Immunological Separation Or Affinity Chromatography Patents (Class 530/413)
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Publication number: 20120077285Abstract: The present invention relates to a method for purifying biomolecules or for analyzing whether an aqueous phase contains biomolecules by means of magnetic separation. The invention further relates to uses, to devices, and to kits that relate to the method according to the invention.Type: ApplicationFiled: March 25, 2010Publication date: March 29, 2012Inventor: Janina Cramer
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Patent number: 8133709Abstract: The invention is based on the discovery that certain biarsenical molecules react with specified target sequences, thereby providing a facile means for labeling polypeptides containing the target sequence. The invention is useful in creating stable mammalian cell lines expressing a certain tetracysteine tagged polypeptides, thereby overcoming toxicity associated with native tetracysteine. In addition, the invention allows for orthogonal labeling of polypeptides, thereby allowing for the observation of protein-protein interactions and conformational changes in proteins, for example.Type: GrantFiled: April 3, 2008Date of Patent: March 13, 2012Assignee: Life Technologies CorporationInventor: George Hanson
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Patent number: 8124364Abstract: A method for the conditioning of an extracorporeal device is described, as well as method for extracorporeal extraction of toxic material from mammalian body fluids in connection with diagnosis or treatment of a mammalian condition or disease, in which methods reagents having the ability to extract toxic material from mammalian body fluids are involved, and an extracorporeal device comprising said reagent.Type: GrantFiled: June 18, 2001Date of Patent: February 28, 2012Assignee: Glycorex Transplantation ABInventors: Bengt Sandberg, Scott Wilbur, Rune Nilsson
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Patent number: 8124743Abstract: The present invention discloses a method of purifying bivalent antibodies or antibody fragments that are active at both Fab sites from a source of antibodies or antibody fragments using a non-chromatographic method that includes inducing the formation of cyclic immunoglobulin aggregates by addition of multivalent hapten to a salt solution of soluble antibodies or antibody fragments, wherein the multivalent hapten possesses a linker between the two haptens effective to prevent the binding of both haptens of the ligand to the same antibody or antibody fragment.Type: GrantFiled: June 1, 2007Date of Patent: February 28, 2012Assignee: President and Fellows of Harvard CollegeInventors: Vijay M. Krishnamurthy, Lara A. Estroff, Vincent Semetey, Samuel W. Thomas, George K. Kaufman, Zihni Basar Bilgicer, George M. Whitesides
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Publication number: 20120046184Abstract: Provided herein is a method for the isolation or removal of a cellular component from a cell that comprises the steps of applying a pulse of nanoparticles to the cell, allowing the nanoparticles to traffic through the cell for a period of time sufficient to allow the nanoparticles locate to and interact with the cellular component to be isolated, and separation of the nanoparticles and isolated cellular component from the cell.Type: ApplicationFiled: February 26, 2010Publication date: February 23, 2012Applicant: UNIVERSITY COLLEGE DUBLIN, NATIONAL UNIVERSITY OF IRELAND, DUBLINInventors: Kenneth Dawson, Iseult Lynch, Martin Lundqvist, Tommy Cedervall
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Publication number: 20120029176Abstract: 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: ApplicationFiled: July 27, 2011Publication date: February 2, 2012Applicant: MILLIPORE CORPORATIONInventors: David Yavorsky, John Amara, Joaquin Umana, William Cataldo, Mikhail Kozlov, Matthew Stone
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Publication number: 20120018380Abstract: A chromatography column that captures components in a process liquid in a free flow state and allows elution in steps is described.Type: ApplicationFiled: September 27, 2011Publication date: January 26, 2012Applicant: Therapeutic Proteins Inc.Inventor: Sarfaraz K. Niazi
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Publication number: 20120022006Abstract: Binding polypeptides that specifically bind B lymphocyte stimulator protein or B lymphocyte stimulator-like polypeptides can be used in methods of the invention for detecting, diagnosing, or prognosing a disease or disorder associated with aberrant B lymphocyte stimulator or B lymphocyte stimulator receptor expression or inappropriate function of B lymphocyte stimulator or B lymphocyte stimulator receptor, comprising B lymphocyte stimulator binding polypeptides or fragments or variants thereof, that specifically bind to B lymphocyte stimulator.Type: ApplicationFiled: September 22, 2011Publication date: January 26, 2012Applicant: HUMAN GENOME SCIENCES, INC.Inventors: James P. Beltzer, M. Daniel Potter, Marilou Potter, Tony J. Fleming, Craig A. Rosen
