Proteinase Patents (Class 435/219)
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Publication number: 20120183993Abstract: The invention relates to a process for the preparation of a fermentation product from ligno-cellulosic material, comprising the following steps: a) optionally pre-treatment b) optionally washing; c) enzymatic hydrolysis; d) fermentation; and e) optionally recovery of a fermentation product; wherein in step c) an enzyme composition is used that has a temperature optimum of 55 degrees C. or more, the hydrolysis time is 40 hours or more and the temperature is 50 degrees C. or more.Type: ApplicationFiled: October 5, 2010Publication date: July 19, 2012Applicant: DSM IP ASSETS B.V.Inventors: Johannes Petrus Smits, Elisabeth Maria Gierveld, Fop Cornelis Van Der Hor
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Publication number: 20120183525Abstract: A horsefly protease tabfiblysin isolated from the salivary gland of the horsefly, Tabanus Yao, a gene encoding the protease and use thereof are disclosed by the present invention. It belongs to the technical field of biomedicine. The molecular weight of the horsefly protease tabfiblysin is 27145.5 Daltons. Its full-length sequence is composed of 255 amino acids. Its encoding sequence is composed of 768 nucleotides. The horsefly protease tabfiblysin can hydrolyze fibrinogen and inhibit the aggregation of blood platelet dramatically, and can be used for preparing the drug for treating thrombotic diseases.Type: ApplicationFiled: June 14, 2010Publication date: July 19, 2012Inventors: Ren Lai, Dongying Ma
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Publication number: 20120183995Abstract: The present invention provides cells that have been genetically manipulated to have an altered capacity to produce expressed proteins. In particular, the present invention relates to Gram-positive microorganisms, such as Bacillus species having enhanced expression of a protein of interest, wherein one or more chromosomal genes have been inactivated, and preferably wherein one or more chromosomal genes have been deleted from the Bacillus chromosome. In some further embodiments, one or more indigenous chromosomal regions have been deleted from a corresponding wild-type Bacillus host chromosome.Type: ApplicationFiled: January 23, 2012Publication date: July 19, 2012Applicant: Danisco US Inc.Inventors: Eugenio Ferrari, Carole Harbison, M. Harunur Rashid, Walter Weyler
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Publication number: 20120172244Abstract: Genetic biomarkers for left side colon cancer (LCC) (such as expression levels of an RNA transcript or expression product of NOX4, MMP3, or a combination) and right side colon cancer (RCC) (such as expression levels of an RNA transcript or expression product of CDCX2, FAM69A, or a combination), are disclosed. Methods for using the biomarkers in providing a prognosis of relapse-free survival probability in patients having LCC or RCC are also presented. Prognostic panels using gene expression values of the biomarkers are also presented. Computer implemented methods employing the biomarkers, and as well as for determining relapse-free survival probability in a patient having RCC or LCC are provided. A genetic method for classifying a colon cancer tissue as a RCC or as a LCC is also disclosed.Type: ApplicationFiled: December 20, 2011Publication date: July 5, 2012Inventors: Steven Buechler, Amanda Hummon
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Publication number: 20120171711Abstract: The present invention relates to a method for the detection of essentially intact encapsulated or non-encapsulated parasites in meat, comprising the maceration of the meat with an alkaline digestion solution which contains a digestive enzyme that is active in an alkaline environment. Further, uses of a serine endopeptidase in a method for the detection of essentially intact encapsulated or non-encapsulated parasites in meat are described. The present invention also describes serine endopeptidases for use in a diagnostic method for the detection of essentially intact encapsulated or non-encapsulated parasites in meat. Finally, a kit is disclosed which comprises the enzymes and alkaline digestion solutions of the present invention.Type: ApplicationFiled: June 21, 2010Publication date: July 5, 2012Inventor: Philipp Bauer
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Patent number: 8211485Abstract: The present invention relates to the use of a solution containing at least one endopeptidase to substantially reduce or completely eliminate allergenic proteins contained in the peanut (Arachis hypogea). In particular, the direct application of a solution containing at least one endopeptidase to either raw, blanched, or roasted peanuts or peanut products or derivates, has been shown to substantially reduce or completely eliminate the activity of allergenic proteins. The treated peanuts showed no degradation in quality or sensory acceptability, and have the flavor and aroma of natural whole peanuts. Hypoallergenic or non-allergenic peanuts produced in accordance with the present invention may be used as ingredients in various food products and other edible materials.Type: GrantFiled: June 6, 2007Date of Patent: July 3, 2012Assignee: North Carolina A&T State UniversityInventors: Mohamed Ahmedna, Jianmei Yu, Ipek Goktepe
