Oxygen Containing Reactant Patents (Class 530/410)
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Patent number: 11951162Abstract: The present invention provides an immunogenic composition comprising a Streptococcus pneumoniae polysaccharide-protein conjugate, comprising a capsular polysaccharide derived from one or more selected from the group consisting of serotypes 1, 2, 3, 4, 5, 6A, 6B, 7F, 8, 9N, 9V, 10A, 11A, 12F, 14, 15B, 17F, 18C, 19A, 19F, 20, 22F, 23F, and 33F, derived from Streptococcus pneumoniae; and one or 2 or more of carrier proteins conjugated to the respective capsular polysaccharide, and method of preparation thereof. Through one example of the present invention, an immunogenic composition for preventing or treating pneumococcal infection can be provided.Type: GrantFiled: April 18, 2019Date of Patent: April 9, 2024Assignee: SK BIOSCIENCE CO., LTD.Inventors: Hun Kim, Dong Soo Ham, Jin-Hwan Shin, Kyung-jun An, Sung-hyun Kim
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Patent number: 11821009Abstract: Modified AAV vectors and uses thereof are provided.Type: GrantFiled: May 14, 2019Date of Patent: November 21, 2023Assignee: Cornell UniversityInventors: Ronald G. Crystal, Katie Stiles
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Patent number: 11433004Abstract: The present invention relates to a dental composition comprising (i) an acidic polymerizable compound of the following formula (Ia), (Ib) or (Ic): wherein X, Y, Y?, Z, L, R2, R3 and R4 are as defined in claim 1; and (ii) an initiator system. Furthermore, the present invention relates to the use of the polymerizable compound of formula (I) for the preparation of a dental composition.Type: GrantFiled: May 19, 2017Date of Patent: September 6, 2022Assignee: DENTSPLY SIRONA INC.Inventors: Christoph Fik, Sven Pohle, Joachim E. Klee, Marina Barudzija, Magnus Schmidt, Markus Ringwald
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Publication number: 20150024430Abstract: The disclosure relates to milk protein nanoparticles produced according to a polymerization method in which at least one protein, which is obtained from milk and which can be thermally plasticized, is plasticized using a plasticizing agent, such as for example, water or glycerol at temperatures between room temperature and 140° C., subjected to mechanical stress and subsequently retreated, for example, in the top down or bottom up method to form nanoparticles.Type: ApplicationFiled: November 12, 2012Publication date: January 22, 2015Inventor: Anke Domaske
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Publication number: 20140378670Abstract: The invention relates to the field of covalently attaching proteins to a substrate, particularly to methods of immobilizing proteins by posttranslationally modifying a cysteine residue of said protein through the addition of functional groups. The invention also relates to biological molecules used in such techniques, including proteins, and detection methods and kits that utilize such immobilized proteins, such as a microdevice or “protein chip”, a high-throughput screening device, and for the microscopy of proteins on a surface.Type: ApplicationFiled: December 23, 2013Publication date: December 25, 2014Inventors: Charles Dale Poulter, Guillermo Roberto Labadi, Cecile Gauchet, Rochelle Frances Hawkins Bohaty
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Patent number: 8911776Abstract: The present invention relates to novel therapies for treatment of new and existing type 1 and type 2 diabetes, PreDiabetes, Latent Autoimmune Diabetes of Adulthood, and diseases of insulin deficiency, beta cell deficiency, insulin resistance and impaired glucose metabolism. In particular, the present invention identifies common peptides within the human Reg1a, Reg1b, Reg3a and Reg4, as signaling peptides for beta cell generation acting through the human Reg Receptor on the surface of human pancreatic extra-islet tissue.Type: GrantFiled: October 26, 2012Date of Patent: December 16, 2014Inventor: Claresa Levetan
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Publication number: 20140329290Abstract: The present invention allows formation of covalent bonds in a bioactive compound having at least one amino group so as to efficiently provide the compound modified with PEG. The present invention thus provides a functionalized polyethylene glycol having a structure that allows reaction of two aldehyde groups with one amino group to form two covalent bonds.Type: ApplicationFiled: December 13, 2012Publication date: November 6, 2014Inventors: Yukio Nagasaki, Yutaka Ikeda, Hiromichi Kawasaki, Jinya Katamachi
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Patent number: 8865188Abstract: Provided herein are methods and compositions for controlling assembly of modified viral core proteins, for example, into a viral capsid or a nanocage. In some embodiments, the disclosed modified viral core proteins comprise at least one mutation or modification that can substantially prevent assembly of the viral core proteins until assembly is desired. In some embodiments, assembly of the viral core proteins may be triggered, for example, by contacting the viral core proteins with a reducing agent and/or by reducing the concentration of a denaturant. The viral core proteins may self-assemble to form a viral capsid or nanocage.Type: GrantFiled: September 10, 2012Date of Patent: October 21, 2014Assignee: Biomed Realty, L.P.Inventors: Miguel de los Rios, Stephanie de los Rios, Jacek Ostrowski, Kenneth J. Oh, Ilan Zipkin
