MX2008013363A - Metodos y composiciones basados en la proteina tipo 1 de la toxina shiga. - Google Patents
Metodos y composiciones basados en la proteina tipo 1 de la toxina shiga.Info
- Publication number
- MX2008013363A MX2008013363A MX2008013363A MX2008013363A MX2008013363A MX 2008013363 A MX2008013363 A MX 2008013363A MX 2008013363 A MX2008013363 A MX 2008013363A MX 2008013363 A MX2008013363 A MX 2008013363A MX 2008013363 A MX2008013363 A MX 2008013363A
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- Prior art keywords
- antibody
- stxl
- polypeptide
- seq
- protein
- Prior art date
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Classifications
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- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/24—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia
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- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
- A61K39/39533—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals
- A61K39/3955—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals against proteinaceous materials, e.g. enzymes, hormones, lymphokines
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
- C07K16/1203—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria
- C07K16/1228—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
- C07K16/1203—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria
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- C07K16/1232—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia from Escherichia (G)
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
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- A—HUMAN NECESSITIES
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- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
Landscapes
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| PCT/US2007/009799 WO2007124133A2 (en) | 2006-04-20 | 2007-04-20 | Methods and compositions based on shiga toxin type 1 protein |
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| MX2008013363A MX2008013363A (es) | 2006-04-20 | 2007-04-20 | Metodos y composiciones basados en la proteina tipo 1 de la toxina shiga. |
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| WO (1) | WO2007124133A2 (cg-RX-API-DMAC7.html) |
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| US20030170248A1 (en) * | 1997-12-23 | 2003-09-11 | Jeffrey R. Stinson | Humanized monoclonal antibodies that protect against shiga toxin induced disease |
| EP1229045A1 (en) * | 2001-02-01 | 2002-08-07 | Institut Curie | Universal carrier for targeting molecules to Gb3 receptor expressing cells |
| AU2007240614B2 (en) | 2006-04-20 | 2013-09-12 | The Henry M. Jackson Foundation For The Advancement Of Military Medicine Incorporated | Methods and compositions based on Shiga toxin type 1 protein |
| US20090258010A1 (en) * | 2006-05-31 | 2009-10-15 | Thallion Pharmaceuticals, Inc. | Methods, compositions, and kits for treating shiga toxin associated conditions |
| PE20120425A1 (es) * | 2009-01-23 | 2012-05-03 | Jackson H M Found Military Med | Metodos y composiciones en base a la proteina tipo 2 de la toxina shiga |
| US8734811B2 (en) * | 2009-04-06 | 2014-05-27 | University Of Saskatchewan | Methods and compositions for treating and preventing Shiga toxin-producing Escherichia coli infection |
| AU2014285024A1 (en) * | 2013-07-03 | 2016-01-21 | Roka Bioscience, Inc. | Compositions, kits, and related methods for detecting and/or monitoring Shiga toxin producing Escherichia coli |
| CN104558167B (zh) * | 2014-12-26 | 2017-12-26 | 江苏省疾病预防控制中心 | 检测i型志贺毒素双抗夹心法酶联免疫试剂盒及其应用 |
| CN111902539B (zh) * | 2018-02-07 | 2025-05-16 | 吉尼松公司 | 杂合调控元件 |