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Publication number: 20120010390Abstract: The present invention relates to a process of enriching one target compound from a liquid, which process comprises at least one step of isolation performed by differentially partitioning between two aqueous phases. In the present invention the phases are formed by adding a thermally responsive, self-associating (i.e. clouding) hydrophilic polymer, and if needed some additional salts, to an aqueous biotechnical solution (such as a fermentation sample or bioseparation process stream) under thermal and other conditions where the solution separates into a one polymer, two-phase system with one phase enriched in the polymer. The target compound is to be found in the phase not enriched in the polymer, while a significant though varying percentage of contaminants may differentially partition to the phase interface or the polymer enriched phase.Type: ApplicationFiled: January 7, 2010Publication date: January 12, 2012Applicant: GE HEALTHCARE BIO-SCIENCES ABInventors: James Van Alstine, Jamil Shanagar, Rolf Hjorth, Martin Hall, Camilla Estmer Nilsson
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Publication number: 20120004179Abstract: The present invention relates to an antibody which specifically binds to unprocessed and/or partially processed neurotoxin polypeptide or an antibody which specifically binds an epitope consisting of a peptide having an amino acid sequence as shown in any one of SEQ ID NOs: 1 to 16 and to methods for the manufacture of such antibodies. Moreover, the present invention relates to a composition comprising processed neurotoxin polypeptide free of unprocessed or partially processed neurotoxin polypeptide and a method for manufacturing said neurotoxin polypeptide based on the antibodies of the invention. The present invention also relates to the use of the aforementioned antibody for separating processed neurotoxin polypeptides from unprocessed or partially processed neurotoxin polypeptides or for determining unprocessed or partially processed neurotoxin polypeptides. The present invention relates to a method for the manufacture of a medicament.Type: ApplicationFiled: February 17, 2010Publication date: January 5, 2012Applicant: MERZ PHARMA GmbH & CO. KGaAInventors: Michael Pfeil, Josef Friedrich, Harold Victor Taylor, Karl-Heinz Eisele, Cornelia Brunn
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Patent number: 8084580Abstract: The invention discloses a purified albumin solution of human origin with low prekallicrein activator (PKA) activity and stability over time characterized in that it has an antithrombin content equal to or greater than 0.03 mg/g of albumin, and a process for production thereof by the partial extraction of the antithrombin during fractionation of the human plasma.Type: GrantFiled: March 21, 2007Date of Patent: December 27, 2011Assignee: Grifols, S.A.Inventors: Juan Ignacio Jorquera Nieto, Nuria Hosta Mateu, Olga Santaeularia Lozano
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Patent number: 8084224Abstract: A method to facilitate recovery troponin I and/or troponin T from a sample comprising addition of troponin C to the sample or to a surface from which the troponin I and/or troponin T are recovered.Type: GrantFiled: April 5, 2010Date of Patent: December 27, 2011Assignee: Alere San Diego, Inc.Inventors: Kenneth F. Buechler, Paul H. McPherson
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Patent number: 8080555Abstract: Compounds useful in the treatment of autoimmune disease are described by the following general formula: n=0-2 m=0-2 m is not necessarily equal to n; where R1, R3?NH2, F, Cl, C1-C4 alkoxy or phenoxy group, but R1 is not necessarily equal to R3; and R2?H, F, Cl, NH2, or NH—R—XH;Type: GrantFiled: May 15, 2006Date of Patent: December 20, 2011Assignee: Prometic Biosciences Inc.Inventors: Boulos Zacharie, Daniel Fortin, Nicole Wilb, Christopher Penney
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Publication number: 20110306068Abstract: The present invention relates to bacteriophage tail proteins and the derivatives and fragments thereof that are capable of binding endotoxins in the absence of bivalent positive ions, especially Ca2+ or Mg2+. Further, the present invention relates to methods for depleting endotoxins from solutions and samples using the bacteriophage tail proteins according to the present invention and to a detection method for endotoxins.Type: ApplicationFiled: July 12, 2011Publication date: December 15, 2011Applicant: HYGLOS INVEST GMBHInventors: Stefan Miller, Roman Meyer, Renate Grassl, Manfred Biebl, Holger Grallert