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Patent number: 8206968Abstract: The present invention provides a mutant 27 kDa NIa proteinase having reduced self-cleavage activity relative to the self-cleavage activity of its wild-type proteinase. The mutant has the same substrate cleavage activity as the wild-type proteinase but is more stable than the wild-type proteinase. The present invention also provides a method of obtaining large quantities of active 27 kDa NIa proteinase for use as a tool for purification of other proteins.Type: GrantFiled: August 1, 2008Date of Patent: June 26, 2012Assignee: Yale UniversityInventors: Jennifer A. Doudna, Louise J. Lucast, Robert T. Batey
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CHEMICALLY MODIFIED MUTANT SERINE HYDROLASES SHOW IMPROVED CATALYTIC ACTIVITY AND CHIRAL SELECTIVITY
Publication number: 20120156721Abstract: This invention provides novel chemically modified mutant serine hydrolases that catalyze a transamidation and/or a transpeptidation and/or a transesterification reaction. The modified serine hydrolases have one or more amino acid residues in a subsite replaced with a cysteine, wherein the cysteine is modified by replacing the thiol hydrogen in the cysteine with a substituent group providing a thiol side chain comprising a moiety selected from the group consisting of a polar aromatic substituent, an alkyl amino group with a positive charge, and a glycoside. In particularly preferred embodiments, the substitutents include an oxazolidinone, a C1 to C15 alkyl amino group with a positive charge, or a glycoside.Type: ApplicationFiled: February 24, 2012Publication date: June 21, 2012Applicant: The Governing Council of the University of TorontoInventors: John Bryan Jones, Michael Dickman, Richard C. Lloyd -
Publication number: 20120148599Abstract: The invention provides antibodies to specific neural proteins and methods of using the same.Type: ApplicationFiled: November 9, 2011Publication date: June 14, 2012Inventors: Jasvinder Atwal, Yongmei Chen, Cecilia Pui Chi Chiu, Robert A. Lazarus, Weiru Wang, Ryan J. Watts, Yan Wu, Yingnan Zhang
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Publication number: 20120149624Abstract: The present invention relates to novel subtilase variants exhibiting alterations relative to the parent subtilase in one or more properties including: Wash performance, thermal stability, storage stability or catalytic activity. The variants of the invention are suitable for use in e.g. cleaning or detergent compositions, such as laundry detergent compositions and dish wash compositions, including automatic dish wash compositions.Type: ApplicationFiled: December 20, 2010Publication date: June 14, 2012Applicant: Novozymes A/SInventors: Henriette Draborg, Peter Kamp Hansen, Mads Eskelund Bjornvad, Mads Norregaard-Madsen, Mikael Mikkelsen
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Publication number: 20120149880Abstract: The invention provides a nucleic acid cassette comprising components in the following structure: A-B-C, wherein “A” is a nucleic acid sequence encoding a light chain of a first antibody (or antigen binding domain thereof), “B” is a nucleic acid sequence encoding a 2A peptide, “C” is a nucleic acid sequence encoding a heavy chain of a second antibody (or antigen binding domain thereof), and “-” is a phosphodiester or phosphorothioate bond. Also provided is a nucleic acid cassette with the structure A-p-B-C, where “p” is a nucleic acid encoding a protease recognition site, Also provided are methods for making recombinant antibodies using the nucleic acid cassette of the invention, cells and vector comprising the nucleic acid cassette of the invention, and kits for making the nucleic acid cassette of the invention.Type: ApplicationFiled: August 20, 2010Publication date: June 14, 2012Applicant: CELL SIGNALING TECHNOLOGY, INC.Inventors: Wan Cheung Cheung, Shuji Sato, Roberto Polakiewicz
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Publication number: 20120149088Abstract: Methods of directly isolating nucleic acid from an embedded biological sample are provided. An emulsified digest is generated in the presence of a thermostable protease, and an additive selected from an alkylene glycol, a poly(alkylene glycol), or a block copolymer having an average Mn of 76 to 2900, or a salt or derivative or combination thereof. Nucleic acid is isolated directly from the emulsified digest. The methods eliminate the use of organic solvents such as xylene in a deparaffinization step prior to isolating nucleic acids from paraffin-embedded samples, for example.Type: ApplicationFiled: November 30, 2011Publication date: June 14, 2012Applicant: LIFE TECHNOLOGIES CORPORATIONInventors: Richard CONRAD, Marie Gonzalez, Emily Zeringer