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Publication number: 20140309175Abstract: Polymer conjugates containing a C1-inhibitor having at least one substantially non-antigenic polymer covalently attached to the C1-inhibitor via thiol group of the C1 inhibitor is provided. In the polymer conjugates of the present invention, the substantially non-antigenic polymer is attached to either free thiol from a cysteine of thiol generated from disulfide bonds in C1 inhibitor. Alternatively, the substantially non-antigenic polymer is attached to one of more thiols in C1 inhibitor via bifunctional spacer. In addition, methods of making the conjugates as well as methods of treatment using the conjugate of the present invention are also provided.Type: ApplicationFiled: March 15, 2013Publication date: October 16, 2014Inventors: Hong Zhao, Karen Yang
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Patent number: 8859294Abstract: The object of the present invention is to provide a method for immobilizing the SpA protein on the surface of a substrate with high density without causing dimerization. The following method solves the object. That is, the method for binding a protein to a surface of a substrate, comprising steps (A) to (B): step (A) of preparing said protein to the surface, step (B) of supplying said protein to the surface, wherein said protein consists of a Protein A or at least one domain of A to E of said Protein A, and said protein comprises C-terminal modified amino acid sequence represented by SEQ ID:1(SFNRSEC).Type: GrantFiled: March 29, 2011Date of Patent: October 14, 2014Assignee: Panasonic CorporationInventors: Jin Muraoka, Takachika Azuma, Akikazu Murakami
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Publication number: 20140296181Abstract: Described herein, at least in part, are methods of modulating oncogenic fusion proteins.Type: ApplicationFiled: April 9, 2012Publication date: October 2, 2014Applicant: Coferon, Inc.Inventors: Lee Daniel Arnold, Kenneth W. Foreman
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Publication number: 20140294877Abstract: The present invention is directed to an inventive polymeric carrier molecule according to generic formula (I) and variations thereof, which allows for efficient transfection of nucleic acids into cells in vivo and in vitro, a polymeric carrier cargo complex formed by a nucleic acid and the inventive polymeric carrier molecule, but also to methods of preparation of this inventive polymeric carrier molecule and of the inventive polymeric carrier cargo complex. The present invention also provides methods of application and use of this inventive polymeric carrier molecule and the inventive polymeric carrier cargo complex as a medicament, for the treatment of various diseases, and in the preparation of a pharmaceutical composition for the treatment of such diseases.Type: ApplicationFiled: March 4, 2014Publication date: October 2, 2014Applicant: CUREVAC GMBHInventors: Patrick BAUMHOF, Thomas SCHLAKE
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Patent number: 8809274Abstract: Disclosed is an adhesive hemostatic agent based on non-blood constituents including DOPA, able to strongly adhere to collagen fibers, and which comprises an antifibrinolytic agent in addition to an esterified atelocollagen which is non-immunogenic and may become positively charged thereon such that the adhesive hemostatic agent has no possibility of mediating particular diseases or viral infections (HIV, HCV, HBV, CMV, etc), unlike conventional agents comprising blood constituents, and readily binds to negatively charged platelets at high adhesive strength, thus inducing quick blood coagulation. Also, provided is a method for preparing the same.Type: GrantFiled: September 21, 2011Date of Patent: August 19, 2014Assignees: Dalim Biotech Co., Ltd., Industry-Academic Cooperation Foundation, Yongsei-UniversityInventor: Hwal Suh
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Patent number: 8809453Abstract: The present invention is directed to branched reactive water-soluble polymers comprising at least two polymer arms, such as poly(ethylene glycol), attached to a central aliphatic hydrocarbon core molecule through heteroatom linkages. The branched polymers bear at least one functional group for reacting with a biologically active agent to form a biologically active conjugate. The functional group of the branched polymer can be directly attached to the aliphatic hydrocarbon core or via an intervening linkage, such as a heteroatom, -alkylene-, —O-alkylene-O—, -alkylene-O-alkylene-, -aryl-O—, —O-aryl-, (—O-alkylene-)m, or (-alkylene-O—)m linkage, wherein m is 1-10.Type: GrantFiled: April 18, 2013Date of Patent: August 19, 2014Assignee: Nektar TherapeuticsInventors: Michael David Bentley, Xuan Zhao, Xiaoming Shen, William Dudley Battle, III
