JP2006512921A - 多量体タンパク質の生産 - Google Patents
多量体タンパク質の生産 Download PDFInfo
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| US7527966B2 (en) | 2002-06-26 | 2009-05-05 | Transgenrx, Inc. | Gene regulation in transgenic animals using a transposon-based vector |
| US8071364B2 (en) * | 2003-12-24 | 2011-12-06 | Transgenrx, Inc. | Gene therapy using transposon-based vectors |
| US7718847B2 (en) * | 2004-05-27 | 2010-05-18 | Kyoto University | Method of gene introduction in in-vivo spermatogenic cell |
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| US8932861B2 (en) | 2008-04-10 | 2015-01-13 | Cj Cheiljedang Corporation | Transformation vector comprising transposon, microorganisms transformed with the vector, and method for producing L-lysine using the microorganism |
| KR101126041B1 (ko) * | 2008-04-10 | 2012-03-19 | 씨제이제일제당 (주) | 트랜스포존을 이용한 형질전환용 벡터, 상기 벡터로형질전환된 미생물 및 이를 이용한 l-라이신 생산방법 |
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| EP2342224A2 (en) * | 2008-09-25 | 2011-07-13 | TransGenRx, Inc. | Novel vectors for production of interferon |
| WO2010036978A2 (en) * | 2008-09-25 | 2010-04-01 | Transgenrx, Inc. | Novel vectors for production of growth hormone |
| US9150881B2 (en) * | 2009-04-09 | 2015-10-06 | Proteovec Holding, L.L.C. | Production of proteins using transposon-based vectors |
| US9314005B2 (en) | 2009-07-01 | 2016-04-19 | Transposagen Biopharmaceuticals, Inc. | Genetically modified rat models for severe combined immunodeficiency (SCID) |
| EP2462230B1 (en) * | 2009-08-03 | 2015-07-15 | Recombinetics, Inc. | Methods and compositions for targeted gene modification |
| WO2012051615A1 (en) | 2010-10-15 | 2012-04-19 | Transgenrx, Inc. | Novel vectors for production of glycosylated interferon |
| AU2013204327B2 (en) * | 2012-04-20 | 2016-09-01 | Aviagen | Cell transfection method |
| US10323279B2 (en) | 2012-08-14 | 2019-06-18 | 10X Genomics, Inc. | Methods and systems for processing polynucleotides |
| US11591637B2 (en) | 2012-08-14 | 2023-02-28 | 10X Genomics, Inc. | Compositions and methods for sample processing |
| US9701998B2 (en) | 2012-12-14 | 2017-07-11 | 10X Genomics, Inc. | Methods and systems for processing polynucleotides |
| US10221442B2 (en) | 2012-08-14 | 2019-03-05 | 10X Genomics, Inc. | Compositions and methods for sample processing |
| US9951386B2 (en) | 2014-06-26 | 2018-04-24 | 10X Genomics, Inc. | Methods and systems for processing polynucleotides |
| US10273541B2 (en) | 2012-08-14 | 2019-04-30 | 10X Genomics, Inc. | Methods and systems for processing polynucleotides |
| US10752949B2 (en) | 2012-08-14 | 2020-08-25 | 10X Genomics, Inc. | Methods and systems for processing polynucleotides |
| US10400280B2 (en) | 2012-08-14 | 2019-09-03 | 10X Genomics, Inc. | Methods and systems for processing polynucleotides |
| CN111748607B (zh) | 2012-08-14 | 2024-04-30 | 10X基因组学有限公司 | 微胶囊组合物及方法 |
| CA2894694C (en) | 2012-12-14 | 2023-04-25 | 10X Genomics, Inc. | Methods and systems for processing polynucleotides |
| US10533221B2 (en) | 2012-12-14 | 2020-01-14 | 10X Genomics, Inc. | Methods and systems for processing polynucleotides |
| WO2014124338A1 (en) | 2013-02-08 | 2014-08-14 | 10X Technologies, Inc. | Polynucleotide barcode generation |
| WO2014145736A2 (en) * | 2013-03-15 | 2014-09-18 | Transposagen Biopharmaceuticals, Inc. | Reproducible method for testis-mediated genetic modification (tgm) and sperm-mediated genetic modification (sgm) |
| WO2014189957A2 (en) | 2013-05-23 | 2014-11-27 | The Board Of Trustees Of The Leland Stanford Junior University | Transposition into native chromatin for personal epigenomics |
| CN114534806B (zh) | 2014-04-10 | 2024-03-29 | 10X基因组学有限公司 | 用于封装和分割试剂的流体装置、系统和方法及其应用 |
| US12312640B2 (en) | 2014-06-26 | 2025-05-27 | 10X Genomics, Inc. | Analysis of nucleic acid sequences |