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Publication number: 20110301333Abstract: The present invention provides novel and improved compositions containing calcium phosphate and methods of using the same for the removal of protein aggregates from biopharmaceutical compositions containing a product of interest, e.g., a therapeutic antibody or protein.Type: ApplicationFiled: May 10, 2011Publication date: December 8, 2011Applicant: Millipore CorporationInventors: Ajish Potty, Alex Xenopolous
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Publication number: 20110301342Abstract: 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: ApplicationFiled: April 13, 2011Publication date: December 8, 2011Applicant: ABBOTT LABORATORIES, INC.Inventors: Chen Wang, Robert K. Hickman, Edwin O. Lundell, Roy D. Hegedus
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Patent number: 8058014Abstract: The present invention is directed to methods of diagnosing a disease or predicting an increased risk of a disease, such as obesity, obesity-dependent subacute inflammation, atherosclerosis, cardiovascular disease and a metabolic disease, by determining the levels of omentin 1 and 2 protein in a subject, or by determining the levels of omentin 1 and 2 gene expression in a subject. The present invention is also directed to methods of disease treatment using omentin 1 protein and omentin 2 protein.Type: GrantFiled: September 29, 2007Date of Patent: November 15, 2011Assignee: University of Maryland, BaltimoreInventors: Da-Wei Gong, John C. McLenithan, Alan R. Shuldiner, Rong-Ze Yang
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Patent number: 8058410Abstract: Disclosed is an affinity matrix comprising a solid phase and an affinity ligand comprising peptide bonds coupled to this solid phase, wherein the affinity ligand comprising peptide bond is selected from the following group of ligands: a) peptides comprising the formula X1X2X3X4, wherein X1 to X4 are amino acid residues and at least two of X1 to X4 is W, Y or F; b) peptides comprising the formula X5X6X7X8, wherein X5 to X8 are amino acid residues, at least one of X5 to X8 is W, and at least one of X5 to X8 is E or D; and c) poly-amino acids consisting of an amino acid monomer of the group consisting of R, K, E and D and an amino acid monomer of the group consisting of Y, F and W, preferably poly-KY, poly-KF, poly-KW, poly-RY, poly-RF, poly-RW, poly-EY, poly-DY, poly-EF, poly-EW, poly-DF and poly-DW, with the proviso that the peptides according to a) and b) have a maximum length of 35 amino acid residues and that the poly-amino acids according to c) have a minimum length of 20 amino acid residues.Type: GrantFiled: April 25, 2006Date of Patent: November 15, 2011Assignees: Sandoz AG, Boehringer Ingelheim RCV GmbH & Co KGInventors: Alois Jungbauer, Rainer Hahn, Waltraud Kaar, Michael Seifert, Bernhard Auer, Clemens Achmüller, Philipp Wechner
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Patent number: 8058017Abstract: Provided herein are methods and compositions for purifying human factor VIII, human factor VIII-like peptide or fragments thereof. The methods comprise immobilizing a binding molecule for human factor VIII, human factor VIII-like protein or fragments thereof to a solid support, contacting the immobilized binding molecule with a solution containing the human factor VIII, human factor VIII-like protein or fragments thereof, and purifying the factor by separating the solution from the solid support.Type: GrantFiled: January 22, 2010Date of Patent: November 15, 2011Assignee: Dyax Corp.Inventors: Jinan Yu, M. Daniel Potter, Marilous Potter, legal representative, Brian D. Kelley, Jeffrey S. Deetz, James E. Booth
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Patent number: 8053565Abstract: In an affinity-type purification, ligands dissociated from a packed bed that would otherwise leach into the solution containing the species being purified are captured by a second ligand that resides in a porous barrier downstream from the packed bed, the second ligand exhibiting an affinity-type interaction with the dissociated first ligand with sufficient specificity to avoid the undesired retention by the second ligand of species from the liquid sample or source liquid other than the species sought to be purified in the affinity column.Type: GrantFiled: May 28, 2009Date of Patent: November 8, 2011Assignee: Bio-Rad Laboratories, Inc.Inventor: Mark A. Snyder
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Patent number: 8034785Abstract: The present invention provides a peptide which selectively adsorbs an anti-?1 adrenoreceptor antibody being one of the contributing factors in dilated cardiomyopathy. The peptide of the invention can be immobilized on a carrier in a short period of time with rarely inducing side reactions, and adsorbent for adsorbing an anti-?1 adrenoreceptor antibody can be produced with good efficiency by using the peptide. In addition, the present invention provides an adsorbent comprising such peptide immobilized on a carrier, an adsorber wherein such adsorbent is used, and a method for adsorbing an anti-?1 adrenoreceptor antibody. The adsorbent and adsorber according to the invention can efficiently deprive an anti-?1 adrenoreceptor antibody-containing liquid, in particular body fluid, of the antibody.Type: GrantFiled: October 26, 2005Date of Patent: October 11, 2011Assignee: Kaneka CorporationInventors: Kazumasa Ohara, Eiji Ogino, Sakiko Hanita, Takehiro Nishimoto
