DK2632479T3 - FVIII PEPTIDES FOR IMMUNT TOLERANCE INDUCTION AND IMMUNODIAGNOSTICS - Google Patents
FVIII PEPTIDES FOR IMMUNT TOLERANCE INDUCTION AND IMMUNODIAGNOSTICS Download PDFInfo
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- DK2632479T3 DK2632479T3 DK11796846.1T DK11796846T DK2632479T3 DK 2632479 T3 DK2632479 T3 DK 2632479T3 DK 11796846 T DK11796846 T DK 11796846T DK 2632479 T3 DK2632479 T3 DK 2632479T3
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Landscapes
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| US40740210P | 2010-10-27 | 2010-10-27 | |
| US201161467894P | 2011-03-25 | 2011-03-25 | |
| US201161502476P | 2011-06-29 | 2011-06-29 | |
| PCT/US2011/058165 WO2012058480A1 (en) | 2010-10-27 | 2011-10-27 | Fviii peptides for immune tolerance induction and immunodiagnostics |
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| DK2632479T3 true DK2632479T3 (en) | 2017-08-07 |
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| DK11796846.1T DK2632479T3 (en) | 2010-10-27 | 2011-10-27 | FVIII PEPTIDES FOR IMMUNT TOLERANCE INDUCTION AND IMMUNODIAGNOSTICS |
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| WO2006063031A2 (en) | 2004-12-06 | 2006-06-15 | Haplomics | Allelic variants of human factor viii |
| PL2917232T3 (pl) * | 2012-11-12 | 2017-09-29 | Apitope International Nv | Pochodzące od czynnika VIII peptydy do zastosowania w leczeniu hemofilii A |
| US10272163B2 (en) | 2012-12-07 | 2019-04-30 | The Regents Of The University Of California | Factor VIII mutation repair and tolerance induction |
| EP2968499A4 (en) * | 2013-03-15 | 2016-11-30 | Haplomics Inc | COMPOSITIONS AND METHODS FOR THE IMMUNO-TOLERANCE INDUCTION FOR FACTOR VIII SPATIAL THERAPIES IN PERSONS WITH HEMOPHILIA A |
| WO2015192101A1 (en) * | 2014-06-12 | 2015-12-17 | University Of Hawaii | Uses of humanized cobra venom factor for reducing or preventing immunogenicity |
| CA2973529A1 (en) * | 2015-01-26 | 2016-08-04 | Cellectis | Cll1-specific multi-chain chimeric antigen receptor |
| SG11201808475XA (en) | 2016-04-15 | 2018-10-30 | Baxalta Inc | Method and apparatus for providing a pharmacokinetic drug dosing regiment |
| US10896749B2 (en) | 2017-01-27 | 2021-01-19 | Shire Human Genetic Therapies, Inc. | Drug monitoring tool |
Family Cites Families (11)
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| JP2005538694A (ja) * | 2002-04-18 | 2005-12-22 | メルク パテント ゲゼルシャフト ミット ベシュレンクテル ハフトング | 修飾されたｖｉｉｉ因子 |
| US7485314B2 (en) * | 2002-05-06 | 2009-02-03 | Los Angeles Biomedical Research Institute At Harbor-Ucla Medical Center | Induction of antigen specific immunologic tolerance |
| WO2005114221A2 (en) * | 2004-05-21 | 2005-12-01 | The Institute For Systems Biology | Compositions and methods for quantification of serum glycoproteins |
| US20060094104A1 (en) | 2004-10-29 | 2006-05-04 | Leopold Grillberger | Animal protein-free media for cultivation of cells |
| ES2474573T3 (es) | 2006-01-04 | 2014-07-09 | Baxter International Inc | Medio de cultivo celular sin oligop�ptidos |
| GB0723712D0 (en) | 2007-12-04 | 2008-01-16 | Apitope Technology Bristol Ltd | Peptides |
| US7673687B2 (en) | 2007-12-05 | 2010-03-09 | Halliburton Energy Services, Inc. | Cement compositions comprising crystalline organic materials and methods of using same |
| DE202007017320U1 (de) | 2007-12-07 | 2008-02-28 | Dittmann, Ludwig | Vorrichtung zur Raumbeduftung |
| GB0801513D0 (en) * | 2008-01-28 | 2008-03-05 | Circassia Ltd | Peptides from factor VIII |
| US20110081362A1 (en) | 2008-01-31 | 2011-04-07 | The Brigham And Women's Hospital, Inc. | Treatment of cancer |
| US20100168018A1 (en) | 2008-11-07 | 2010-07-01 | Baxter International Inc. | Factor viii formulations |
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