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Publication number: 20140220633Abstract: 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: April 7, 2014Publication date: August 7, 2014Applicant: 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
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Patent number: 8791092Abstract: This invention provides novel compositions to inhibit the aggregation of amyloid proteins. In various embodiments the compositions comprise a molecular tweezers that binds lysine and/or arginine and thereby inhibits the aggregation of amyloidogenic proteins.Type: GrantFiled: March 5, 2010Date of Patent: July 29, 2014Assignees: The Regents of the University of California, The United States of America as represented by the Department of Veterans Affairs, Massachusetts Institute of Technology, Universitat Duisburg-EssenInventors: Gal Bitan, Akila Shanmugam, Aleksey Lomakin, Thomas Schrader, Frank Gerrit Klarner, Peter Talbiersky, Jolanta Polkowska, Frank Bastkowski, Sharmistha Sinha, Sally Frautschy
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Coenzyme Q10 nanoparticles, preparation method thereof and composition containing said nanoparticles
Patent number: 8785598Abstract: Provided are a coenzyme Q10 nanoparticle, a method of preparing the same and a composition having the nanoparticle. According to the present invention, Coenzyme Q10 may be dissolved in only a water-miscible organic solvent, and easily made into a nano-sized particle and solubilized under a low energy condition, for example, by simple stirring. The coenzyme Q10 may be dispersion-stabilized by an amino acid or protein. The coenzyme Q10 is formed in a nano-sized particle and solubilized, an absorption rate may be increased and simultaneously deliver the amino acid and protein with the nanoparticle. Thus, the coenzyme Q10 nanoparticle can be effectively used in food, cosmetics and medicine.Type: GrantFiled: April 6, 2010Date of Patent: July 22, 2014Assignee: Korea Research Institute of Bioscience and BiotechnologyInventors: Bong Hyun Chung, Jung Hyun Han -
Patent number: 8742013Abstract: The present disclosure provides polymer compounds binding with lipoamide produced by the reaction of the primary amine group of lipoamide with the carboxy group of polysaccharide compounds such as chondroitin sulfates, carboxymethyl celluloses, or hyaluronic acids; functional compounds such as peptides, proteins, growth factors; or drugs; or biocompatible polymers such as poly(ethylene oxide), poly(vinyl alcohol), or poly(vinyl pyrrolidone). The present disclosure also provides their synthesis methods, products of hydrogels and films using the same as and methods for manufacturing the products.Type: GrantFiled: October 29, 2009Date of Patent: June 3, 2014Assignee: Seoul National University of Technology Center for Industrial CollaborationInventors: Insup Noh, Seongyeun Jo, Doyeon Kim, Junghoon Woo
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Publication number: 20140120154Abstract: The present invention relates to novel therapies for treatment of new and existing type 1 and type 2 diabetes, PreDiabetes, Latent Autoimmune Diabetes of Adulthood, and diseases of insulin deficiency, beta cell deficiency, insulin resistance and impaired glucose metabolism. In particular, the present invention identifies common peptides within the human Reg1a, Reg1b, Reg3a and Reg4, as signaling peptides for beta cell generation acting through the human Reg Receptor on the surface of human pancreatic extra-islet tissue.Type: ApplicationFiled: October 26, 2012Publication date: May 1, 2014Inventor: Claresa Levetan
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Publication number: 20140054163Abstract: Methods for labeling or modifying cysteine residues in proteins and/or enzymes are disclosed. The methods include the reaction of an o-naphthoquinone methide with a thiol group of a cysteine residue of a protein or enzyme, which can be reversible in preferred embodiments. The o-naphthoquinone methide can conveniently be generated by irradiation of a precursor compound, preferably in an aqueous solution, suspension, or dispersion.Type: ApplicationFiled: February 20, 2013Publication date: February 27, 2014Applicant: University of Georgia Research Foundation, Inc.Inventors: VLADIMIR V. POPIK, GEERT-JAN BOONS, JUN GUO, SELVANATHAN ARUMUGAM, EMMANUEL NEKONGO, NANNAN LIN
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Publication number: 20140056966Abstract: The present invention provides an anti-tumor or anti-angiogenesis medicament, the combination or kit containing the medicament, and the method for producing the same. The anti-tumor or anti-angiogenesis medicament contains a conjugate comprising a modifying agent and the angiostatin or its fragments, wherein the conjugate exhibits prolonged in vivo half-life as compared to an unmodified angiostatin or its fragments. The modifying agent is selected from the group consisting of macromolecular polymers, protein molecules or fragments thereof, peptides, small molecules, or chemical substances of any other forms.Type: ApplicationFiled: June 5, 2012Publication date: February 27, 2014Applicant: PROTGEN LTD.Inventors: Yongzhang LUO, Guodong Chang, Shuling Yang, Lei Gao, Yan Fu