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Publication number: 20120144504Abstract: The invention relates to the treatment or prevention of an inflammatory skin disease, disorder or condition, by modulating a protein that is normally regulated by caspase-8 in the skin or by increasing caspase-8 activity or level in the skin. Another aspect of the invention relates to methods for diagnosing an inflammatory skin disease, disorder or condition or a predisposition to develop said disease disorder or condition in an individual. Further aspects of the invention relate to methods for identifying target proteins involved in the course or pathology of an inflammatory skin disease, disorder or condition and to methods of screening a candidate compound for treating said disease, disorder or condition. In particular, the invention relates to inflammatory skin diseases such as atopic dermatitis and psoriasis.Type: ApplicationFiled: October 16, 2006Publication date: June 7, 2012Applicant: Yeda Research and Development Co. Ltd.Inventors: David Wallach, Andrei Kovalenko, Tae-Bong Kang, Jin Chul Kim
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Publication number: 20120128652Abstract: The present invention relates to a polypeptide with an amino acid sequence according to SEQ ID NO:1. The present invention further relates to the nucleic acid molecules comprising a nucleotide sequence coding for the polypeptide, vectors comprising the nucleic acid molecules, and host cells for the expression of the polypeptides. In addition, the present invention relates to the use of the polypeptide as a human medical, veterinary medical or diagnostic substance, as an antimicrobial substance in food, in cosmetics, as disinfecting agent or in the environmental field.Type: ApplicationFiled: September 12, 2011Publication date: May 24, 2012Inventors: Martin LOESSNER, Mathias SCHMELCHER
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Patent number: 8182808Abstract: Polynucleotides and polypeptides relating to a recombinantly modified plasmin(ogen) molecule are provided. The plasmin(ogen) molecule has a single kringle domain N-terminal to the activation site present in the native human plasminogen molecule, combined such that no foreign sequences are present, and exhibits lysine-binding and significant enzymatic characteristics associated with the native enzyme.Type: GrantFiled: November 22, 2011Date of Patent: May 22, 2012Assignee: Grifols Therapeutics Inc.Inventor: Valery Novokhatny
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Publication number: 20120122110Abstract: The present invention relates to a method and kit for the isolation of cells from a sample. The sample is treated with an extraction solution that comprises at least MgCl2 and/or an ionic liquid resulting in the isolation of preferably viable cells.Type: ApplicationFiled: May 31, 2010Publication date: May 17, 2012Applicant: MERCK PATENT GESELLSCHAFT MIT BESDCHRANKTER HAFTUNGInventors: Peter Rossmanith, Patrick Julian Mester, Martin Wagner
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Publication number: 20120114629Abstract: Polypeptide agents useful in the treatment of IgA1 deposition diseases and methods of using such polypeptide agents. Methods of screening for inhibitors of IgA1 proteases and agents that inhibit IgA1 proteases are also disclosed.Type: ApplicationFiled: April 20, 2010Publication date: May 10, 2012Applicant: TUFTS MEDICAL CENTER, INC.Inventors: Todd Holyoak, Jiazhou Qiu, Andrew G. Plaut
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Publication number: 20120114771Abstract: The present invention provides an enhancer for enhancing the activity of oxidized protein hydrolase. The oxidized protein hydrolase activity enhancer according to the present invention contains an extract of at least one plant selected from the group consisting of Compositae Anthemis, Saururaceae Houttuynia, Rosaceae Crataegus, and Vitaceae Vitis.Type: ApplicationFiled: June 29, 2010Publication date: May 10, 2012Applicant: ARKRAY Inc.Inventors: Masayuki Yagi, Tomoko Takahashi