| CN113249435B (zh) | 2014-06-26 | 2024-09-03 | 10X基因组学有限公司 | 分析来自单个细胞或细胞群体的核酸的方法 |
| CN106536756A (zh) | 2014-06-26 | 2017-03-22 | 10X基因组学有限公司 | 核酸序列的分析 |
| PL3164130T3 (pl) | 2014-07-01 | 2020-02-28 | Millennium Pharmaceuticals, Inc. | Związki heteroarylowe użyteczne jako inhibitory enzymu aktywującego sumo |
| CN114807307A (zh) | 2014-10-29 | 2022-07-29 | 10X 基因组学有限公司 | 用于靶核酸测序的方法和组合物 |
| US9975122B2 (en) | 2014-11-05 | 2018-05-22 | 10X Genomics, Inc. | Instrument systems for integrated sample processing |
| SG11201705615UA (en) | 2015-01-12 | 2017-08-30 | 10X Genomics Inc | Processes and systems for preparing nucleic acid sequencing libraries and libraries prepared using same |
| WO2016137973A1 (en) | 2015-02-24 | 2016-09-01 | 10X Genomics Inc | Partition processing methods and systems |
| US11274343B2 (en) | 2015-02-24 | 2022-03-15 | 10X Genomics, Inc. | Methods and compositions for targeted nucleic acid sequence coverage |
| US10934636B2 (en) | 2015-08-12 | 2021-03-02 | CeMM—FORSCHUNGSZENTRUM FÜR MOLEKULARE MEDIZIN GmbH | Methods for studying nucleic acids |
| SG11201804086VA (en) | 2015-12-04 | 2018-06-28 | 10X Genomics Inc | Methods and compositions for nucleic acid analysis |
| WO2017197343A2 (en) | 2016-05-12 | 2017-11-16 | 10X Genomics, Inc. | Microfluidic on-chip filters |
| WO2017197338A1 (en) | 2016-05-13 | 2017-11-16 | 10X Genomics, Inc. | Microfluidic systems and methods of use |
| US10815525B2 (en) | 2016-12-22 | 2020-10-27 | 10X Genomics, Inc. | Methods and systems for processing polynucleotides |
| US10011872B1 (en) | 2016-12-22 | 2018-07-03 | 10X Genomics, Inc. | Methods and systems for processing polynucleotides |
| US10550429B2 (en) | 2016-12-22 | 2020-02-04 | 10X Genomics, Inc. | Methods and systems for processing polynucleotides |
| US12264411B2 (en) | 2017-01-30 | 2025-04-01 | 10X Genomics, Inc. | Methods and systems for analysis |
| EP3545089B1 (en) | 2017-01-30 | 2022-03-09 | 10X Genomics, Inc. | Methods and systems for droplet-based single cell barcoding |
| CN116064732A (zh) | 2017-05-26 | 2023-05-05 | 10X基因组学有限公司 | 转座酶可接近性染色质的单细胞分析 |
| US20180340169A1 (en) | 2017-05-26 | 2018-11-29 | 10X Genomics, Inc. | Single cell analysis of transposase accessible chromatin |
| US11733248B2 (en) | 2017-09-25 | 2023-08-22 | Fred Hutchinson Cancer Center | High efficiency targeted in situ genome-wide profiling |
| CN111051523B (zh) | 2017-11-15 | 2024-03-19 | 10X基因组学有限公司 | 功能化凝胶珠 |
| US10829815B2 (en) | 2017-11-17 | 2020-11-10 | 10X Genomics, Inc. | Methods and systems for associating physical and genetic properties of biological particles |
| CN119020348A (zh) | 2018-02-05 | 2024-11-26 | 斯坦福大学托管董事会 | 用于单细胞和集合细胞的多重测量的系统和方法 |
| SG11202009889VA (en) | 2018-04-06 | 2020-11-27 | 10X Genomics Inc | Systems and methods for quality control in single cell processing |
| KR20220080091A (ko) | 2019-09-06 | 2022-06-14 | 체엠엠 - 포르슝스첸트룸 퓨어 몰레쿨라레 메디친 게엠베하 | Rna 올리고뉴클레오티드를 시퀀싱하기 위한 방법 |
| CN114317600A (zh) * | 2020-10-12 | 2022-04-12 | 上海君赛生物科技有限公司 | 新型PiggyBac转座子系统及其用途 |
| CN118510910A (zh) * | 2022-01-10 | 2024-08-16 | 塞提斯生物技术有限公司 | 用于处理含核酸样品的方法 |
| WO2025183084A1 (ja) * | 2024-02-28 | 2025-09-04 | 国立研究開発法人産業技術総合研究所 | 蛋白質の分泌促進方法 |
Family Cites Families (166)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4870009A (en) | 1982-11-22 | 1989-09-26 | The Salk Institute For Biological Studies | Method of obtaining gene product through the generation of transgenic animals |
| US4670388A (en) | 1982-12-30 | 1987-06-02 | Carnegie Institution Of Washington | Method of incorporating DNA into genome of drosophila |
| US4914025A (en) | 1985-12-05 | 1990-04-03 | Colin Manoil | Export of intra-cellular substances |
| EP0279582A3 (en) | 1987-02-17 | 1989-10-18 | Pharming B.V. | Dna sequences to target proteins to the mammary gland for efficient secretion |