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Publication number: 20140039167Abstract: The invention conjugates that can be prepared by contacting a polymer comprising an acetal or ketal branching point with a pharmacologically active agent under conditions suitable to form a covalent attachment between the polymer and the pharmacologically active agent.Type: ApplicationFiled: October 3, 2013Publication date: February 6, 2014Applicant: Nectar TherapeuticsInventors: Samuel P. McManus, Antoni Kozlowski
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Publication number: 20130344590Abstract: An object of the present invention is to provide, as a method for immobilizing a protein molecule, protein immobilization method and means in which orientation of a molecule to be immobilized can be controlled, the molecule can be stably immobilized without a complicated process and a chemical group used for immobilization does not affect the activity and the function of the protein. Specifically, the present invention relates to a method for immobilizing a molecule including the steps of forming a labeled molecule by attaching a label peptide sequence comprising a hydroxyl group-containing amino acid to a molecule; and bringing a molecule having a phenylboronic acid group into contact with the labeled molecule, to capture the labeled molecule by the molecule having a phenylboronic acid group.Type: ApplicationFiled: January 30, 2012Publication date: December 26, 2013Inventors: Tomohiro Konno, Kazuhiko Ishihara, Hirokazu Nishida
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Publication number: 20130337536Abstract: The present disclosure is directed to a reactive ester agent capable of conjugating a reporter molecule to a carrier molecule or solid support. The reactive ester agent has the general formula: wherein the variables are described throughout the application.Type: ApplicationFiled: August 21, 2013Publication date: December 19, 2013Applicant: LIFE TECHNOLOGIES CORPORATIONInventors: Evan Antoulinakis, Kyle Gee, Aleksey Rukavishnikov
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Patent number: 8604127Abstract: The present invention relates to a conjugate of a protein or peptide with a polyethylene glycol derivative having catechol, wherein the protein or peptide is mono-PEGylated at the N-terminal with the polyethylene glycol derivative, and to a preparation method thereof. According to the invention, the catechol-PEG derivative can be site-specifically conjugated with the N-terminal amine group of a protein or peptide, so that a homogeneous polyethylene glycol-protein or -peptide conjugate can be obtained in high yield. Unlike a prior art conjugate, the conjugate obtained according to the invention allows the decrease in the activity of the protein to be minimized without chemically modifying the protein, and thus the conjugate has an excellent pharmacological effect. Also, because the conjugate is homogeneous, the process for preparing the conjugate can be simplified. Moreover, the conjugate has uniform biological efficacy in vivo and shows strong resistance to hydrolysis and thus a long in vivo duration time.Type: GrantFiled: October 29, 2010Date of Patent: December 10, 2013Assignees: Korea Advanced Institute of Science and Technology, Inno Therapy Inc.Inventors: Haeshin Lee, Hyukjin Lee, In Taek Song, Moon Sue Lee
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Publication number: 20130324701Abstract: The invention provides FGFR fusion proteins, methods of making them, and methods of using them to treat proliferative disorders, including cancers and disorders of angiogenesis. The FGFR fusion molecules can be made in CHO cells and may comprise deletion mutations in the extracellular domains of the FGFRs which improve their stability. These fusion proteins inhibit the growth and viability of cancer cells in vitro and in vivo. The combination of the relatively high affinity of these receptors for their ligand FGFs and the demonstrated ability of these decoy receptors to inhibit tumor growth is an indication of the clinical value of the compositions and methods provided herein.Type: ApplicationFiled: May 29, 2013Publication date: December 5, 2013Applicant: FIVE PRIME THERAPEUTICS, INC.Inventors: Lewis T. WILLIAMS, Elizabeth BOSCH, Stephen K. DOBERSTEIN, Kevin HESTIR, Diane HOLLENBAUGH, Ernestine LEE, Minmin QIN QIN, Ali SADRA, Justin WONG, Ge WU, Hongbing ZHANG ZHANG
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Publication number: 20130324465Abstract: The invention provides compositions and methods for treating a disease or disorder associated with vascular endothelial growth factor (VEGF). Specifically, the invention relates to an oligomerized VEGF binding domain to provide VEGF antagonism, and thereby treat diseases associated thereof.Type: ApplicationFiled: August 5, 2011Publication date: December 5, 2013Applicant: Genzyem CorporationInventors: James Stefano, Clark Pan, Huawei Qiu, Michael O'Callaghan, Gloria Matthews
