ES2388932T3 - Polipéptidos de unión y usos de los mismos - Google Patents
Polipéptidos de unión y usos de los mismos Download PDFInfo
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- ES2388932T3 ES2388932T3 ES06849911T ES06849911T ES2388932T3 ES 2388932 T3 ES2388932 T3 ES 2388932T3 ES 06849911 T ES06849911 T ES 06849911T ES 06849911 T ES06849911 T ES 06849911T ES 2388932 T3 ES2388932 T3 ES 2388932T3
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| US74218505P | 2005-12-02 | 2005-12-02 | |
| US742185P | 2005-12-02 | ||
| US80555306P | 2006-06-22 | 2006-06-22 | |
| US805553P | 2006-06-22 | ||
| PCT/US2006/046046 WO2007094842A2 (en) | 2005-12-02 | 2006-12-01 | Binding polypeptides and uses thereof |
Publications (1)
| Publication Number | Publication Date |
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| ES2388932T3 true ES2388932T3 (es) | 2012-10-19 |
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| ES06849911T Active ES2388932T3 (es) | 2005-12-02 | 2006-12-01 | Polipéptidos de unión y usos de los mismos |
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| US (1) | US8957187B2 (enExample) |
| EP (1) | EP1957540B1 (enExample) |
| JP (1) | JP5808070B2 (enExample) |
| KR (1) | KR101434682B1 (enExample) |
| AU (1) | AU2006338198B2 (enExample) |
| CA (1) | CA2631327C (enExample) |
| ES (1) | ES2388932T3 (enExample) |
| RU (1) | RU2470941C2 (enExample) |
| WO (1) | WO2007094842A2 (enExample) |
| ZA (1) | ZA200805045B (enExample) |
Families Citing this family (34)
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|---|---|---|---|---|
| ES2577292T3 (es) | 2005-11-07 | 2016-07-14 | Genentech, Inc. | Polipéptidos de unión con secuencias hipervariables de VH/VL diversificadas y consenso |
| US20070237764A1 (en) * | 2005-12-02 | 2007-10-11 | Genentech, Inc. | Binding polypeptides with restricted diversity sequences |
| US8877688B2 (en) | 2007-09-14 | 2014-11-04 | Adimab, Llc | Rationally designed, synthetic antibody libraries and uses therefor |
| CN101855242B (zh) * | 2007-09-14 | 2014-07-30 | 阿迪马布有限责任公司 | 合理设计的合成抗体文库及其用途 |
| EP2889370A1 (en) | 2007-12-11 | 2015-07-01 | The Scripps Research Institute | In vivo unnatural amino acid expression in the methylotrophic yeast Pichia pastoris |
| US9102711B2 (en) | 2007-12-31 | 2015-08-11 | Xoma Technology Ltd. | Methods and materials for targeted mutagenesis |
| JP5487570B2 (ja) * | 2008-07-09 | 2014-05-07 | 富士フイルム株式会社 | 抗体と蛋白質との融合蛋白質の製造方法 |
| AU2009274129B2 (en) * | 2008-07-21 | 2016-02-25 | Immunomedics Inc. | Structural variants of antibodies for improved therapeutic characteristics |
| UA112050C2 (uk) * | 2008-08-04 | 2016-07-25 | БАЄР ХЕЛСКЕР ЛЛСі | Терапевтична композиція, що містить моноклональне антитіло проти інгібітора шляху тканинного фактора (tfpi) |
| WO2010019565A2 (en) * | 2008-08-12 | 2010-02-18 | Medlmmune, Llc | Anti-ephrin b2 antibodies and their use in treatment of disease |
| CN102753193A (zh) | 2008-10-31 | 2012-10-24 | 比奥根艾迪克Ma公司 | Light靶向分子及其用途 |
| WO2010068278A2 (en) * | 2008-12-10 | 2010-06-17 | The Scripps Research Institute | Production of carrier-peptide conjugates using chemically reactive unnatural amino acids |