| RU2732155C1 (ru) * | 2019-09-24 | 2020-09-11 | Открытое акционерное общество "Всероссийский научный Центр молекулярной диагностики и лечения" (ОАО ВНЦМДЛ) | Гуманизированное антитело или его антигенсвязывающий фрагмент (Fab) против шига-токсинов первого и/или второго типов (варианты), композиция для лечения токсических состояний, вызванных энтерогеморрагической кишечной палочкой, содержащая указанные антитела и/или Fab |
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| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| JPS6147500A (ja) | 1984-08-15 | 1986-03-07 | Res Dev Corp Of Japan | キメラモノクロ−ナル抗体及びその製造法 |
| EP0173494A3 (en) | 1984-08-27 | 1987-11-25 | The Board Of Trustees Of The Leland Stanford Junior University | Chimeric receptors by dna splicing and expression |
| GB8422238D0 (en) | 1984-09-03 | 1984-10-10 | Neuberger M S | Chimeric proteins |
| US4573986A (en) * | 1984-09-17 | 1986-03-04 | The Procter & Gamble Company | Disposable waste-containment garment |
| JPS61134325A (ja) | 1984-12-04 | 1986-06-21 | Teijin Ltd | ハイブリツド抗体遺伝子の発現方法 |
| WO1987002671A1 (en) | 1985-11-01 | 1987-05-07 | International Genetic Engineering, Inc. | Modular assembly of antibody genes, antibodies prepared thereby and use |
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| JPS62292890A (ja) | 1986-06-13 | 1987-12-19 | Sanritsu Kikaku Kk | 固形潤滑材 |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| US5258498A (en) | 1987-05-21 | 1993-11-02 | Creative Biomolecules, Inc. | Polypeptide linkers for production of biosynthetic proteins |
| US5164298A (en) * | 1988-06-24 | 1992-11-17 | Hsc Research Development Corporation | Verocytotoxin receptor assay |
| GB8823869D0 (en) | 1988-10-12 | 1988-11-16 | Medical Res Council | Production of antibodies |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US6150584A (en) | 1990-01-12 | 2000-11-21 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US6657103B1 (en) | 1990-01-12 | 2003-12-02 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| WO1992003918A1 (en) | 1990-08-29 | 1992-03-19 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US6255458B1 (en) | 1990-08-29 | 2001-07-03 | Genpharm International | High affinity human antibodies and human antibodies against digoxin |
| WO1994004679A1 (en) | 1991-06-14 | 1994-03-03 | Genentech, Inc. | Method for making humanized antibodies |
| IE922437A1 (en) | 1991-07-25 | 1993-01-27 | Idec Pharma Corp | Recombinant antibodies for human therapy |
| JP3939746B2 (ja) | 1991-07-25 | 2007-07-04 | バイオジェン・アイデック・インコーポレイテッド | 細胞毒性ｔ−リンパ球応答の誘導 |
| US5709860A (en) | 1991-07-25 | 1998-01-20 | Idec Pharmaceuticals Corporation | Induction of cytotoxic T-lymphocyte responses |
| US5756096A (en) | 1991-07-25 | 1998-05-26 | Idec Pharmaceuticals Corporation | Recombinant antibodies for human therapy |
| CA2078539C (en) * | 1991-09-18 | 2005-08-02 | Kenya Shitara | Process for producing humanized chimera antibody |
| NZ255101A (en) | 1992-07-24 | 1997-08-22 | Cell Genesys Inc | A yeast artificial chromosome (yac) vector containing an hprt minigene expressible in murine stem cells and genetically modified rodent therefor |
| US5747272A (en) * | 1994-02-14 | 1998-05-05 | Henry M. Jackson Foundation For The Advancement Of Military Medicine | Detection of shiga-like toxins of enterohemoragic Escherichia coli |
| US5968894A (en) * | 1994-02-22 | 1999-10-19 | Lingwood; Clifford A. | Verotoxin pharmaceutical compositions and medical treatments therewith |
| ATE483733T1 (de) | 1995-06-14 | 2010-10-15 | Univ California | Hochaffine humane antikörper gegen tumorantigene |
| CA2265887A1 (en) * | 1996-09-10 | 1998-03-19 | Henry M. Jackson Foundation For The Advancement Of Military Medicine | Histidine-tagged shiga toxins, toxoids, and protein fusions with such toxins and toxoids, methods for the purification and preparation thereof |