| DE3854476T2 (de) | 1987-07-06 | 1996-04-04 | Univ Louisiana State | Inhibierung von eukaryotischen pathogenen und neoplasmen mit lytischen peptiden. |
| CA1327311C (en) | 1987-07-06 | 1994-03-01 | Jesse M. Jaynes | Therapeutic antimicrobial polypeptides, their use and methods for preparation |
| US5861478A (en) | 1987-07-06 | 1999-01-19 | Helix Biomedix, Inc. | Lytic peptides |
| US5212080A (en) | 1987-10-05 | 1993-05-18 | Washington University | Method of DNA sequencing using DNA transposon Tn5seql |
| US5137829A (en) | 1987-10-05 | 1992-08-11 | Washington University | DNA transposon TN5SEQ1 |
| US5162215A (en) | 1988-09-22 | 1992-11-10 | Amgen Inc. | Method of gene transfer into chickens and other avian species |
| US5703055A (en) | 1989-03-21 | 1997-12-30 | Wisconsin Alumni Research Foundation | Generation of antibodies through lipid mediated DNA delivery |
| US5102797A (en) | 1989-05-26 | 1992-04-07 | Dna Plant Technology Corporation | Introduction of heterologous genes into bacteria using transposon flanked expression cassette and a binary vector system |
| EP0584279B1 (en) | 1991-05-14 | 2001-03-14 | The University Of Connecticut | Targeted delivery of genes encoding immunogenic proteins |
| US5753502A (en) | 1993-08-05 | 1998-05-19 | Icos Corporation | Neuron-specific ICAM-4 promoter |
| WO1993015185A1 (en) | 1992-01-27 | 1993-08-05 | North Carolina State University | GENE TRANSFER IN POULTRY BY INTRODUCTION OF EMBRYO CELLS $i(IN OVO) |
| AU2146092A (en) | 1992-05-28 | 1993-12-30 | Scientific Dimensions Usa, Inc. | Transgenic animal production with biolistically transformed spermatozoa |
| EP0669986B1 (en) | 1992-11-13 | 2003-04-09 | Idec Pharmaceuticals Corporation | Fully impaired consensus kozac sequences for mammalian expression |
| EP0688358A4 (en) | 1993-03-12 | 1997-10-01 | Univ Creighton | IMPROVED VECTORS FOR GENTHERAPY |
| US6607884B1 (en) | 1993-03-19 | 2003-08-19 | The Johns Hopkins University School Of Medicine | Methods of detecting growth differentiation factor-8 |
| US20030074680A1 (en) | 1993-03-19 | 2003-04-17 | Johns Hopkins University School Of Medicine | Growth differentiation factor-8 |
| US5645991A (en) | 1993-05-04 | 1997-07-08 | Univ. Of Connecticut | Transposon-containing DNA cloning vector and uses thereof |
| US5512483A (en) | 1993-05-21 | 1996-04-30 | Mcgill University | Expression vectors responsive to steroid hormones |
| AU7321294A (en) * | 1993-06-30 | 1995-01-24 | Board Of Supervisors Of Louisiana State University And Agricultural And Mechanical College, The | Transformed eukaryotic cells, and transposon-based transformation vectors |
| US6156568A (en) | 1993-06-30 | 2000-12-05 | Board Of Supervisors Of Louisiana State University And Agricultural And Mechanical College | Transformed eukaryotic cells |
| WO1995001424A1 (en) | 1993-06-30 | 1995-01-12 | Board Of Supervisors Of Louisiana State University And Agricultural And Mechanical College | Transformed mammalian cells capable of expressing cecropin b |
| US5648244A (en) * | 1993-09-27 | 1997-07-15 | President And Fellows Of Harvard College | Production, purification, cleavage and use of fusion peptides |
| US5827690A (en) | 1993-12-20 | 1998-10-27 | Genzyme Transgenics Corporatiion | Transgenic production of antibodies in milk |
| EP0759087B1 (en) | 1994-05-13 | 2001-03-28 | Chiron Corporation | Compositions and methods for targeting gene delivery vehicles |
| US5914234A (en) | 1994-07-08 | 1999-06-22 | The Johns Hopkins University School Of Medicine | Methods of detecting growth differentiation factor-11 |
| US20030167492A1 (en) | 1994-07-08 | 2003-09-04 | Johns Hopkins University School Of Medicine | Transgenic non-human animals expressing a gdf-11 dominant negative polypeptide, and methods of making and using same |