| US20090197339A1 (en) * | 2008-12-10 | 2009-08-06 | The Scripps Research Institute | In vivo unnatural amino acid expression in the methylotrophic yeast pichia pastoris |
| JP5756802B2 (ja) | 2009-08-13 | 2015-07-29 | クリスタル バイオサイエンス インク．Ｃｒｙｓｔａｌ Ｂｉｏｓｃｉｅｎｃｅ Ｉｎｃ． | 最小ｃｄｒを有する抗体を産生するトランスジェニック動物 |
| CA2775350A1 (en) * | 2009-09-24 | 2011-03-31 | Seattle Genetics, Inc. | Dr5 ligand drug conjugates |
| WO2011084496A1 (en) * | 2009-12-16 | 2011-07-14 | Abbott Biotherapeutics Corp. | Anti-her2 antibodies and their uses |
| AU2011223710B2 (en) | 2010-03-01 | 2016-04-14 | Bayer Healthcare Llc | Optimized monoclonal antibodies against tissue factor pathway inhibitor (TFPI) |
| FR2959994B1 (fr) * | 2010-05-12 | 2012-08-24 | Lfb Biotechnologies | Nouveaux anticorps humanises 12g4 mutes et leurs fragments diriges contre le recepteur humain de l'hormone anti-mullerienne de type ii |
| NZ701444A (en) | 2010-08-27 | 2016-06-24 | Gilead Biologics Inc | Antibodies to matrix metalloproteinase 9 |
| US20140121123A1 (en) * | 2010-10-29 | 2014-05-01 | Kevin Caili Wang | Methods for diversifying antibodies, antibodies derived therefrom and uses thereof |
| CA2826142A1 (en) * | 2011-02-03 | 2012-08-09 | Xoma Technology Ltd. | Methods and materials for enhancing functional protein expression in bacteria |
| EP2699586B1 (en) * | 2011-04-21 | 2019-03-06 | Ology Bioservices, Inc. | Methods for isolating and quantifying antigen from vaccines |
| ES2925799T3 (es) * | 2011-04-28 | 2022-10-19 | Univ Leland Stanford Junior | Identificación de polinucleótidos asociados a una muestra |
| MD20140107A2 (ro) * | 2012-02-29 | 2015-03-31 | Gilead Biologics, Inc. | Anticorpi împotriva metaloproteinazei 9 din matrice |
| WO2013130905A1 (en) * | 2012-02-29 | 2013-09-06 | Gilead Biologics, Inc. | Antibodies to matrix metalloproteinase 9 |
| KR101505157B1 (ko) * | 2012-05-08 | 2015-03-24 | 주식회사 종근당 | 항―ＥｒｂＢ２ 항체 변이체 |
| WO2016007625A1 (en) * | 2014-07-08 | 2016-01-14 | Tdw Group | Antibodies to argininosuccinate synthase and related methods |
| US11254738B2 (en) * | 2016-09-07 | 2022-02-22 | The Governing Council Of The University Of Toronto Banting Institute | Synthetic antibodies against VEGF and their uses |
| CN106946990B (zh) * | 2017-02-23 | 2021-02-23 | 南昌大佳科技有限公司 | 一种针对c-Myc标签的纳米抗体 |
| KR102344616B1 (ko) | 2017-05-30 | 2021-12-31 | 더 보드 오브 리젠츠 오브 더 유니버시티 오브 오클라호마 | 항-더블코르틴-유사 키나제 1 항체 및 사용 방법 |
| EP3720481A4 (en) | 2017-12-04 | 2021-10-13 | Coare Holdings, Inc. | ANTI-DCLK1 ANTIBODIES AND CHIMERA ANTIGEN RECEPTORS AND COMPOSITIONS AND METHODS OF USING THEREOF |
| CN109627319B (zh) * | 2019-01-11 | 2022-06-21 | 北京协同创新研究院 | 一种抗her-2的重链抗体及其应用 |
| AU2020368789B2 (en) | 2019-10-16 | 2024-01-18 | Naturesense Co., Ltd. | Peptide for improving memory and preventing or alleviating cognitive impairment, composition containing same and preparation method therefor |
| KR102107808B1 (ko) * | 2019-11-12 | 2020-05-07 | 주식회사 네이처센스 농업회사법인 | 기억력 및 인지기능 개선용 펩타이드 |
Family Cites Families (110)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3773919A (en) * | 1969-10-23 | 1973-11-20 | Du Pont | Polylactide-drug mixtures |