| WO1998020903A1 (en) * | 1996-11-15 | 1998-05-22 | Trustees Of Tufts College | Humanized neutralizing antibodies against hemolytic uremic syndrome |
| US7910096B2 (en) * | 1996-11-15 | 2011-03-22 | Trustees Of Tufts College | Human neutralizing antibodies against hemolytic uremic syndrome |
| US20020160005A1 (en) * | 1996-11-15 | 2002-10-31 | Trustees Of Tufts College | Human neutralizing antibodies against hemolytic urmec syndrome |
| US20030170248A1 (en) * | 1997-12-23 | 2003-09-11 | Jeffrey R. Stinson | Humanized monoclonal antibodies that protect against shiga toxin induced disease |
| KR100548167B1 (ko) | 1998-05-20 | 2006-01-31 | 데이진 가부시키가이샤 | 베로톡신 ⅱ를 인식하는 인체 적응된 항체 및 그것을 생산하는 세포주 |
| JP2002529695A (ja) * | 1998-10-30 | 2002-09-10 | フォトニック センサー システムズ | 酸または塩基を検出または測定するための方法およびセンサ |
| US6833268B1 (en) | 1999-06-10 | 2004-12-21 | Abgenix, Inc. | Transgenic animals for producing specific isotypes of human antibodies via non-cognate switch regions |
| EP1648501B1 (en) * | 2003-07-21 | 2011-04-06 | Intervet International BV | Hybrid toxins comprising shiga-like toxin subunits fused to escherichia coli heat labile enterotoxin subunits and vaccines thereof |
| JP5618453B2 (ja) | 2003-11-28 | 2014-11-05 | ナショナル リサーチ カウンシル オブ カナダ | 抗癌抗体およびその使用 |
| CA2555306A1 (en) * | 2004-02-06 | 2005-08-18 | Nymox Corporation | Humanized antibody |
| US8846058B2 (en) * | 2006-02-16 | 2014-09-30 | The Henry M. Jackson Foundation For The Advancement Of Military Medicine, Inc. | Shiga toxoid chimeric proteins |
| AU2007240614B2 (en) | 2006-04-20 | 2013-09-12 | The Henry M. Jackson Foundation For The Advancement Of Military Medicine Incorporated | Methods and compositions based on Shiga toxin type 1 protein |
| US20090258010A1 (en) * | 2006-05-31 | 2009-10-15 | Thallion Pharmaceuticals, Inc. | Methods, compositions, and kits for treating shiga toxin associated conditions |
| WO2008080218A1 (en) | 2006-12-29 | 2008-07-10 | Osprey Pharmaceuticals Usa, Inc. | Methods of selecting and producing modified toxins, conjugates containing modified toxins and uses thereof |
| PE20120425A1 (es) | 2009-01-23 | 2012-05-03 | Jackson H M Found Military Med | Metodos y composiciones en base a la proteina tipo 2 de la toxina shiga |
-
2007
- 2007-04-20 AU AU2007240614A patent/AU2007240614B2/en not_active Ceased
- 2007-04-20 WO PCT/US2007/009799 patent/WO2007124133A2/en not_active Ceased
- 2007-04-20 US US11/788,546 patent/US8293245B2/en active Active
- 2007-04-20 EP EP11179552A patent/EP2420246A1/en not_active Withdrawn
- 2007-04-20 EP EP07775978A patent/EP2019684A4/en not_active Withdrawn
- 2007-04-20 JP JP2009506629A patent/JP2009536818A/ja active Pending
- 2007-04-20 MX MX2008013363A patent/MX2008013363A/es not_active Application Discontinuation
- 2007-04-20 CA CA002646319A patent/CA2646319A1/en not_active Abandoned
-
2012
- 2012-10-05 US US13/645,928 patent/US20130101591A1/en not_active Abandoned
-
2013
- 2013-10-02 US US14/044,580 patent/US20140023652A1/en not_active Abandoned
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|---|---|
| AU2007240614A1 (en) | 2007-11-01 |
| WO2007124133A2 (en) | 2007-11-01 |
| EP2420246A1 (en) | 2012-02-22 |
| JP2009536818A (ja) | 2009-10-22 |
| US20070292426A1 (en) | 2007-12-20 |
| WO2007124133A3 (en) | 2008-11-27 |
| US20140023652A1 (en) | 2014-01-23 |
| US8293245B2 (en) | 2012-10-23 |
| AU2007240614B2 (en) | 2013-09-12 |
| CA2646319A1 (en) | 2007-11-01 |
| US20130101591A1 (en) | 2013-04-25 |
| EP2019684A2 (en) | 2009-02-04 |
| EP2019684A4 (en) | 2009-08-26 |
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| FA | Abandonment or withdrawal |