| US5843705A (en) | 1995-02-21 | 1998-12-01 | Genzyme Transgenic Corporation | Transgenically produced antithrombin III |
| US5998698A (en) | 1995-06-07 | 1999-12-07 | Board Of Supervisors Of Louisiana State University And Agricultural And Mechanical College | Transgenic fish capable of expressing exogenous lytic peptides |
| NZ312332A (en) | 1995-06-07 | 2000-01-28 | Life Technologies Inc | Recombinational cloning using engineered recombination sites |
| WO1997005266A1 (en) | 1995-07-25 | 1997-02-13 | Introgene B.V. | Methods and means for targeted gene delivery |
| GB9518323D0 (en) * | 1995-09-07 | 1995-11-08 | Steidler Lothar | Materials and methods relating to the attachment and display of substances on cell surfaces |
| US6218185B1 (en) | 1996-04-19 | 2001-04-17 | The United States Of America As Represented By The Secretary Of Agriculture | Piggybac transposon-based genetic transformation system for insects |
| WO1997046589A2 (en) | 1996-06-07 | 1997-12-11 | Neorx Corporation | Humanized antibodies that bind to the same antigen as bound by antibody nr-lu-13, and their use in pretargeting methods |
| US6825396B2 (en) | 1996-06-12 | 2004-11-30 | Board Of Trustees Operating Michigan State University | Methods for tissue specific synthesis of protein in eggs of transgenic hens |
| CA2259908A1 (en) | 1996-07-08 | 1998-01-15 | Dnavec Research Inc. | In vivo electroporation method for early animal embryo |
| WO1998007830A2 (en) | 1996-08-22 | 1998-02-26 | The Institute For Genomic Research | COMPLETE GENOME SEQUENCE OF THE METHANOGENIC ARCHAEON, $i(METHANOCOCCUS JANNASCHII) |
| US5965443A (en) | 1996-09-09 | 1999-10-12 | Wisconsin Alumni Research Foundation | System for in vitro transposition |
| US5925545A (en) | 1996-09-09 | 1999-07-20 | Wisconsin Alumni Research Foundation | System for in vitro transposition |
| US6107477A (en) | 1996-09-26 | 2000-08-22 | Aurora Biosciences Corporation | Non-optimal Kozaks sequences |
| US6420524B1 (en) | 1997-02-20 | 2002-07-16 | Johns Hopkins University School Of Medicine | Gain of function mutations in ATP-dependent transposition proteins |
| AU6184298A (en) | 1997-02-25 | 1998-09-09 | Genzyme Transgenics Corporation | Transgenically produced non-secreted proteins |
| AU745049B2 (en) | 1997-03-11 | 2002-03-07 | Regents Of The University Of Minnesota | DNA-based transposon system for the introduction of nucleic acid into DNA of a cell |
| US6080912A (en) | 1997-03-20 | 2000-06-27 | Wisconsin Alumni Research Foundation | Methods for creating transgenic animals |
| CA2297375A1 (en) | 1997-07-24 | 1999-02-04 | Valentis, Inc. | Ghrh expression system and methods of use |
| WO1999005295A1 (en) | 1997-07-25 | 1999-02-04 | Thomas Jefferson University | Composition and method for targeted integration into cells |
| US20030115622A1 (en) | 1997-08-04 | 2003-06-19 | Ponce De Leon F. Abel | Production of avian embryonic germ (eg) cell lines by prolonged culturing of pgc's, use thereof for cloning and chimerization |
| US6716823B1 (en) | 1997-08-13 | 2004-04-06 | The Uab Research Foundation | Noninvasive genetic immunization, expression products therefrom, and uses thereof |
| EP1006790A1 (en) | 1997-08-22 | 2000-06-14 | Biotechnology and Biological Sciences Research Council | Use of mariner transposon in the production of transgenic animals |
| US6140129A (en) | 1997-09-17 | 2000-10-31 | Wisconsin Alumni Research Foundation | Chromosomal targeting in bacteria using FLP recombinase |
| US6897066B1 (en) | 1997-09-26 | 2005-05-24 | Athersys, Inc. | Compositions and methods for non-targeted activation of endogenous genes |
| US7129390B2 (en) | 1997-10-16 | 2006-10-31 | Avigenics, Inc | Poultry Derived Glycosylated Interferon Alpha 2b |
| IL135604A0 (en) | 1997-10-16 | 2001-05-20 | Univ Georgia | Vectors comprising a magnum-specific promoter for avian transgenesis |