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Publication number: 20120115186Abstract: The present invention relates to a process for the production of one or more fermentation product from a sugar composition, comprising the following steps: a) fermentation of the sugar composition in the presence of a yeast belonging to the genera Saccharomyces, Kluyveromyces, Candida, Pichia, Schizosaccharomyces, Hansenula, Kloeckera, Schwanniomyces or Yarrowia, and b) recovery of the fermentation product, wherein the yeast comprises the genes araA, araB and araD and the sugar composition comprises glucose, galactose and arabinose.Type: ApplicationFiled: July 6, 2010Publication date: May 10, 2012Applicant: DSM IP ASSETS B.V.Inventors: Paul Klaassen, Gijsberdina Pieternella Van Suylekom, Bianca Elisabeth Maria Gielesen, Nicolette Jasmijn Broers, Beate Wiedemann, Wilhelmus Theodorus Antonius Maria De Laat
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Publication number: 20120115204Abstract: The present invention relates to a novel method for improving the viral safety of liquid Factor VII compositions, in particular those comprising active Factor VII polypeptides (a Factor VIIa polypeptide).Type: ApplicationFiled: January 13, 2012Publication date: May 10, 2012Applicant: Novo Nordisk Healthcare A/GInventors: Jesper Christensen, Erik Halkjaer, Turid Preuss, Thomas Budde Hansen, Lene Vaedele Madsen Tomoda, Nina Johansen
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Publication number: 20120115153Abstract: The present invention relates to a marker for the prognosis of liver cancer; a composition for estimating the prognosis of liver cancer, which contains a substance for detecting a change in the expression level of the prognostic marker for liver cancer; a kit for estimating the prognosis of liver cancer, which contains the composition for estimating liver cancer prognosis; a method for estimating the prognosis of liver cancer using the marker for liver cancer prognosis; and a method for screening a therapeutic agent for liver cancer using the marker for the prognosis of liver cancer.Type: ApplicationFiled: April 16, 2010Publication date: May 10, 2012Applicants: CBS BIOSCIENCE, CO., LTD.Inventors: Jin young Park, Seok joo Hong, Jong Min Kim
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Publication number: 20120108513Abstract: The present invention relates to a method for the purification of divalent cation binding proteins with high purity on an anion exchange resin material, to divalent cation binding proteins obtainable by said method, and to a kit comprising means for carrying out said method.Type: ApplicationFiled: April 29, 2011Publication date: May 3, 2012Applicants: Baxter Healthcare S.A., Baxter International Inc.Inventors: Artur Mitterer, Meinhard Hasslacher, Christian Fiedler
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Publication number: 20120107869Abstract: 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 comprising 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 said steps are conducted on one affinity chromatography system.Type: ApplicationFiled: January 11, 2012Publication date: May 3, 2012Applicants: BOEHRINGER INGELHEIM RCV GmbH & Co KG, SANDOZ AGInventors: Alois JUNGBAUER, Rainer Hahn, Anne Tscheliessnig, Waltraud Karr
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Publication number: 20120107847Abstract: We describe a method to determine effectiveness of a compound or composition in treatment of celiac disease or gluten intolerance, the method comprising: administration of the compound or composition to one or more human patients who were on a gluten-free diet for 10 years or less, preferably 6 years or less; challenge with gluten of the one or more human patients who were administered the compound or composition; and determining whether there is a change in condition of celiac disease or gluten intolerance of the one or more patients that results from administration of the compound or composition and challenge with gluten; whereby no significant change in condition indicates that the compound or composition would be effective in treating celiac disease or gluten intolerance.Type: ApplicationFiled: June 24, 2010Publication date: May 3, 2012Applicant: DSM IP ASSETS B.V.Inventors: Maaike Johanna Bruins, Luppo Edens
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Publication number: 20120107342Abstract: Described is an ex vivo animal or challenge model used as a method to identify protective (e.g., recombinant) proteins and rapidly measure protective immunity in intestinal segments directed against parasites and vaccines directed against parasitic infections. Further described are vaccines directed against infection with parasites, such as Fasciola hepatica, which vaccines contain protective (recombinant) proteins identified and shown to be protective in studies using the ex vivo model. Further described are protective (e.g., recombinant) proteins obtained from newly excysted juveniles (NEJ) of F. hepatica. The protective (recombinant) protein corresponding to an NEJ protein has an apparent molecular weight of 32 kD and an N-terminal amino acid molecule comprising the sequence XXDVSWPFWDRMYNY (SEQ ID NO:1).Type: ApplicationFiled: November 14, 2011Publication date: May 3, 2012Inventors: Florine Johanna van Milligen, Johannes Bernardus Wilhelmus Joseph Cornelissen, Bernard Adri Bokhout