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Patent number: 8017740Abstract: This invention relates to the use of mixed mode chromatography for purification of at least one intact non-aggregated antibody from a mixture containing intact non-aggregated antibodies and undesirable materials, including fragmented or aggregated antibodies, host cell proteins, DNA, endotoxin, and/or virus. This invention further relates to the integration of such a method into a multi-step procedure with other fractionation methods for purification of antibodies suitable for in vivo applications.Type: GrantFiled: February 19, 2010Date of Patent: September 13, 2011Assignee: Bio-Rad Laboratories, Inc.Inventor: Peter S. Gagnon
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Publication number: 20110217752Abstract: Ligand functionalized substrates, methods of making ligand functionalized substrates, and methods of using functionalized substrates are disclosed.Type: ApplicationFiled: February 14, 2011Publication date: September 8, 2011Inventors: 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
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Publication number: 20110212509Abstract: A device and method are provided for facilitating extraction of a fraction from a biological sample. The biological sample includes non-desired material and a fraction-bound solid phase substrate. The device includes an input zone for receiving the biological sample therein and a phase-gate zone for receiving an isolation buffer therein. An output zone receives a reagent therein. A force is movable between a first position adjacent the input zone and a second position adjacent the output zone. The force urges the fraction-bound solid phase substrate from the input zone, through the phase-gate zone and into the output zone.Type: ApplicationFiled: February 23, 2011Publication date: September 1, 2011Inventors: David J. Beebe, Scott M. Berry, Richard Burgess, Lindsay Strotman
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Patent number: 8003768Abstract: A system and method for providing 20% ethanol solutions meeting bioburden and endotoxin specifications, which provides the 20% ethanol solution in a ready-to-use form which may be dispensed directly from the container in which the solution is shipped, and which may be used in connection with storage, reuse and/or rejuvination of Protein A.Type: GrantFiled: July 5, 2006Date of Patent: August 23, 2011Assignee: Decon Labs, Inc.Inventor: Tim Gordon
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Patent number: 7998960Abstract: For the separation, removal, isolation, purification, characterization, identification or quantification of plasminogen or a protein that is a plasminogen 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; A is a support matrix, optionally linked to the triazine ring by a spacer; Z is O, S or N—R and R is H, C1-6 alkyl, C1-6 hydroxyalkyl, benzyl or &bgr;-phenylethyl; B is an optionally substituted hydrocarbon linkage containing from 1 to 10 carbon atoms; D is H, OH or a primary amino, secondary amino, tertiary amino, quaternary ammonium, imidazole, guanidino or amidino group; or B-D is —CHCOOH—(CH2)3-4—NH2; and q is 2 to 6.Type: GrantFiled: May 9, 2006Date of Patent: August 16, 2011Assignee: Prometic Biosciences Ltd.Inventors: Jason Richard Betley, James Christopher Pearson, Claudia Hildegard Kuhn, Baldev Singh Baines
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Patent number: 7985846Abstract: A process for preparing a hemostatically active preparation containing von Willebrand factor (vWF) from a fraction of human plasma by chromatographic purification of a vWF-containing plasma fraction on an anion-exchange material which has the anion-exchanging groups on grafted polymeric structures (tentacle materials), collecting a vWF-containing fraction, followed by purification of said fraction using gel permeation to prepare a purified thermally stable vWF-containing preparation; and heating the preparation for inactivating viruses.Type: GrantFiled: January 4, 2007Date of Patent: July 26, 2011Assignee: Octapharma AGInventors: Djuro Josic, Monika Stadler, Gerhard Gruber
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Publication number: 20110171220Abstract: One aspect of the present disclosure provides antibodies that can act as agonists of PD-1, thereby modulating immune responses regulated by PD-1. Another aspect of the disclosure provides compositions comprising PD-1 specific antibodies and their use in methods of down regulating the immune response. These methods can be practiced on any subject, including humans or animals. Anti-PD-1 antibodies disclosed herein may be used, in another aspect of the invention, to detect PD-1 or its fragments in a biological sample. The amount of PD-1 detected may be correlated with the expression level of PD-1, and associated with the activation status of immune cells (e.g., activated T cells, B cells, and/or monocytes) in the subject.Type: ApplicationFiled: September 14, 2009Publication date: July 14, 2011Applicant: Isis Innovation LimitedInventor: Simon Davis