| US20020053092A1 (en) | 1997-11-14 | 2002-05-02 | Readhead Carol W. | Nucleic acid constructs containing a cyclin A1 promoter, and kit |
| WO1999025863A1 (en) | 1997-11-14 | 1999-05-27 | Cedars-Sinai Medical Center | Transfection and transfer of male germ cells for generation of transgenic species |
| EP0935385A3 (en) * | 1998-02-04 | 2002-06-19 | Hitachi, Ltd. | Decoder device and receiver using the same |
| NZ506341A (en) | 1998-02-09 | 2003-02-28 | Tranxenogen Inc | Genetic manipulation of spermatogonia |
| IL123411A0 (en) | 1998-02-22 | 1998-09-24 | Kimron Veterinary Inst | High efficiency methods and compositions for integrating exogenous dna into genomic dna of sperm |
| US6022716A (en) | 1998-04-10 | 2000-02-08 | Genset Sa | High throughput DNA sequencing vector |
| US6291214B1 (en) | 1998-05-11 | 2001-09-18 | Glaxo Wellcome Inc. | System for generating recombinant viruses |
| US20020013955A1 (en) | 1998-06-10 | 2002-01-31 | Sharon Ogden | Production of recombinant protein in transgenic fish |
| EP1105469B1 (en) | 1998-08-11 | 2010-09-29 | University Of Hawaii | Mammalian transgenesis by intracytoplasmic sperm injection |
| AU5690799A (en) | 1998-08-25 | 2000-03-14 | Avigenics, Inc. | Direct oviduct transgenesis |
| US20030217375A1 (en) | 1998-08-31 | 2003-11-20 | Eyal Zcharia | Transgenic animals expressing heparanase and uses thereof |
| US6159736A (en) | 1998-09-23 | 2000-12-12 | Wisconsin Alumni Research Foundation | Method for making insertional mutations using a Tn5 synaptic complex |
| US20010036647A1 (en) | 1998-10-22 | 2001-11-01 | Prabhakara V. Choudary | Functionally assembled antigen-specific intact recombinant antibody and a method for production thereof |
| EP1375654A3 (en) | 1998-11-02 | 2008-01-16 | GTC Biotherapeutics, Inc. | Transgenic and cloned mammals |
| DE69933528T2 (de) | 1998-11-09 | 2007-08-09 | Nippon Biologicals, Inc. | Verfahren zur Cytokinproduktionn unter Verwendung eines Sendai Virus Expressionssystems |
| US7160682B2 (en) | 1998-11-13 | 2007-01-09 | Regents Of The University Of Minnesota | Nucleic acid transfer vector for the introduction of nucleic acid into the DNA of a cell |
| EP1130960A4 (en) | 1998-11-19 | 2003-07-30 | Wisconsin Alumni Res Found | TRANSGENIC ANIMALS |
| WO2000032039A1 (en) | 1998-12-04 | 2000-06-08 | Duke University | PURIFIED AND ISOLATED piwi FAMILY GENES AND GENE PRODUCTS AND METHODS EMPLOYING SAME |
| US20020148000A1 (en) | 1998-12-04 | 2002-10-10 | Shen Che-Kun James | HS-40 enhancer-containing vector in transgenic animals |
| WO2000056932A2 (en) | 1999-03-22 | 2000-09-28 | The University Of Georgia Research Foundation, Inc. | Germline-competent avian cells |
| JP2002542781A (ja) | 1999-04-28 | 2002-12-17 | ザ、ボード、オブ、トラスティーズ、オブ、ザ、リーランド、スタンフォード、ジュニア、ユニバーシティ | P因子由来ベクター及びその使用法 |
| US6518481B1 (en) | 1999-08-12 | 2003-02-11 | Exelixis, Inc. | Universal markers of transgenesis |
| US6773914B1 (en) | 1999-08-19 | 2004-08-10 | The United States Of America As Represented By The Secretary Of Agriculture | PiggyBac transformation system |
| CZ289464B6 (cs) | 1999-09-08 | 2002-01-16 | Biopharm Výzkumný Ústav Biofarmacie A Veterinárníc | Způsob konstrukce transgenní drůbeľe |
| KR20020073127A (ko) | 1999-09-17 | 2002-09-19 | 겐자임 트랜스제닉스 코포레이션 | 형질전환에 의하여 생성된 융합 단백질 |
| WO2001023525A2 (en) | 1999-09-30 | 2001-04-05 | Genzyme Transgenics Corporation | Methods of producing cloned and transgenic mammals |
| US20020055172A1 (en) | 1999-10-07 | 2002-05-09 | Harrington John J. | Multiple promoter expression constructs and methods of use |
| HUP0203537A2 (hu) | 1999-10-14 | 2003-02-28 | Genzyme Transgenics Corporation | Célmolekula transzgénikus állatban történő előállítására és tisztítására szolgáló eljárások |
| JP4609869B2 (ja) | 1999-12-03 | 2011-01-12 | 独立行政法人科学技術振興機構 | トランスポゾン転移酵素および遺伝子改変方法 |