| US3896111A (en) * | 1973-02-20 | 1975-07-22 | Research Corp | Ansa macrolides |
| US4151042A (en) * | 1977-03-31 | 1979-04-24 | Takeda Chemical Industries, Ltd. | Method for producing maytansinol and its derivatives |
| US4137230A (en) * | 1977-11-14 | 1979-01-30 | Takeda Chemical Industries, Ltd. | Method for the production of maytansinoids |
| USRE30985E (en) * | 1978-01-01 | 1982-06-29 | Serum-free cell culture media | |
| US4265814A (en) * | 1978-03-24 | 1981-05-05 | Takeda Chemical Industries | Matansinol 3-n-hexadecanoate |
| US4307016A (en) * | 1978-03-24 | 1981-12-22 | Takeda Chemical Industries, Ltd. | Demethyl maytansinoids |
| JPS5562090A (en) * | 1978-10-27 | 1980-05-10 | Takeda Chem Ind Ltd | Novel maytansinoid compound and its preparation |
| JPS5566585A (en) * | 1978-11-14 | 1980-05-20 | Takeda Chem Ind Ltd | Novel maytansinoid compound and its preparation |
| US4256746A (en) * | 1978-11-14 | 1981-03-17 | Takeda Chemical Industries | Dechloromaytansinoids, their pharmaceutical compositions and method of use |
| JPS55164687A (en) * | 1979-06-11 | 1980-12-22 | Takeda Chem Ind Ltd | Novel maytansinoid compound and its preparation |
| JPS55102583A (en) * | 1979-01-31 | 1980-08-05 | Takeda Chem Ind Ltd | 20-acyloxy-20-demethylmaytansinoid compound |
| JPS55162791A (en) * | 1979-06-05 | 1980-12-18 | Takeda Chem Ind Ltd | Antibiotic c-15003pnd and its preparation |
| JPS55164685A (en) * | 1979-06-08 | 1980-12-22 | Takeda Chem Ind Ltd | Novel maytansinoid compound and its preparation |
| JPS55164686A (en) * | 1979-06-11 | 1980-12-22 | Takeda Chem Ind Ltd | Novel maytansinoid compound and its preparation |
| US4309428A (en) * | 1979-07-30 | 1982-01-05 | Takeda Chemical Industries, Ltd. | Maytansinoids |
| JPS5645483A (en) * | 1979-09-19 | 1981-04-25 | Takeda Chem Ind Ltd | C-15003phm and its preparation |
| JPS5645485A (en) * | 1979-09-21 | 1981-04-25 | Takeda Chem Ind Ltd | Production of c-15003pnd |
| EP0028683A1 (en) * | 1979-09-21 | 1981-05-20 | Takeda Chemical Industries, Ltd. | Antibiotic C-15003 PHO and production thereof |
| WO1982001188A1 (en) * | 1980-10-08 | 1982-04-15 | Takeda Chemical Industries Ltd | 4,5-deoxymaytansinoide compounds and process for preparing same |
| US4450254A (en) * | 1980-11-03 | 1984-05-22 | Standard Oil Company | Impact improvement of high nitrile resins |
| US4419446A (en) * | 1980-12-31 | 1983-12-06 | The United States Of America As Represented By The Department Of Health And Human Services | Recombinant DNA process utilizing a papilloma virus DNA as a vector |
| US4313946A (en) * | 1981-01-27 | 1982-02-02 | The United States Of America As Represented By The Secretary Of Agriculture | Chemotherapeutically active maytansinoids from Trewia nudiflora |
| US4315929A (en) * | 1981-01-27 | 1982-02-16 | The United States Of America As Represented By The Secretary Of Agriculture | Method of controlling the European corn borer with trewiasine |
| JPS57192389A (en) * | 1981-05-20 | 1982-11-26 | Takeda Chem Ind Ltd | Novel maytansinoid |