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Publication number: 20110150911Abstract: Immunogenic compositions for use in treating, preventing and diagnosing infection caused by the California (CAL) serotype of the genus Bunyavirus, such as La Crosse virus (LACV), are disclosed. Also described are reagents for use in diagnostic assays.Type: ApplicationFiled: November 19, 2004Publication date: June 23, 2011Inventors: Qui-Lim Choo, Michael Houghton, Elizabeth Scott, Amy Weiner
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Patent number: 7947813Abstract: Methods are presented for isolating and purifying proteins by adding a polyelectrolyte to a cell culture fluid, such as a harvested cell culture fluid, and precipitating a protein-polyelectrolyte complex or a complex of impurities and the polyelectrolyte.Type: GrantFiled: January 10, 2008Date of Patent: May 24, 2011Assignee: Genentech, Inc.Inventors: Robert L. Fahrner, Jayme Franklin, Paul McDonald, Thanmaya Peram, Vikram Sisodiya, Corazon Victa
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Publication number: 20110118452Abstract: The invention provides, inter alia, methods, devices and reagents for the preparation of native and non-denatured biomolecules using solid-phase extraction channels. The invention is particularly suited for the purification, concentration and/or analysis of protein analytes. The invention further provides, inter alia, methods, devices and reagents for the purification, concentration and/or analysis of multi-protein complexes.Type: ApplicationFiled: January 6, 2011Publication date: May 19, 2011Inventors: Douglas T. Gjerde, Christopher P. Hanna
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Patent number: 7943046Abstract: Embodiments of the present invention provide a method of chromatographic delipidation comprising separating a lipid-containing sample on a superficially porous stationary phase at greater than about 70° C., at least about 80° C., having at least one mobile phase comprising an ion-pairing agent in water, an ion-pairing agent in an organic modifier, an acid in an organic modifier, and an alcohol. The invention provides minimal protein losses and high run-to-run reproducibility. The on-column delipidation method aventageously utilize reversed phase liquid chromatography.Type: GrantFiled: June 22, 2006Date of Patent: May 17, 2011Assignee: Agilent Technologies, IncInventors: James D. Martosella, Nina I. Zolotarjova
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Patent number: 7939643Abstract: This invention relates to a process for the production of a von Willebrand factor preparation, hydroxylapatite being used as a chromatography medium.Type: GrantFiled: September 9, 2005Date of Patent: May 10, 2011Assignee: Biotest AGInventors: Michael Kretschmar, Wolfgang Moeller
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Publication number: 20110105736Abstract: A novel separating agent for protein purification which not only can adsorb proteins in a sufficient amount for protein purification from a low concentration buffer but also can desorb the adsorbed protein easily just by altering the pH of the buffer and a simple and economical method for its production and a method for protein purification using it. One or two ligands selected from the group consisting of a ligand represented by the following formula (1): (wherein m is an integer of from 2 to 6) and a ligand represented by the following formula (2): (wherein each of R1 and R2 is independently a hydrogen atom or a C1-4 alkyl group, and n is an integer of from 1 to 6) are immobilized on a support via a urethane bond without intervention of a spacer arm.Type: ApplicationFiled: June 22, 2009Publication date: May 5, 2011Applicant: TOSOH CORPORATIONInventors: Seiji Masumoto, Katsuo Komiya, Koji Nakamura
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Publication number: 20110105730Abstract: The invention provides methods of coupling protein ligands to a solid support. The invention also provides affinity chromatography matrices and methods of using affinity chromatography matrices to purify a target molecule.Type: ApplicationFiled: November 1, 2010Publication date: May 5, 2011Applicant: Millipore CorporationInventors: Nanying Bian, John Charkoudian, Neil Soice, Joaquin Umana, Chen Wang