| NZ519217A (en) | 1999-12-10 | 2004-03-26 | Invitrogen Corp | Use of multiple recombination sites with unique specificity in recombinational cloning |
| WO2001044459A2 (en) | 1999-12-15 | 2001-06-21 | Regents Of The University Of Minnesota | Method to enhance agrobacterium-mediated transformation of plants |
| AU2103601A (en) | 1999-12-17 | 2001-06-25 | Oregon Health And Science University | Methods for producing transgenic animals |
| BR0109269A (pt) | 2000-03-17 | 2002-12-17 | Benitec Australia Ltd | Construto genético e seu uso, célula de animal vertebrado, métodos de alteração do fenótipo de uma célula de animal vertebrado e de terapia genética em animal vertebrado, animal e animal murino geneticamente modificados |
| CA2402924A1 (en) | 2000-03-21 | 2001-09-27 | Charalambos Savakis | Method of generating transgenic organisms using transposons |
| US20030150007A1 (en) | 2000-03-21 | 2003-08-07 | Charalambos Savakis | Method of generating transgenic organisms using transposons |
| US7067308B1 (en) | 2000-03-28 | 2006-06-27 | Bioagri Corporation | Vector for genetically modifying non-human animals |
| US6589783B2 (en) | 2000-04-13 | 2003-07-08 | Novagen, Inc. | Multiple host expression vector |
| JP4510355B2 (ja) | 2000-05-01 | 2010-07-21 | ミッドウエスト リサーチ インスティチュート | 安定なチモモナスモビリスのキシロースおよびアラビノース醗酵株 |
| US7354755B2 (en) | 2000-05-01 | 2008-04-08 | Midwest Research Institute | Stable zymomonas mobilis xylose and arabinose fermenting strains |
| EP1156114A1 (en) | 2000-05-10 | 2001-11-21 | Europäisches Laboratorium für Molekularbiologie | Vectors for use in transponson-based DNA sequencing methods |
| JP2003535122A (ja) | 2000-06-02 | 2003-11-25 | ザイコス インク. | 生物活性物質のための送達システム |
| US20020028488A1 (en) | 2000-06-19 | 2002-03-07 | Sujay Singh | Transgenic avian species for making human and chimeric antibodies |
| JP2002078491A (ja) | 2000-06-22 | 2002-03-19 | National Institute Of Agrobiological Sciences | 青枯病菌由来の挿入配列因子 |
| US6852510B2 (en) | 2000-07-03 | 2005-02-08 | Gala Design Inc | Host cells containing multiple integrating vectors |
| US20020072097A1 (en) | 2000-07-07 | 2002-06-13 | Delcardayre Stephen | Molecular breeding of transposable elements |
| EA007958B1 (ru) | 2000-08-03 | 2007-02-27 | Терапеутик Хьюман Поликлоналз Инк. | ТРАНСГЕННЫЙ ВЕКТОР, СОДЕРЖАЩИЙ ГУМАНИЗИРОВАННЫЙ ЛОКУС Ig, И ЕГО ПРИМЕНЕНИЕ ДЛЯ ПОЛУЧЕНИЯ ТРАНСГЕННЫХ ЖИВОТНЫХ |
| GB2368064B (en) | 2000-09-30 | 2002-11-13 | Imp Cancer Res Tech | DNA Element and Associated Protein |
| US7105343B1 (en) | 2000-10-31 | 2006-09-12 | University Of Notre Dame Du Lac | Methods and compositions for transposition using minimal segments of the eukaryotic transformation vector Piggybac |
| US7067644B2 (en) | 2000-12-05 | 2006-06-27 | Wisconsin Alumni Research Foundation | Double transposition methods for manipulating nucleic acids |
| JP2002176880A (ja) | 2000-12-12 | 2002-06-25 | Kanegafuchi Chem Ind Co Ltd | 効率的な遺伝子導入鳥類の作製法及びそれによって得られる遺伝子導入鳥類 |
| US20020108132A1 (en) | 2001-02-02 | 2002-08-08 | Avigenics Inc. | Production of a monoclonal antibody by a transgenic chicken |
| JP2002238559A (ja) * | 2001-02-16 | 2002-08-27 | Nagoya Industrial Science Research Inst | 鳥類の卵内で外来遺伝子発現産物を生産する方法 |
| US20020119573A1 (en) | 2001-02-28 | 2002-08-29 | Shaw Karen J. | Footprinting plasmid |
| EP1478751A4 (en) | 2001-03-30 | 2005-10-19 | Avigenics Inc | LYSOZYM PROMOTER IN BIRDS |
| US7176300B2 (en) | 2001-03-30 | 2007-02-13 | Avigenics, Inc. | Avian lysozyme promoter |
| JP3723839B2 (ja) | 2001-06-07 | 2005-12-07 | 国立大学法人広島大学 | ニワトリの白血病阻止因子(lif)、及びそれをコードする遺伝子 |
| GB0119497D0 (en) | 2001-08-10 | 2001-10-03 | Viragen Inc | Expression of modified antibodies in avian cells |
| EP1451316B1 (en) | 2001-09-13 | 2014-08-06 | California Institute Of Technology | Method for producing transgenic birds |