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Patent number: 8575282Abstract: A modified compound that has at least one further functional group, in particular a bio- or macromolecule, comprising at least one x-fold (x?1) chemoselectively incorporated phosphoramidate group of general formula (I), NPO(OR1)(OR1?), and/or at least one x-fold (x?1) chemoselectively incorporated phosphonamide group of general formula (Ia), NPO(R1)(OR1?). R1 and R1? is selected from the group containing glycerol, polyglycerol, PEG polymers of the general empirical formula C2nH4n+2On+1 with n?1, Cn-alkyl chains with n?1; functionalized Cn-alkyl chains with n?1, aryls, heteroaryl, silyl, lipids, fluorophores, saccharides, peptides, crown ethers, or a linker, which links the aforementioned groups. R1 and R1? can be identical to or different from one another.Type: GrantFiled: March 9, 2010Date of Patent: November 5, 2013Assignee: Freie Universitaet BerlinInventors: Christian Hackenberger, Giuseppe Del Signore, Remigiusz Serwa, Ina Wilkening, Robert Vallee
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Publication number: 20130281357Abstract: Anti-angiogenic agents or polypeptides comprising an amino acid segment substantially similar to domain one of CD2 wherein the polypeptide has a ?-sheet formed by two segments. Methods of using such agents and polypeptide are also included.Type: ApplicationFiled: July 13, 2011Publication date: October 24, 2013Applicant: Georgia State University Research FoundationInventors: Zhi-Ren Liu, Jenny J. Yang, Yin Lu
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Publication number: 20130274322Abstract: A new process for the manufacture of iodinated xanthenes in high purity includes a cyclization step followed by an iodination step. No extraction, chromatographic or solvent concentration steps are required, and the intermediate as well as final compounds are isolated via filtration or similar means. The process requires a single organic solvent, and the steps are completed at temperatures below 100° C. The exclusion of chloride ions, of chloride free-radicals, hypochlorite ions, or hypochlorous acid as reagents or from reagents that may generate these species in situ in the presence of oxidants, prevents undesirable impurity formation. Several new compounds have been conceived and isolated using these methods. These new compounds are also formed into new medicaments.Type: ApplicationFiled: June 12, 2013Publication date: October 17, 2013Inventors: Jamie Singer, Eric A. Wachter, Timothy Scott, Marlon Lutz, Kevin Babiak
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Publication number: 20130237474Abstract: Modified biosynthetic polypeptide fusion inhibitors, methods for manufacturing, and uses thereof are provided.Type: ApplicationFiled: November 13, 2012Publication date: September 12, 2013Applicant: AMBRX, INC.Inventors: Roberto Mariani, Bruce E. Kimmel
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Patent number: 8530626Abstract: Methods to produce keratin elastomer, involving: (A)(1) reacting a diisocyanate with a blocking agent to form a diisocyanate with one —NCO group blocked by the blocking agent and one —NCO group unblocked, (2) reacting the diisocyanate with one —NCO group blocked by the blocking agent and one —NCO group unblocked with keratin at about 100° to about 120° C. to form keratin urethane with —NCO group functionality (i.e., with one —NCO group unblocked), (3) optionally reacting the keratin urethane with —NCO group functionality with a compound capable of reacting with the —NCO group; (B) reacting a diisocyanate with keratin to form keratin elastomer; or (C) reacting a monoisocyanate with keratin to form keratin elastomer.Type: GrantFiled: May 13, 2011Date of Patent: September 10, 2013Assignee: The United States of America, as represented by the Secretary of AgricultureInventor: Jeanette M. Cardamone
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Publication number: 20130216539Abstract: The present invention includes methods of generating derivatives of a protein, as well as methods of treating a subject with the derivatized proteins. More particularly, the present invention includes methods of generating derivatives of HSP 70 proteins and methods of treating a subject with the derivatized HSP 70 proteins.Type: ApplicationFiled: February 15, 2013Publication date: August 22, 2013Applicant: ALS Biopharma, LLCInventor: ALS Biopharma, LLC
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Publication number: 20130196928Abstract: This application relates to ABx toxin mutants and libraries of said mutant proteins, in which a peptide insert is introduced into the protease-sensitive loop of the A-chain sequence to alter the type of cells to which toxic species are delivered. Said libraries are used in the development of therapeutics targeted against specific cell types.Type: ApplicationFiled: January 11, 2013Publication date: August 1, 2013Applicant: MOLECULAR TEMPLATES, INC.Inventor: Molecular Templates, Inc.