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Publication number: 20110097715Abstract: A method for purifying or detecting a target protein present in a solution, includes, before carrying out the actual detection or purification step, a step of contacting the solution with an aptamer binding specifically to the target protein, where the aptamer does not bind to a protein homologous to the target protein that could also be present in the solution.Type: ApplicationFiled: August 13, 2008Publication date: April 28, 2011Applicant: LFB - BIOTECHNOLOGIESInventors: Laurent Siret, Abdessatar Chtourou, Frédéric Dhanaut, Gérald Perret
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Patent number: 7919582Abstract: The invention relates, inter alia, to the use of neuregulin-? as a target in a screening method for active compounds, in particular for exerting an influence on changes in calcium concentration which are mediated by glutamate receptors. The invention furthermore relates to the use of neuregulins, preferably a neuregulin isoform having an isoelectric point in the range from pH 4.3 to 5.0, as a target for detecting and/or exerting an influence on neuronal processes, in particular for exerting an influence on long-term memory. Neuregulins, in particular neuregulin-.beta. and also substances which exert an influence on the status, i.e. the expression and/or post -translational modification, of neuregulin-.beta., can therefore be used as agents for controlling the course of, treating and/or alleviating neuronal diseases, e.g. Alzheimer's disease.Type: GrantFiled: April 16, 2009Date of Patent: April 5, 2011Assignee: Mind-Ngr SAInventor: Andre Schrattenholz
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Patent number: 7919597Abstract: A cell extract for cell-free protein synthesis is produced by removing substances, which bind to an affinity support to be used in purification or interaction analysis, from a cell extract having protein synthetic activity. Then, a target protein is synthesized by using the cell extract for cell-free protein synthesis. The synthesized target protein can be purified by using the affinity support and used in interaction analysis.Type: GrantFiled: July 30, 2010Date of Patent: April 5, 2011Assignee: Cellfree Sciences Co., Ltd.Inventors: Yoshiko Yoshiyama, Hirohisa Koga
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Publication number: 20110065901Abstract: 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: ApplicationFiled: August 5, 2010Publication date: March 17, 2011Applicant: MILLIPORE CORPORATIONInventors: Neil Soice, John Dana Hubbard, Yu Zhang, James Hamzik
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Patent number: 7901670Abstract: Provided is a process for purifying human interferon beta from a recombinant human interferon beta-containing culture comprising performing affinity chromatography and cation exchange chromatography, wherein the affinity chromatography includes: adsorbing the interferon beta-containing culture to an equilibrated affinity chromatography column, followed by washing with an equilibration buffer solution; washing the column with a washing buffer solution A of pH 6.5-7.5 containing 30-60 wt % of propylene glycol and a washing buffer solution B of pH 6.5-7.5 containing 10-30 wt % of propylene glycol and 1-2M NaCl; and eluting a human interferon beta-containing fraction with a buffer solution of pH 6.5-7.5 containing 40-60 wt % of propylene glycol and 1-2M NaCl.Type: GrantFiled: December 4, 2004Date of Patent: March 8, 2011Assignee: CJ Cheiljedang CorporationInventors: Ji Sook Park, Jong Sang Chung, Min Ji Baek, Jee Won Ahn, Ki Wan Kim, Hyung Ki Park, Dong Eok Lee, Myung Suk Oh
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Publication number: 20110039331Abstract: The present invention provides a tag peptide comprising an amino acid sequence represented by the following formula (I): X1-Tyr-X2-Gly-Gln-X3??(I) (wherein X1, X2 and X3 are the same or different and each represent any amino acid residue) and an antibody against the tag peptide. By combined use of the tag peptide and antibody of the present invention, a system that enables proteins expressed from cloned genes to be highly purified in an inexpensive and easy manner can be established.Type: ApplicationFiled: December 18, 2008Publication date: February 17, 2011Inventor: Junichi Takagi
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Publication number: 20110034678Abstract: The present invention provides large-scale methods for renaturation of proteins comprising adding a solution of denatured, chemically modified or reduced proteins to a refolding buffer containing sulfate derived from H2SO4 and/or MgSO4 in the presence of guanidine. The present invention further provides methods of isolating a refolded protein at a concentration of about 0.4 to 3.0 gm/L by using a hydrophobic interaction chromatography (HIC) column.Type: ApplicationFiled: March 12, 2010Publication date: February 10, 2011Applicant: AEROVANCE, INC.Inventors: Wayne Froland, Katherine Delaria, David Boisvert, Robert Kuhn
