillard peptide can be used for preventing or treating TRPV1 activity-related diseases such as pain, neurological diseases, urgent defecation, inflammatory bowel disease, respiratory diseases, urinary incontinence, overactive bladder, neurogenic / allergic / inflammatory skin diseases, skin, eye or mucosal irritation, hyperacusis, tinnitus, vestibular hypersensitivity, heart disease, etc.
    Type: Grant
    Filed: November 8, 2010
    Date of Patent: February 18, 2014
    Assignees: Korea Food Research Institute, SNU R & DB Foundation
    Inventors: Mee-Ra Rhyu, Ah-Young Song, Eun-Young Kim, Seog Bae Oh, YoungJoo Lee, Won Chung Lim
  • Patent number: 8652330
    Abstract: The present invention relates to an asymmetric chromatography media suitable for separations applications, particularly as packed bed, fluidized bed or magnetized bed chromatography media. In certain embodiments, the asymmetric chromatography media comprises asymmetric particles, preferably beads, having at least two distinct, controlled pore size distributions. Preferably one of the distinct pore size distributions is in an internal region of the particle, and the other is in an external region or coating on the particle. These distinct pore size distributions can be modified with uniform or alternatively unique functional groups or mixtures of functional groups. The present invention allows for the control over pore size distribution within an asymmetric porous particle by providing a distinct internal region, preferably in the form of a bead, and a distinct external region, preferably in the form of a coating on the bead.
    Type: Grant
    Filed: March 2, 2010
    Date of Patent: February 18, 2014
    Assignee: EMD Millipore Corporation
    Inventors: Kwok-Shun Cheng, Senthilkumar Ramaswamy, Chen Wang, Nanying Bian, Brian Gagnon, Joaquin A. Umana, Dennis Aquino, Neil Soice, Andrew Lyddiatt
  • Patent number: 8653239
    Abstract: The present invention relates to a method for isolating and/or purifying at least one polypeptide from a polypeptide-containing sample, characterized in that the sample is contacted with a boron carbide support material at a pH which allows the binding of the polypeptide to the boron carbide support material. Such isolating can, for example, be used to remove polypeptides from a sample or else to purify and/or to concentrate polypeptides. A matrix comprising a boron carbide support material for purification of polypeptides is further disclosed according to the invention.
    Type: Grant
    Filed: April 9, 2009
    Date of Patent: February 18, 2014
    Assignee: Qiagen GmbH
    Inventor: Christian Feckler
  • Publication number: 20140046023
    Abstract: Sorbent comprising a solid support material, the surface of which comprises first residues comprising a binuclear heteroaromatic structure comprising besides carbon atoms at least one of the heteroatoms N, O, S, and second residues comprising a mononuclear heteroaromatic structure comprising besides carbon atoms at least one of the heteroatoms N, O, S.
    Type: Application
    Filed: July 28, 2010
    Publication date: February 13, 2014
    Applicant: INSTRACTION GMBH
    Inventors: Klaus Gottschall, Markus Arendt, Andres Kirschfeld, Christian Meyer, Markus Weis, Martin Welter, Lothar Ziser
  • Patent number: 8648178
    Abstract: The present invention relates to a method for purifying a protein belonging to the TGF-?, superfamily, preferably BMP, and more preferably BMP-2. According to the invention, the number of purification steps is reduced and the purification process is simplified, compared to the conventional BMP-2 purification method. Thus, the time required for purification can be shortened and the cost can be reduced. In addition, the invention solves the problem that as the time for purification increases and the number of purification steps increases, BMP-2 is degraded by protease or lost during purification steps, resulting in a decrease in the final yield of BMP-2. Thus, the invention increases the final yield of BMP-2.
    Type: Grant
    Filed: May 12, 2010
    Date of Patent: February 11, 2014
    Assignee: Korea Bone Bank Co., Ltd.
    Inventors: Young-Bock Shim, Yeong-Schick Kim, Yon-Rak Choi, Ju-Woong Jang
  • Patent number: 8642745
    Abstract: The invention relates to a method of preparing heteromultimeric polypeptides such as bispecific antibodies, bispecific immunoadhesins and antibody-immunoadhesin chimeras. The invention also relates to the heteromultimers prepared using the method. Generally, the method provides a multispecific antibody having a common light chain associated with each heteromeric polypeptide having an antibody binding domain. Additionally the method further involves introducing into the multispecific antibody a specific and complementary interaction at the interface of a first polypeptide and the interface of a second polypeptide, so as to promote heteromultimer formation and hinder homomultimer formation; and/or a free thiol-containing residue at the interface of a first polypeptide and a corresponding free thiol-containing residue in the interface of a second polypeptide, such that a non-naturally occurring disulfide bond is formed between the first and second polypeptide.