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Publication number: 20130190478Abstract: The current invention reports a method for the purification of a non-glycosylated, heterologous polypeptide, which has been recombinantly produced in a prokaryotic cell, wherein the method comprises three chromatography steps of which the first chromatography step selected from i) hydrophobic charge induction chromatography, or ii) hydrophobic interaction chromatography, or iii) affinity chromatography, or iv) ion exchange chromatography, the second chromatography step is selected from i) anion exchange chromatography, or ii) cation exchange chromatography, or iii) hydroxylapatite chromatography, or iv) hydrophobic interaction chromatography, and the a third chromatography step is selected from i) hydrophobic charge induction chromatography, or ii) anion exchange chromatography, or iii) cation exchange chromatography, or iv) hydrophobic interaction chromatography, whereby the first chromatography step is an affinity chromatography in case of polypeptides capable of interacting with metal ligands, the second cType: ApplicationFiled: September 21, 2012Publication date: July 25, 2013Inventor: Hoffmann-La Roche Inc.
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Publication number: 20130183712Abstract: The invention provides methods and compositions for the rapid and sensitive detection of post-translationally modified proteins, and particularly of those with posttranslational glycosylations. The methods can be used to detect O-GlcNAc posttranslational modifications on proteins on which such modifications were undetectable using other techniques. In one embodiment, the method exploits the ability of an engine˜red mutant of ?-1,4-galactosyltransferase to selectively transfer an unnatural ketone functionality onto O-GlcNAc glycosylated proteins. Once transferred, the ketone moiety serves as a versatile handle for the attachment of biotin, thereby enabling detection of the modified protein. The approach permits the rapid visualization of proteins that are at the limits of detection using traditional methods. Further, the preferred embodiments can be used for detection of certain disease states, such as cancer, Alzheimer's disease, neurodegeneration, cardiovascular disease, and diabetes.Type: ApplicationFiled: February 22, 2013Publication date: July 18, 2013Applicant: CALIFORNIA INSTITUTE OF TECHNOLOGYInventor: California Institute of Technology
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Publication number: 20130171715Abstract: Fluorescent phenyl xanthene dyes are described that comprise any fluorescein, rhodamine or rhodol comprising a particular C9 phenyl ring. One or both of the ortho groups on the lower C9 phenyl ring is ortho substituted with a group selected from alkyl, heteroalkyl, alkoxy, halo, haloalkyl, amino, mercapto, alkylthio, cyano, isocyano, cyanato, mercaptocyanato, nitroso, nitro, azido, sulfeno, sulfinyl, and sulfino. In one embodiment, halo and/or hydroxy groups are used. Optimal dyes contain a lower C9 phenyl ring in which both ortho groups are the same and the lower ring exhibits some form a symmetry relative to an imaginary axis running from the phenyl rings point of attachment to the remainder of the xanthene dye through a point para to the point of attachment. The phenyl xanthene dyes may be activated. Furthermore, the phenyl xanthene dyes may be conjugated to one or more substances including other dyes.Type: ApplicationFiled: January 16, 2013Publication date: July 4, 2013Applicant: LIFE TECHNOLOGIES CORPORATIONInventor: LIFE TECHNOLOGIES CORPORATION
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Publication number: 20130165383Abstract: The disclosure provides Apo-2 ligand variant polypeptides. Methods of making and chemically modifying Apo-2 ligand variant polypeptides are also provided. In addition, formulations of Apo-2 ligand variant polypeptides are provided. In addition, therapeutic methods for using Apo-2 ligand variant polypeptides are provided.Type: ApplicationFiled: April 6, 2012Publication date: June 27, 2013Applicant: Genentech, Inc.Inventors: Robert F. Kelley, Sarah Hymowitz
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Publication number: 20130165382Abstract: The present invention relates to the formation of conjugates (e.g., protein-protein dimers) using a-halo-acetophenones, benzylic halides, quinones, and related compounds as a conjugating system. The invention also features compositions that include the conjugates described herein, as well as uses of these conjugates in methods of medical treatment.Type: ApplicationFiled: June 1, 2011Publication date: June 27, 2013Applicant: ADVANCED PROTEOME THERAPEUTICS INC.Inventors: Alexander Krantz, Peng Yu
