JP6850351B2 - 抗体のインビトロ糖鎖工学 - Google Patents
抗体のインビトロ糖鎖工学 Download PDFInfo
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- JP6850351B2 JP6850351B2 JP2019533340A JP2019533340A JP6850351B2 JP 6850351 B2 JP6850351 B2 JP 6850351B2 JP 2019533340 A JP2019533340 A JP 2019533340A JP 2019533340 A JP2019533340 A JP 2019533340A JP 6850351 B2 JP6850351 B2 JP 6850351B2
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- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/16—Extraction; Separation; Purification by chromatography
- C07K1/22—Affinity chromatography or related techniques based upon selective absorption processes
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
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- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/005—Glycopeptides, glycoproteins
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/40—Immunoglobulins specific features characterized by post-translational modification
- C07K2317/41—Glycosylation, sialylation, or fucosylation
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/52—Constant or Fc region; Isotype
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/55—Fab or Fab'
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| PCT/EP2017/083429 WO2018114877A1 (en) | 2016-12-21 | 2017-12-19 | In vitro glycoengineering of antibodies |
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| US6548640B1 (en) | 1986-03-27 | 2003-04-15 | Btg International Limited | Altered antibodies |
| AU600575B2 (en) | 1987-03-18 | 1990-08-16 | Sb2, Inc. | Altered antibodies |
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| US5770429A (en) | 1990-08-29 | 1998-06-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| WO1992009690A2 (en) | 1990-12-03 | 1992-06-11 | Genentech, Inc. | Enrichment method for variant proteins with altered binding properties |
| AU668505B2 (en) | 1991-03-18 | 1996-05-09 | Scripps Research Institute, The | Oligosaccharide enzyme substrates and inhibitors: methods and compositions |
| EP0590058B1 (en) | 1991-06-14 | 2003-11-26 | Genentech, Inc. | HUMANIZED Heregulin ANTIBODy |
| WO1993006217A1 (en) | 1991-09-19 | 1993-04-01 | Genentech, Inc. | EXPRESSION IN E. COLI OF ANTIBODY FRAGMENTS HAVING AT LEAST A CYSTEINE PRESENT AS A FREE THIOL, USE FOR THE PRODUCTION OF BIFUNCTIONAL F(ab')2 ANTIBODIES |
| WO1993008829A1 (en) | 1991-11-04 | 1993-05-13 | The Regents Of The University Of California | Compositions that mediate killing of hiv-infected cells |
| US5789199A (en) | 1994-11-03 | 1998-08-04 | Genentech, Inc. | Process for bacterial production of polypeptides |
| US5840523A (en) | 1995-03-01 | 1998-11-24 | Genetech, Inc. | Methods and compositions for secretion of heterologous polypeptides |
| US5731168A (en) | 1995-03-01 | 1998-03-24 | Genentech, Inc. | Method for making heteromultimeric polypeptides |
| US6267958B1 (en) | 1995-07-27 | 2001-07-31 | Genentech, Inc. | Protein formulation |
| WO1998033523A1 (en) | 1997-01-31 | 1998-08-06 | Biovation Limited | Vaccination methods and molecules |
| ES2258817T3 (es) | 1997-05-21 | 2006-09-01 | Biovation Limited | Metodo para la produccion de proteinas no inmunogenas. |