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Patent number: 8168159Abstract: The present invention discloses a method for the enzyme-mediated, site-specific, in-vivo precipitation of a water soluble molecule in an animal. The enzyme is either unique to tumor cells, or is produced within a specific site (e.g., tumor) at concentrations that are higher than that in normal tissues. Alternatively, the enzyme is conjugated to a targeting moiety such as an antibody or a receptor-binding molecule.Type: GrantFiled: April 3, 2009Date of Patent: May 1, 2012Assignee: President and Fellows of Harvard CollegeInventors: Amin I. Kassis, Ravi S. Harapanhalli
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Publication number: 20120093788Abstract: We have identified by molecular cloning a protease which originates from the larvae of Lucilia sericata and which was termed debrilase due to its activities useful for debridement of wounds.Type: ApplicationFiled: March 3, 2010Publication date: April 19, 2012Applicant: B.R.A.I.N. Biotechnology Research and Information Network AGInventors: Frank Niehaus, Jürgen Eck, Renate Schulze, Michael Krohn
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Publication number: 20120087908Abstract: The invention relates to a stable pharmaceutical composition in liquid form or in solid form, comprising factor VII, said composition being free of mannitol and of sucrose, or even also of any antioxidant.Type: ApplicationFiled: June 18, 2010Publication date: April 12, 2012Applicant: LFB-BIOTECHNOLOGIESInventors: Annie Bardat, Cornelius Pompe
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Patent number: 8148105Abstract: Methods are provided for the production of gram to kilogram quantities of pro-EP-B2 (proenzyme form of EP-B2) in a lyophilized form. The methods include scalable fermentation, refolding and purification processes, which processes may be combined with lyophilization to yield a stable product.Type: GrantFiled: March 14, 2008Date of Patent: April 3, 2012Assignees: The Board of Trustees of the Leland Stanford Junior University, Alvine Pharmaceuticals, Inc.Inventors: Harmit Vora, James McIntire, Pawan Kumar, Chaitan Khosla
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Publication number: 20120065106Abstract: Methods for enhancing expression levels, secretion, and purification of heterologous fusion proteins in a host cell are disclosed.Type: ApplicationFiled: December 28, 2007Publication date: March 15, 2012Applicant: LIFESENSORS, INC.Inventors: Tauseef R. Butt, Tadas Panavas, Amolkumar Karwa, Raymond J. Peroutka, Jeffrey G. Marblestone
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Publication number: 20120064059Abstract: A single chain, polypeptide fusion protein, comprising: a non-cytotoxic protease, or a fragment thereof, which protease or protease fragment is capable of cleaving a protein of the exocytic fusion apparatus of a nociceptive sensory afferent; a Targeting Moiety that is capable of binding to a Binding Site on the nociceptive sensory afferent, which Binding Site is capable of undergoing endocytosis to be incorporated into an endosome within the nociceptive sensory afferent; a protease cleavage site at which site the fusion protein is cleavable by a protease, wherein the protease cleavage site is located between the non-cytotoxic protease or fragment thereof and the Targeting Moiety; a translocation domain that is capable of translocating the protease or protease fragment from within an endosome, across the endosomal membrane and into the cytosol of the nociceptive sensory afferent. Nucleic acids encoding the fusion proteins, methods of preparing same and uses thereof are also described.Type: ApplicationFiled: September 22, 2011Publication date: March 15, 2012Applicants: ALLERGAN, INC., SYNTAXIN LTD.Inventors: Keith FOSTER, John CHADDOCK, Philip MARKS, Patrick STANCOMBE, Kei Roger AOKI, Joseph FRANCIS, Lance STEWARD
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Publication number: 20120058928Abstract: An alkaline protease variant derived from an alkaline protease consisting of an amino acid sequence represented by SEQ ID NO: 2 or consisting of an amino acid sequence having an identity of 90% or more therewith, which variant has mutations wherein one or more amino acid residues at positions selected from (a) position 6, (b) position 15, (c) position 16, (d) position 65, (e) position 66, (f) position 82, (g) position 83, (h) position 204, (i) position 319, and (j) position 337 of the amino acid sequence represented by SEQ ID NO: 2, or at positions corresponding thereto are substituted with the following amino acid residues: (a) or a position corresponding thereto: Typ, Leu, Val, Ile, Met, Tyr, Gln, Lys, Thr, Phe, Arg, Ser, Cys, Ala, or His; (b) or a position corresponding thereto: Glu, Met, Asp, Val, Gln, Arg, Cys, Trp, Ala, or Phe; (c) or a position corresponding thereto: Met, Glu, Arg, Val, Lys, Phe, Tyr, Ile, His, Asp, or Cys; (d) or a position corresponding thereto: Trp; (e) or a position corresponding tType: ApplicationFiled: April 26, 2010Publication date: March 8, 2012Applicant: Kao CorporationInventors: Masatoshi Tohata, Mitsuyoshi Okuda, Tsuyoshi Sato, Keiji Endo, Katsuhisa Saeki