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Publication number: 20110034672Abstract: 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 cType: ApplicationFiled: January 15, 2009Publication date: February 10, 2011Inventors: Roberto Falkenstein, Birgit Weydanz, Nicole Fuehrler, Claudia Giessel, Sybille Greithanner, Adelbert Grossmann, Friederike Hesse, Marc Pompiati, Andreas Schaubmar, Brigitte Kraemer
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Publication number: 20110008900Abstract: This invention relates to methods of analysis, and in particular to methods for the preliminary fractionation of samples in which low abundance molecules of interest, for example proteins, polysaccharides or fatty acids, are present together with more abundant molecules of little or no interest. In particular, the invention relates to methods of depletion of high abundance proteins from biological samples. Products and kits for use in the method are also disclosed, and form part of the invention. In one aspect, the invention provides a method of depleting a high-abundance molecule from a biological sample, comprising the steps of a) subjecting the sample to affinity depletion using an affinity support with high affinity for a high abundance molecule, and/or b) immunodepletion using an affinity support coupled to an antibody directed against whole or previously fractionated plasma or serum.Type: ApplicationFiled: June 11, 2010Publication date: January 13, 2011Applicant: HEALTHLINX LIMITEDInventors: Gregory E. Rice, Mark S. Baker, Michael Quinn
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Publication number: 20110009604Abstract: The present invention relates to a method for concentrating and/or purifying prion PrPSc proteins by contacting prion PrPSc proteins with sepharose under conditions that allow for the specific and high affinity binding of the sepharose to the prion PrPSc proteins and removing the unbound non-prion proteins from the sepharose, as well as the same method for removing prion PrPSc proteins from body fluids by contacting body fluids with sepharose under conditions that allow for the specific and high affinity binding of the sepharose to the prion PrPSc proteins and removing the body fluid from said sepharose.Type: ApplicationFiled: October 25, 2006Publication date: January 13, 2011Applicant: Alicon AGInventors: Ralph Zahn, Ahmed El Gedaily, Susanne Franitza, Nicola Franscini, Ulrich Matthey
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Publication number: 20110009598Abstract: A cell extract for cell-free protein synthesis is produced by removing substances, which bind to an affinity support to be used in purification or interaction analysis, from a cell extract having protein synthetic activity. Then, a target protein is synthesized by using the cell extract for cell-free protein synthesis. The synthesized target protein can be purified by using the affinity support and used in interaction analysis.Type: ApplicationFiled: July 30, 2010Publication date: January 13, 2011Inventors: Yoshiko Yoshiyama, Hirohisa Koga
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Publication number: 20110003379Abstract: A chimeric polypeptide comprising an autoprocessing segment having an amino acid sequence being capable of auto-cleavage, a polynucleotide encoding such a polypeptide, and uses of such a polypeptide and such a polynucleotide are provided. a polynucleotide are provided.Type: ApplicationFiled: July 26, 2010Publication date: January 6, 2011Applicant: Yeda Research And Development Co. Ltd.Inventors: Shmuel PIETROKOVSKI, Gil Amitai
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Publication number: 20100331526Abstract: Methods of purifying proteins expressed in non-mammalian expression systems in a non-native soluble form directly from cell lysate are disclosed. Methods of purifying proteins expressed in non-mammalian expression systems in a non-native limited solubility form directly from a refold solution are also disclosed. Resin regeneration methods are also provided.Type: ApplicationFiled: June 24, 2010Publication date: December 30, 2010Applicant: AMGEN INC.Inventors: Joseph Edward Shultz, Roger Hart
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Publication number: 20100331530Abstract: Method for purifying therapeutic proteins by multi-stage extractive distillation.Type: ApplicationFiled: February 25, 2009Publication date: December 30, 2010Applicant: BAYER TECHNOLOGY SERVICES GMBHInventors: Werner Bäcker, Sven Sommerfeld, Martina Mutter, Paula Alexandra Albuquerque De Jesus Rosa, Maria Raquel Murias Dos Santos Aires-Barosl, Ana Margarida Nunes Da Mata Pires De Azevedo
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Publication number: 20100310462Abstract: A method for separation of an aggregated misfolded protein from an environment including a non-aggregating normal form of the protein includes contacting both the misfolded and normal protein with a conjugated polyelectrolyte (CPE) and separating the CPE/protein complex from the other constituents of the sample.Type: ApplicationFiled: June 3, 2010Publication date: December 9, 2010Inventors: Peter Åsberg, Olle Inganäs, Fredrik Anghus