    Type: Grant
    Filed: December 8, 2006
    Date of Patent: February 4, 2014
    Assignee: Genentech, Inc.
    Inventors: W. Robert Arathoon, Paul J. Carter, Anne M. Merchant, Leonard G. Presta
  • Patent number: 8618268
    Abstract: The present invention provides the method of obtaining IgA and IgM antibodies from chicken egg whites. The method involves separating chicken egg whites into two fractions which contain IgA and IgM antibodies exclusively. This separation method consists of raising the volume of the egg whites using purified water, lowering the pH of said volume, filtering the IgM fraction from said volume, precipitating the IgA fraction from the remaining volume, dialyzing the IgA fraction and drying the IgA and IgM fractions.
    Type: Grant
    Filed: July 6, 2011
    Date of Patent: December 31, 2013
    Inventors: Hugh B. Fackrell, Linton W. Lee
  • Patent number: 8617531
    Abstract: Disclosed is a method for refolding a protein or peptide that does not contain essential disulfides and that contains at least one free cysteine residue. Also disclosed are polymer IFN-? conjugates that have been created by the chemical coupling of polymers such as polyethylene glycol moieties to IFN-?, particularly via a free cysteine in the protein. Also disclosed are analogs of bioactive peptides that may be used to create longer acting versions of the peptides, including analogs of glucagon, glucagon-like peptide-1 (GLP-1), GLP-2, Gastric inhibitory peptide (GIP), PYY, exendin, ghrelin, gastrin, amylin, and oxyntomodulin.
    Type: Grant
    Filed: December 14, 2007
    Date of Patent: December 31, 2013
    Assignee: Bolder Biotechnology, Inc.
    Inventors: George N. Cox, Mary S. Rosendahl
  • Publication number: 20130338344
    Abstract: The instant invention relates to the field of protein production and purification, and in particular to compositions and processes for controlling the amount of charge variants, aggregates, and fragments of a protein of interest, as well as host cell proteins, present in purified preparations by applying particular chromatography conditions during such protein purification.
    Type: Application
    Filed: March 14, 2013
    Publication date: December 19, 2013
    Applicant: ABBVIE INC.
    Inventors: Natarajan Ramasubramanyan, Lihua Yang, Matthew Omon Herigstad, Hong Yang
  • Patent number: 8604175
    Abstract: The invention relates to a method for purifying a glycoprotein, preferably FSH or a FSH mutant, comprising the steps of subjecting a liquid containing FSH or a FSH mutant to: (1) a dye affinity chromatography; (2) a weak anion exchange chromatography; (3) a hydrophobic interaction chromatography; and (4) a strong anion exchange chromatography; which may be carried out in any order.
    Type: Grant
    Filed: December 6, 2006
    Date of Patent: December 10, 2013
    Assignee: Ares Trading S.A.
    Inventors: Thierry Ziegler, Mara Rossi, Antonello Datola, Sabrina Fiumi
  • Patent number: 8597656
    Abstract: The present invention relates to a process for producing immunogenic polypeptides, comprising reducing disulfide bonds and blocking the resulting free thiol group with a blocking agent. The immunogenic peptides comprise a fragment of MAGE A3.
    Type: Grant
    Filed: December 13, 2011
    Date of Patent: December 3, 2013
    Assignee: GlaxoSmithKline Biologicals S.A.
    Inventors: Teresa Cabezon Silva, Joseph Cohen, Moncef Mohamed Slaoui, Carlota Vinals Bassols
  • Patent number: 8598319
    Abstract: The invention is related to a process for separating proteins fibrinogen, Factor XIII and biological glue from a solubilized plasma fraction and for preparing freeze-dried concentrates of said proteins comprising the steps of: chromatographic purification comprising the steps of loading an anion exchanger of weak base type with the said solubilized fraction, previously equilibrated with a buffer of a predetermined ionic strength of an alkaline pH, which allows to retain the biological glue, elution of the biological glue by increasing the ionic strength of the said buffer, and separation of FXIII from fibrinogen by addition to at least one part of the biological glue eluate of at least one chemical agent precipitating the FXIII, and recovery of the resulting purified fibrinogen containing supernatant solution, and diafiltration of the fibrinogen, biological glue and resolubilized FXIII solutions, followed by a freeze-drying of said solutions.
    Type: Grant
    Filed: June 28, 2006
    Date of Patent: December 3, 2013
    Assignee: Laboratoire Francais du Fractionnement et des Biotechnologies
    Inventors: Nogré Michel, Porte Pierre, Tellier Michel