| ATE513038T1 (de) | 2001-09-18 | 2011-07-15 | Synageva Biopharma Corp | Produktion eines transgenen vogels mittels cytoplasmainjektion |
| US20030061629A1 (en) | 2001-09-21 | 2003-03-27 | Pramod Sutrave | Production of transgenic birds using stage X primordial germ cells |
| AU2002341795A1 (en) | 2001-09-21 | 2003-04-01 | Avigenics, Inc. | Production of transgenic avians using sperm-mediated transfection |
| US20030143740A1 (en) * | 2001-10-15 | 2003-07-31 | Christine Wooddell | Processes for transposase mediated integration into mammalian cells |
| EP1446482A4 (en) | 2001-10-22 | 2006-03-01 | Athersys Inc | COMPOSITIONS AND METHODS FOR GENERATING MUTATIONS IN CELL LINES AND ANIMALS |
| US7972853B2 (en) | 2001-10-22 | 2011-07-05 | Abt Holding Company | Compositions and methods for making mutations in cell lines and animals |
| AU2002365184A1 (en) * | 2001-10-26 | 2003-07-30 | Id Biomedical Corporation Of Washington | Efficient protein expression system |
| US6875588B2 (en) | 2001-11-30 | 2005-04-05 | Avigenics, Inc. | Ovomucoid promoter and methods of use |
| US7294507B2 (en) | 2001-11-30 | 2007-11-13 | Avigenics, Inc. | Ovomucoid promoters and methods of use |
| US7335761B2 (en) | 2001-11-30 | 2008-02-26 | Avigenics, Inc. | Avian gene expression controlling regions |
| JP2005512598A (ja) | 2001-12-21 | 2005-05-12 | オックスフォード バイオメディカ (ユーケー) リミテッド | Eiavなどのレンチウイルス発現ベクターを使用するトランスジェニック生物の作製方法 |
| US20030121062A1 (en) | 2001-12-21 | 2003-06-26 | Oxford Biomedica (Uk) Limited | Transgenic organism |
| US7145057B2 (en) | 2002-02-01 | 2006-12-05 | Origen Therapeutics, Inc. | Chimeric bird from embryonic stem cells |
| US7323618B2 (en) | 2002-02-01 | 2008-01-29 | Origen Therapeutics, Inc. | Tissue specific expression of exogenous proteins in transgenic chickens |
| US7135562B2 (en) | 2002-03-14 | 2006-11-14 | University Of Cincinnati | Avian iFABP gene expression controlling region |
| US20030182675A1 (en) | 2002-03-22 | 2003-09-25 | Origen Therapeutics | Functional disruption of avian immunoglobulin genes |
| AU2003291614A1 (en) | 2002-05-17 | 2004-04-08 | New Horizons Diagnostics Corporation | Identification of a phage associated lytic enzyme to rapidly and specifically detect and kill bacillus anthracis |
| US20040172667A1 (en) | 2002-06-26 | 2004-09-02 | Cooper Richard K. | Administration of transposon-based vectors to reproductive organs |
| US20040235011A1 (en) | 2002-06-26 | 2004-11-25 | Cooper Richard K. | Production of multimeric proteins |
| US7527966B2 (en) | 2002-06-26 | 2009-05-05 | Transgenrx, Inc. | Gene regulation in transgenic animals using a transposon-based vector |
| WO2004009792A2 (en) | 2002-07-24 | 2004-01-29 | Vanderbilt University | Transposon-based vectors and methods of nucleic acid integration |
| US7700356B2 (en) | 2002-11-08 | 2010-04-20 | The United States Of America As Represented By The Secretary Of Agriculture | System for gene targeting and producing stable genomic transgene insertions |
| GB0227645D0 (en) | 2002-11-27 | 2003-01-08 | Viragen Inc | Protein production in transgenic avians |
| WO2004065581A2 (en) | 2003-01-15 | 2004-08-05 | Discovery Genomics, Inc. | Transposon-insulator element delivery systems |
| CN1980571A (zh) | 2003-01-24 | 2007-06-13 | 阿维季尼克斯股份有限公司 | 禽类及禽蛋中表达的外源蛋白质 |
| EP1594971B1 (en) | 2003-02-10 | 2011-02-02 | Max-Delbrück-Centrum für Molekulare Medizin (MDC) | Transposon-based targeting system |
| DK1594973T3 (da) | 2003-02-10 | 2012-02-13 | Max Delbrueck Centrum | Transposonbaseret målretningssystem |
| US20050198700A1 (en) | 2003-03-07 | 2005-09-08 | Avigenics, Inc. | Genomic modification |
| WO2004080162A2 (en) | 2003-03-07 | 2004-09-23 | Avigenics, Inc. | Integrase mediated avian transgenesis |
| US20040255345A1 (en) | 2003-03-07 | 2004-12-16 | Rapp Jeffrey C. | Production of transgenic avians |