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Publication number: 20130157284Abstract: The invention relates to intracellular lipid binding proteins that bind retinoids and/or dye ligands and that are modified to transmit or emit light at a variety of different wavelengths.Type: ApplicationFiled: March 23, 2011Publication date: June 20, 2013Applicant: Board of Trustees of Michigan State UniversityInventors: Babak Borhan, James Geiger, Wenjing Wang, Chrysoula Vasileiou, Kin Sing Lee, Tetyana Berbasova
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Publication number: 20130156818Abstract: Provided herein are methods and compositions for controlling assembly of modified viral core proteins, for example, into a viral capsid or a nanocage. In some embodiments, the disclosed modified viral core proteins comprise at least one mutation or modification that can substantially prevent assembly of the viral core proteins until assembly is desired. In some embodiments, assembly of the viral core proteins may be triggered, for example, by contacting the viral core proteins with a reducing agent and/or by reducing the concentration of a denaturant. The viral core proteins may self-assemble to form a viral capsid or nanocage.Type: ApplicationFiled: September 10, 2012Publication date: June 20, 2013Inventors: Miguel de los Rios, Stephanie de los Rios, Jacek Ostrowski, Kenneth J. Oh, Ilan Zipkin
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Publication number: 20130149732Abstract: A method of labeling a sulfenic acid (—SOH) group of a cysteine residue in a protein; or peptide, comprises contacting said protein or peptide with a beta-ketoester to covalently couple said beta-ketoester to said cysteine residue and form a beta-ketoester-labeled cysteine residue in said protein or peptide.Type: ApplicationFiled: August 24, 2012Publication date: June 13, 2013Inventors: Cristina M. Furdui, Allen W. Tsang, Jiang Qian
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Patent number: 8449880Abstract: Disclosed herein is a composition and method for sample preparation of proteins for their size separation by electrophoresis, suitable for molecular-weight determination of proteins in the range between about 14,000 and 500,000. In an embodiment, proteins, particularly those exhibiting biased migration, are modified to change their intrinsic charge, or carbohydrate component to improve accuracy of their molecular weights as determined by electrophoretic size separation via their interaction with ionic surfactants. In a preferred embodiment, the proteins are carbamylated with potassium cyanate and their carbohydrate components are oxidized with sodium periodate.Type: GrantFiled: November 22, 2010Date of Patent: May 28, 2013Inventors: Vladislav Dolnik, William A. Gurske
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Patent number: 8450276Abstract: A method of improving the resistance of collagenous tissue to mechanical degradation in accordance with the present invention comprises the step of contacting at least a portion of a collagenous tissue with an effective amount of a crosslinking reagent. Methods and devices for enhancing the body's own efforts to stabilize discs in scoliotic spines by increasing collagen crosslinks. This stability enhancement is caused by reducing the bending hysteresis and increasing the bending stiffness of scoliotic spines, by injecting non-toxic crosslinking reagents into the convex side of discs involved in the scoliotic curve. Alternatively, contact between the tissue and the crosslinking reagent is effected by placement of a time-release delivery system directly into or onto the target tissue.Type: GrantFiled: June 16, 2010Date of Patent: May 28, 2013Assignee: Orthopeutics L.P.Inventor: Thomas P. Hedman
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Publication number: 20130115252Abstract: A method of preparing genipin-rich materials from the fruit of Genipa americana fruit for their use as a cross-linking agent and as a raw material to produce colors is disclosed. The genipin-rich materials can be used in a broad range of applications including personal care, cosmetics, dietary supplements, packaging, textiles, beverages, foodstuffs, drugs, and animal feeds.Type: ApplicationFiled: November 7, 2012Publication date: May 9, 2013Applicant: Wild Flavors, Inc.Inventor: Wild Flavors, Inc.