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Publication number: 20120058103Abstract: The invention relates to bioengineering, in particular to producing a composition of individual enzymes exhibiting the extended range of proteolytic activity, thereby enabling the composition to hydrolyse protein substrates up to individual amino acids.Type: ApplicationFiled: June 18, 2009Publication date: March 8, 2012Applicant: JOINT-STOCK COMPANY 'HIGH TECH'Inventor: Olga A. KLIMOVA
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Publication number: 20120058537Abstract: The various embodiments herein provide a chimeric truncated and mutant variant of a tissue plasminogen activator (t-pa) and a method for preparing the same. According to an embodiment herein, the mutant variant comprises a signal sequence domain, followed by a chimeric tetrapeptide, followed by a tripeptide, followed by a kringle 2 domain, followed by a serine protease domain and a substituted amino acids at position 128-131. The substituted amino acids are AAAA (SEQ ID NO: 3) amino acids. The chimeric tetrapeptide is Gly-His-Arg-Pro (SEQ ID NO: 1). The chimeric tetrapeptide is at a position of 36 to 39 amino acid of the mutant variant. The tripeptide is Ser-Tyr-Glu. According to an embodiment herein, a chimeric truncated and mutant variant of a tissue plasminogen activator comprises a native t-pa deleted with Finger domain, a Growth Factor domain and a Kringle 1 domain, a chimeric tetrapeptide and a substituted amino acids at a position of 128-131.Type: ApplicationFiled: July 27, 2011Publication date: March 8, 2012Applicants: PASTEUR INSTITUTE OF IRAN (IPI), No. 69Inventors: Fereidoun Mahboudi, Fatemeh Davami, Soroush Sardari
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Publication number: 20120052550Abstract: The present invention relates to a method for isolating proteins from a solution containing the proteins. The invention also relates to a method for the chromatographic separation of proteins. The present invention also relates to crosslinked hydroxylic polymer particles functionalized with temperature-responsive copolymer, and to methods of preparing such particles.Type: ApplicationFiled: September 22, 2009Publication date: March 1, 2012Inventors: Brad William Woonton, Milton Thomas William Hearn, Pankaj Maharjan, Kirthi De Silva, William Roy Jackson
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Patent number: 8124372Abstract: The present invention relates to a process for the amidation of C-terminal esters or acids of peptide substrates in solution-phase synthesis of peptides, comprising amidating one or more peptide substrates comprising C-terminal esters or acids using the protease subtilisin in any suitable form in the presence of an ammonium salt derived from an acid having a pKa above 0. This process is useful in the production of protected or unprotected peptides.Type: GrantFiled: June 24, 2008Date of Patent: February 28, 2012Assignee: N.V. OrganonInventors: Ivo Franci Eggen, Carmen Gabriela Boeriu
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Patent number: 8124074Abstract: The invention provides a single chain, polypeptide fusion protein, comprising: a non-cytotoxic protease, or a fragment thereof, which protease or protease fragment is capable of cleaving a protein of the exocytic fusion apparatus of a target cell; a Targeting Moiety that is capable of binding to a Binding Site on the target cell, which Binding Site is capable of undergoing endocytosis to be incorporated into an endocome within the target cell; a protease cleaving site at which site the fusion protein is cleavable by the protease, wherein the protease cleavage site is located between the non-cytotoxic protease or fragment thereof and the Targeting Moiety; and the translocation domain that is capable of translocating the protease or protease fragment from within an endosome, across the endosomal membrane and into the cytosol of the target cell.Type: GrantFiled: December 1, 2005Date of Patent: February 28, 2012Assignee: Syntaxin LimitedInventors: Keith Alan Foster, John Chaddock, Philip Marks, Patrick Stancombe, Lyndsey Durose