| US6171586B1 (en) | 1997-06-13 | 2001-01-09 | Genentech, Inc. | Antibody formulation |
| US6040498A (en) | 1998-08-11 | 2000-03-21 | North Caroline State University | Genetically engineered duckweed |
| US6610833B1 (en) | 1997-11-24 | 2003-08-26 | The Institute For Human Genetics And Biochemistry | Monoclonal human natural antibodies |
| JP4460155B2 (ja) | 1997-12-05 | 2010-05-12 | ザ・スクリプス・リサーチ・インステイチユート | マウス抗体のヒト化 |
| ATE352559T1 (de) | 1998-12-08 | 2007-02-15 | Biovation Ltd | Verfahren zur verminderung der immunogenität von proteinen |
| JP2003512821A (ja) | 1999-10-04 | 2003-04-08 | メディカゴ インコーポレイテッド | 外来性遺伝子の転写調節方法 |
| US7125978B1 (en) | 1999-10-04 | 2006-10-24 | Medicago Inc. | Promoter for regulating expression of foreign genes |
| US20030180714A1 (en) | 1999-12-15 | 2003-09-25 | Genentech, Inc. | Shotgun scanning |
| DK1272647T3 (en) | 2000-04-11 | 2014-12-15 | Genentech Inc | Multivalent antibodies and uses thereof |
| US6596541B2 (en) | 2000-10-31 | 2003-07-22 | Regeneron Pharmaceuticals, Inc. | Methods of modifying eukaryotic cells |
| DK1354034T3 (da) | 2000-11-30 | 2008-03-25 | Medarex Inc | Transgene transchromosomale gnavere til fremstilling af humane antistoffer |
| CA2488441C (en) | 2002-06-03 | 2015-01-27 | Genentech, Inc. | Synthetic antibody phage libraries |
| US20050079574A1 (en) | 2003-01-16 | 2005-04-14 | Genentech, Inc. | Synthetic antibody phage libraries |
| US7871607B2 (en) | 2003-03-05 | 2011-01-18 | Halozyme, Inc. | Soluble glycosaminoglycanases and methods of preparing and using soluble glycosaminoglycanases |
| US20060104968A1 (en) | 2003-03-05 | 2006-05-18 | Halozyme, Inc. | Soluble glycosaminoglycanases and methods of preparing and using soluble glycosaminogly ycanases |
| EP1460425A1 (en) * | 2003-03-17 | 2004-09-22 | Boehringer Mannheim Gmbh | Deglycosylated enzymes for conjugates |
| CA2561686C (en) | 2004-03-31 | 2014-12-02 | Genentech, Inc. | Humanized anti-tgf-beta antibodies |
| US7785903B2 (en) | 2004-04-09 | 2010-08-31 | Genentech, Inc. | Variable domain library and uses |
| WO2005111627A2 (en) | 2004-04-15 | 2005-11-24 | Massachusetts Institute Of Technology | Methods and products related to the improved analysis of carbohydrates |
| US20060127950A1 (en) | 2004-04-15 | 2006-06-15 | Massachusetts Institute Of Technology | Methods and products related to the improved analysis of carbohydrates |
| TWI380996B (zh) | 2004-09-17 | 2013-01-01 | Hoffmann La Roche | 抗ｏｘ４０ｌ抗體 |
| JO3000B1 (ar) | 2004-10-20 | 2016-09-05 | Genentech Inc | مركبات أجسام مضادة . |
| EP2465870A1 (en) | 2005-11-07 | 2012-06-20 | Genentech, Inc. | Binding polypeptides with diversified and consensus VH/VL hypervariable sequences |
| US20070237764A1 (en) | 2005-12-02 | 2007-10-11 | Genentech, Inc. | Binding polypeptides with restricted diversity sequences |
| WO2007134050A2 (en) | 2006-05-09 | 2007-11-22 | Genentech, Inc. | Binding polypeptides with optimized scaffolds |
| TW200813086A (en) | 2006-05-11 | 2008-03-16 | Hoffmann La Roche | Immunereconstituted mouse |
| ES2399075T3 (es) | 2006-08-30 | 2013-03-25 | Genentech, Inc. | Anticuerpos multiespecíficos |