| US20050034186A1 (en) | 2003-03-07 | 2005-02-10 | Harvey Alex J. | Site specific nucleic acid integration |
| US20050273873A1 (en) | 2003-03-07 | 2005-12-08 | Avigenics, Inc. | Genomic modification |
| WO2004092351A2 (en) | 2003-03-27 | 2004-10-28 | Avigenics, Inc. | Production of a transgenic avian by cytoplasmic injection |
| US7083980B2 (en) | 2003-04-17 | 2006-08-01 | Wisconsin Alumni Research Foundation | Tn5 transposase mutants and the use thereof |
| US7381712B2 (en) | 2003-05-09 | 2008-06-03 | Avigenics, Inc. | In vivo transfection in avians |
| US20050014932A1 (en) | 2003-05-15 | 2005-01-20 | Iogenetics, Llc | Targeted biocides |
| EP1633781A2 (en) | 2003-06-06 | 2006-03-15 | Avigenics, Inc. | Ovomucoid promoters and methods of use |
| AU2003252483A1 (en) | 2003-07-08 | 2005-01-21 | Japan Science And Technology Corporation | Method and system of constructing transgenic organism |
| US20060218852A1 (en) * | 2003-09-12 | 2006-10-05 | Graham David E | Controlling the formation of crystalline hydrates in fluid systems |
| US20080104723A1 (en) | 2003-11-21 | 2008-05-01 | Osaka Industrial Promojtion Organization C/O Mydom | Development of Mammalian Genome Modification Technique Using Retrotransposon |
| US8071364B2 (en) | 2003-12-24 | 2011-12-06 | Transgenrx, Inc. | Gene therapy using transposon-based vectors |
| US20060123504A1 (en) | 2004-12-07 | 2006-06-08 | Avigenics, Inc. | Methods of producing polyclonal antibodies |
| US7569223B2 (en) | 2004-03-22 | 2009-08-04 | The Rockefeller University | Phage-associated lytic enzymes for treatment of Streptococcus pneumoniae and related conditions |
| EP1812568A2 (en) | 2004-08-25 | 2007-08-01 | Avigenics, Inc. | Rna interference in avians |
| GB0419424D0 (en) | 2004-09-02 | 2004-10-06 | Viragen Scotland Ltd | Transgene optimisation |
| US20060160220A1 (en) | 2004-11-12 | 2006-07-20 | Iogenetics | Retroviral vectors with introns |
| WO2006055931A2 (en) | 2004-11-18 | 2006-05-26 | Stratatech Corporation | Vectors for stable gene expression |
| WO2006055040A2 (en) | 2004-11-19 | 2006-05-26 | Government Of The United States Of America, Department Of Health And Human Services | Identification of proteins in a genome |
| EP1819823A2 (en) | 2004-12-01 | 2007-08-22 | Bayer Schering Pharma Aktiengesellschaft | Generation of replication competent viruses for therapeutic use |
| US20060153800A1 (en) | 2004-12-14 | 2006-07-13 | Roland Buelow | DNA immunization with recombinase/transposase |
| WO2006093847A1 (en) | 2005-02-28 | 2006-09-08 | Avigenics, Inc. | Artificial chromosomes and transchromosomic avians |
| US7657816B2 (en) * | 2005-07-13 | 2010-02-02 | Leanics Corporation | Low-complexity hybrid LDPC code encoder |
-
2003
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- 2003-12-24 EP EP03800225A patent/EP1592789B1/en not_active Expired - Lifetime
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| EP1592789A4 (en) | 2006-09-13 |
| AU2003303831A1 (en) | 2004-08-23 |
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| EP1592789A2 (en) | 2005-11-09 |
| WO2004067706A2 (en) | 2004-08-12 |
| AU2003299959A1 (en) | 2004-08-23 |
| JP2006512922A (ja) | 2006-04-20 |
| ATE431849T1 (de) | 2009-06-15 |
| EP1592789B1 (en) | 2009-05-20 |
| US20080235813A1 (en) | 2008-09-25 |
| AU2003303830A8 (en) | 2004-08-23 |
| WO2004067706A3 (en) | 2004-12-23 |
| DE60327717D1 (de) | 2009-07-02 |
| AU2003303830A1 (en) | 2004-08-23 |
| US20040197910A1 (en) | 2004-10-07 |
| US7608451B2 (en) | 2009-10-27 |
| AU2003303831A8 (en) | 2004-08-23 |
| AU2003299959A8 (en) | 2004-08-23 |
| US7527966B2 (en) | 2009-05-05 |
| EP1597378A2 (en) | 2005-11-23 |
| WO2004067743A1 (en) | 2004-08-12 |
| WO2004067707A2 (en) | 2004-08-12 |
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