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Publication number: 20120046329Abstract: Disclosed herein are compositions and methods relating to modulators of Nod-like Receptors NOD1 (NLRC1) and NOD2 (NLRC2) signaling. Further provided are methods of identifying modulators of Nod-like Receptors NOD1 and NOD2 activity. Further provided are compositions and methods for treating or preventing inflammation, including diseases associated with inflammation such as inflammatory bowel diseases (Crohn's disease, ulcerative colitis), pancreatitis, arthritis, asthma, psoriasis. Alzheimer's disease, cardiovascular disease (arteritis), diabetes, and sepsis.Type: ApplicationFiled: August 10, 2011Publication date: February 23, 2012Inventors: Gregory Paul Roth, Ricardo Garcia Correa, Pasha Moeenuddin Khan, John Christian Reed
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Patent number: 8119171Abstract: The invention relates to a method for the prevention or reduction of haze in a beverage by the addition of an prolyl-specific endoprotease and to new beverages obtainable by the method according to the invention. It also relates to new endoproteases. Sequence information of a genomic DNA, cDNA as well as protein sequences.Type: GrantFiled: December 6, 2001Date of Patent: February 21, 2012Assignee: DSM IP Assets B.V.Inventors: Michel Lopez, Luppo Edens
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Patent number: 8119124Abstract: The present invention relates to a debriding composition obtained from bromelain and to methods of producing same. Particularly, the present invention relates to a debriding composition obtained from bromelain comprising proteolytic enzymes having molecular weights of about 23 kDa, being essentially devoid of bromelain inhibitors, and to pharmaceutical compositions comprising same. The debriding compositions and the pharmaceutical compositions comprising same are particularly useful in debriding eschar tissues and in wound healing.Type: GrantFiled: November 22, 2005Date of Patent: February 21, 2012Assignee: MediWound Ltd.Inventors: Marian Gorecki, Amir Toren
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Patent number: 8119597Abstract: The invention concerns the use and the production of non-neurotoxic plasminogen activating factors, derived, for example, from the common vampire Desmodus rotundus (DSPA), for therapeutic treatment of stroke in humans. The invention provides a novel therapeutic base for treating stroke in humans.Type: GrantFiled: August 22, 2008Date of Patent: February 21, 2012Assignee: Paion GmbHInventors: Mariola Sohngen, Wolfgang Sohngen, Wolf-Dieter Schleuning, Robert Medcalf
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Publication number: 20120040436Abstract: The present invention provides an improved type protease which comprises an amino acid sequence that is at least 75% identical to SEQ ID NO:3, said improved type protease has at least one mutation selected from the group consisting of: (A) replacement of glutamine corresponding to glutamine at position 265 in SEQ ID NO: 3 with an acidic amino acid; and (B) replacement of glutamine at position 266 in SEQ ID NO: 3 with an acidic amino acid, and wherein said improved type protease has milk-clotting activity.Type: ApplicationFiled: March 19, 2010Publication date: February 16, 2012Applicant: Meito Sangyo Co., Ltd.Inventors: Kazunori Harada, Hiroyuki Kobayashi, Taro Suga, Hiroyuki Yamaguchi, Akira Tsunoda, Shigeaki Kato
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Publication number: 20120039863Abstract: A Factor X (hereinafter referred to as “FX”) with a high activity is provided. The present invention relates to a method for efficiently preparing a recombinant, two-chain FX which comprises intervening glycosylation at such an amino acid sequence that is essential for glycosylation in FX to thereby allow for expression of a recombinant FX with no glycosylation, and the recombinant FX with no glycosylation obtained by said method.Type: ApplicationFiled: September 16, 2011Publication date: February 16, 2012Applicant: JURIDICAL FDN THE CHEMO-SERO-THERAPEUTIC RES INSTInventors: Kenji SOEJIMA, Takayuki Imamura, Ryoichi Kawamura, Hiroshi Nakatake, Arisa Maeyashiki, Hitomi Togo
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Patent number: 8114656Abstract: The present invention provides methods and compositions comprising at least one neutral metalloprotease enzyme that has improved storage stability. In some embodiments, the neutral metalloprotease finds use in cleaning and other applications. In some particularly preferred embodiments, the present invention provides methods and compositions comprising neutral metalloprotease(s) obtained from Bacillus sp. In some more particularly preferred embodiments, the neutral metalloprotease is obtained from B. amyloliquefaciens. In still further preferred embodiments, the neutral metalloprotease is a variant of the B. amyloliquefaciens neutral metalloprotease. In yet additional embodiments, the neutral metalloprotease is a homolog of the B. amyloliquefaciens neutral metalloprotease. The present invention finds particular use in applications including, but not limited to cleaning, bleaching and disinfecting.Type: GrantFiled: May 28, 2009Date of Patent: February 14, 2012Assignee: Danisco US Inc.Inventors: Andrew Shaw, Louise Wallace, David A. Estell, Ronaldus W. J. Hommes, Sang-Kyu Lee, Hiroshi Oh, Eugene S. Sadlowski