| CN100592373C (zh) | 2007-05-25 | 2010-02-24 | 群康科技(深圳)有限公司 | 液晶显示面板驱动装置及其驱动方法 |
| RU2010112236A (ru) * | 2007-08-31 | 2011-10-10 | Ф.Хоффманн-Ля Рош Аг (Ch) | Анализ профиля гликозилирования |
| US9266967B2 (en) | 2007-12-21 | 2016-02-23 | Hoffmann-La Roche, Inc. | Bivalent, bispecific antibodies |
| US20090162359A1 (en) | 2007-12-21 | 2009-06-25 | Christian Klein | Bivalent, bispecific antibodies |
| US8242247B2 (en) | 2007-12-21 | 2012-08-14 | Hoffmann-La Roche Inc. | Bivalent, bispecific antibodies |
| US8227577B2 (en) | 2007-12-21 | 2012-07-24 | Hoffman-La Roche Inc. | Bivalent, bispecific antibodies |
| PT2235064E (pt) | 2008-01-07 | 2016-03-01 | Amgen Inc | Método de preparação de moléculas heterodiméricas de fc de anticorpos utilizando efeitos de indução eletrostática |
| BRPI1014089A2 (pt) | 2009-04-02 | 2016-04-19 | Roche Glycart Ag | anticorpos multiespecíficos que compreendem anticorpos de comprimento completo e fragmentos fab de cadeia simples |
| DK2417156T3 (en) | 2009-04-07 | 2015-03-02 | Roche Glycart Ag | Trivalent, bispecific antibodies |
| RU2570633C2 (ru) | 2009-05-27 | 2015-12-10 | Ф.Хоффманн-Ля Рош Аг | Три- или тетраспецифические антитела |
| US9676845B2 (en) | 2009-06-16 | 2017-06-13 | Hoffmann-La Roche, Inc. | Bispecific antigen binding proteins |
| US8703132B2 (en) | 2009-06-18 | 2014-04-22 | Hoffmann-La Roche, Inc. | Bispecific, tetravalent antigen binding proteins |
| AU2010278290A1 (en) | 2009-07-30 | 2012-02-09 | F. Hoffmann-La Roche Ag | Enzymatic antibody processing |
| US10087236B2 (en) | 2009-12-02 | 2018-10-02 | Academia Sinica | Methods for modifying human antibodies by glycan engineering |
| WO2012037407A1 (en) † | 2010-09-17 | 2012-03-22 | Prozyme, Inc. | Isolation and deglycosylation of glycoproteins |
| AU2012351751B2 (en) * | 2011-10-19 | 2017-09-07 | Novimmune S.A. | Methods of purifying antibodies |
| BR112014019825B1 (pt) * | 2012-02-10 | 2021-08-24 | University Of Maryland, Baltimore | Glicoengenharia quimioenzimática de anticorpos e fragmentos fc dos mesmos |
| WO2015123754A1 (en) | 2014-02-18 | 2015-08-27 | The University Of Manitoba | Methods to produce single glycoform antibodies |
| CN114181312A (zh) | 2014-09-10 | 2022-03-15 | 豪夫迈·罗氏有限公司 | 半乳糖改造的免疫球蛋白1抗体 |
| JP6850351B2 (ja) | 2016-12-21 | 2021-03-31 | エフ．ホフマン−ラ ロシュ アーゲーＦ． Ｈｏｆｆｍａｎｎ−Ｌａ Ｒｏｃｈｅ Ａｋｔｉｅｎｇｅｓｅｌｌｓｃｈａｆｔ | 抗体のインビトロ糖鎖工学 |
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| AU2017384276B9 (en) | 2020-11-26 |
| AU2017384276B2 (en) | 2020-07-02 |
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| US20240101643A1 (en) | 2024-03-28 |
| EP3559248A1 (en) | 2019-10-30 |
| CN110088291A (zh) | 2019-08-02 |
| WO2018114877A1 (en) | 2018-06-28 |
| TW201835333A (zh) | 2018-10-01 |
| EP3559248B1 (en) | 2021-11-17 |
| IL267351A (en) | 2019-08-29 |
| EP3559248B2 (en) | 2024-11-20 |
| AU2017384276A1 (en) | 2019-05-30 |
| KR102317884B1 (ko) | 2021-10-26 |
| CA3044920C (en) | 2022-06-28 |
| TWI780097B (zh) | 2022-10-11 |
| US20200165320A1 (en) | 2020-05-28 |
| MX2019006266A (es) | 2019-08-21 |
| BR112019010485A2 (pt) | 2019-09-10 |
| CN119685431A (zh) | 2025-03-25 |
| CA3044920A1 (en) | 2018-06-28 |
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