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Publication number: 20130109072Abstract: A support for enzyme immobilization is described, which is for immobilizing enzymes of various molecular sizes and also for, due to the modification of the surface silanol groups of porous silica particles, for immobilizing various kinds of enzymes, and enables the design of an immobilized enzyme, which exhibits an activity equivalent to that of the corresponding non-immobilized enzyme and withstands repeated use. A method for producing the support is also described. The support includes porous silica particles having an interparticle void structure therein, characterized in that the porous silica particles have a specific average particle size, a specific surface area, a specific pore volume, a specific pore size distribution and a specific porosity and have a substituent containing an organic group or an amino group on the surface thereof. An immobilized protein obtained by immobilizing a protein on the above support is also described.Type: ApplicationFiled: June 8, 2011Publication date: May 2, 2013Applicants: NATIONAL INSTITUTE OF ADVANCED INDUSTRIAL SCIENCE AND TECHNOLOGY, JGC CORPORATIONInventors: Tatsuo Tsunoda, Takayuki Nara, Seigo Ono, Chisato Sekikawa, Fujio Mizukami, Shuzo Kojima, Naoki Tahara, Hideaki Togashi, Miki Egami
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Publication number: 20130108578Abstract: The disclosure provides Apo-2 ligand variant polypeptides. Methods of making and chemically modifying Apo-2 ligand variant polypeptides are also provided. In addition, formulations of Apo-2 ligand variant polypeptides are provided.Type: ApplicationFiled: May 17, 2012Publication date: May 2, 2013Applicant: Genentech, Inc.Inventors: Robert F. Kelley, Stephanie Ho Lindstrom
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Patent number: 8414880Abstract: Photosensitizer mixtures and method of treating cellulites by light illumination are presented. Photosensitizer is combined with cellular products, e.g. adipose cells, collagen, previously removed by liposuction. Concentrations used depend on treatment area, cellulite stage and whether cellulites are in depressed or elevated skin areas. The cosmetic treatment reduces/removes localized lipodystrophies, flaccidity, cellulite using localized laser, LED, etc emissions. Applied light energy destroys “fat” cells by a combination of chemical reactions primarily, and temperature, wherein cell walls break releasing cell fluid. Transmission devices guide radiation to the treatment site. One or more light sources like laser diodes or LEDs may be coupled into one or more optical fibers to increase the covered area and increase the amount of radiation in that area. Optical fibers can be introduced percutaneously or interstitially. Cell fluid in the treatment area is removed by a combination of techniques.Type: GrantFiled: October 6, 2010Date of Patent: April 9, 2013Assignee: Bioliter Pharme Marketing LtdInventors: Danilo Castro, Wolfgang Neuberger
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Patent number: 8409814Abstract: The present invention relates to biosensors. In some embodiments, the biosensors are modified ligand binding molecules. In some embodiments, the modified ligand binding molecule is a phosphate binding protein (PBP). In some embodiments, the modified ligand binding molecules are labeled to be capable of RET, e.g., comprising a donor and acceptor moiety. In some embodiments of the invention, there is a detectable change in RET (e.g., FRET) when the modified ligand binding molecule binds and/or releases the ligand (e.g., phosphate). The invention also provides related methods, reactions and assays.Type: GrantFiled: September 1, 2010Date of Patent: April 2, 2013Assignee: Life Technologies CorporationInventors: Kurt Vogel, Rhonda Newman, Steven Riddle
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Publication number: 20130079499Abstract: Disclosed are: an Fc binding protein having increased stability with respect to heat, acid, and/or alkalinity compared with the wild type; a method for producing same; and a method for specifically isolating protein containing an Fc binding protein binding site using said Fc binding protein as a ligand for affinity chromatography. An Fc binding protein was obtained having increased stability with respect to heat, acid, and/or alkalinity compared with the wild-type human Fc receptor by means of substituting at least one specific amino acid residue in the extracellular domain of the wild-type human Fc receptor with another amino acid residue. The Fc binding protein is useful as a ligand for affinity chromatography for example by immobilizing in a solid phase.Type: ApplicationFiled: March 10, 2011Publication date: March 28, 2013Applicants: TOSOH CORPORATION, SAGAMI CHEMICAL RESEARCH INSTITUTEInventors: Kouta Hatayama, Yoshiharu Asaoka, Toru Tanaka, Teruhiko Ide