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Patent number: 8105804Abstract: The present invention provides novel polynucleotides encoding PCSK9b and PCSK9c polypeptides, fragments and homologues thereof. Also provided are vectors, host cells, antibodies, and recombinant and synthetic methods for producing said polypeptides. The invention further relates to diagnostic and therapeutic methods for applying these novel PCSK9b and PCSK9c polypeptides to the diagnosis, treatment, and/or prevention of various diseases and/or disorders related to these polypeptides. The invention further relates to screening methods for identifying agonists and antagonists of the polynucleotides and polypeptides of the present invention.Type: GrantFiled: October 13, 2010Date of Patent: January 31, 2012Assignee: Bristol-Myers Squibb CompanyInventors: Gabriel A. Mintier, Jian Chen, John N. Feder, Bowman Miao, Rex Arnold Parker
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Patent number: 8101394Abstract: Polynucleotides and polypeptides relating to a recombinantly-modified plasmin(ogen) molecule are provided. The plasmin(ogen) molecule has a single kringle domain N-terminal to the activation site present in the native human plasminogen molecule, combined such that no foreign sequences are present, and exhibits lysine-binding and significant enzymatic characteristics associated with the native enzyme.Type: GrantFiled: November 25, 2008Date of Patent: January 24, 2012Assignee: Grifols Therapeutics Inc.Inventor: Valery Novokhatny
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Publication number: 20120009187Abstract: The invention relates to nucleic acids encoding a novel Vespula venom protease or fragments thereof, in particular the protease Ves v 4, recombinant vectors comprising such nucleic acids, and host cells containing the recombinant vectors. The invention is further directed to the expression of such nucleic acids to produce a recombinant Vespula venom protease, or recombinant fragments thereof, or synthetic peptides thereof. Such a protease or fragments thereof or synthetic peptides thereof are useful for diagnosis of insect venom allergy and for therapeutic treatment of insect venom allergy.Type: ApplicationFiled: March 3, 2010Publication date: January 12, 2012Applicant: PLS-DESIGN GMBHInventors: Henning Seismann, Ingke Braren, Thomas Grunwald
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Patent number: 8093035Abstract: A Pseudomonas sp. strain TKU015 is deposited under DSMZ GmbH (Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH) Number DSM 21747). The Pseudomonas sp. strain TKU015 can be used to produce chitinase, chitosanase and nattokinase. A method of producing chitinase, chitosanase and nattokinases can use the Pseudomonas sp. strain TKU015.Type: GrantFiled: November 18, 2008Date of Patent: January 10, 2012Assignee: Tamkang UniversityInventors: San-Lang Wang, Hsin-Jen Chen
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Publication number: 20120003187Abstract: A method for preserving a preparation of insulin-secreting cells includes the step of placing the preparation of insulin-secreting cells in contact with a biological medium, the biological medium including a nutritive product including albumin, and further includes a peptone or a mixture of peptones in sufficient quantity to preserve the insulin-secreting cells.Type: ApplicationFiled: May 5, 2011Publication date: January 5, 2012Applicants: MACO PHARMA, UNIVERSITE DU DROIT ET DE LA SANTE DE LILLE 2, CENTRE HOSPITALIER REGIONAL UNIVERSITAIRE DE LILLEInventors: Julie Kerr-Conte, Bruno Delorme
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Publication number: 20120003717Abstract: The invention provides novel biologically pure cultures of microorganisms high in protease activity and capable of decomposing proteins recalcitrant to proteolysis as contained in garbage, waste water, organic waste liquids, industrial wastes and the like, a protease produced by such microorganisms and capable of decomposing proteins recalcitrant to proteolysis, and a method of utilizing the same. The novel culture is of a soil-derived microorganism belonging to Streptomyces sp., or a strain derived therefrom, which produces a protease capable of efficiently decomposing proteins recalcitrant to proteolysis as contained in waste water, organic waste liquids, industrial wastes and so forth.Type: ApplicationFiled: August 9, 2011Publication date: January 5, 2012Applicant: MICROBIAL CHEMISTRY RESEARCH FOUNDATIONInventors: Hiroyasu DOI, Naoko KINOSHITA, Tatsuzo OKA, Zhao HUI