| US4670393A (en) * | 1982-03-22 | 1987-06-02 | Genentech, Inc. | DNA vectors encoding a novel human growth hormone-variant protein |
| US4601978A (en) * | 1982-11-24 | 1986-07-22 | The Regents Of The University Of California | Mammalian metallothionein promoter system |
| US4560655A (en) * | 1982-12-16 | 1985-12-24 | Immunex Corporation | Serum-free cell culture medium and process for making same |
| US4657866A (en) * | 1982-12-21 | 1987-04-14 | Sudhir Kumar | Serum-free, synthetic, completely chemically defined tissue culture media |
| US4816567A (en) * | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4755465A (en) * | 1983-04-25 | 1988-07-05 | Genentech, Inc. | Secretion of correctly processed human growth hormone in E. coli and Pseudomonas |
| IL71991A (en) | 1983-06-06 | 1994-05-30 | Genentech Inc | Preparation of human FGI and FGE in their processed form through recombinant AND tranology in prokaryotes |
| US4767704A (en) * | 1983-10-07 | 1988-08-30 | Columbia University In The City Of New York | Protein-free culture medium |
| US4965199A (en) * | 1984-04-20 | 1990-10-23 | Genentech, Inc. | Preparation of functional human factor VIII in mammalian cells using methotrexate based selection |
| US4970198A (en) * | 1985-10-17 | 1990-11-13 | American Cyanamid Company | Antitumor antibiotics (LL-E33288 complex) |
| GB8516415D0 (en) | 1985-06-28 | 1985-07-31 | Celltech Ltd | Culture of animal cells |
| SE8505922D0 (sv) | 1985-12-13 | 1985-12-13 | Kabigen Ab | Construction of an igg binding protein to facilitate downstream processing using protein engineering |
| US4927762A (en) * | 1986-04-01 | 1990-05-22 | Cell Enterprises, Inc. | Cell culture medium with antioxidant |
| EP0266032A1 (en) | 1986-08-29 | 1988-05-04 | Beecham Group Plc | Modified fibrinolytic enzyme |
| IL85035A0 (en) * | 1987-01-08 | 1988-06-30 | Int Genetic Eng | Polynucleotide molecule,a chimeric antibody with specificity for human b cell surface antigen,a process for the preparation and methods utilizing the same |
| US5079233A (en) * | 1987-01-30 | 1992-01-07 | American Cyanamid Company | N-acyl derivatives of the LL-E33288 antitumor antibiotics, composition and methods for using the same |
| EP0307434B2 (en) * | 1987-03-18 | 1998-07-29 | Scotgen Biopharmaceuticals, Inc. | Altered antibodies |
| EP0288451B1 (en) | 1987-04-23 | 1994-08-10 | Monsanto Company | Secretion of insulin-like growth factor 1 in E. coli |
| US4975278A (en) * | 1988-02-26 | 1990-12-04 | Bristol-Myers Company | Antibody-enzyme conjugates in combination with prodrugs for the delivery of cytotoxic agents to tumor cells |
| US5770701A (en) * | 1987-10-30 | 1998-06-23 | American Cyanamid Company | Process for preparing targeted forms of methyltrithio antitumor agents |
| US5606040A (en) * | 1987-10-30 | 1997-02-25 | American Cyanamid Company | Antitumor and antibacterial substituted disulfide derivatives prepared from compounds possessing a methyl-trithio group |
| US5053394A (en) * | 1988-09-21 | 1991-10-01 | American Cyanamid Company | Targeted forms of methyltrithio antitumor agents |
| JP3040121B2 (ja) * | 1988-01-12 | 2000-05-08 | ジェネンテク，インコーポレイテッド | 増殖因子レセプターの機能を阻害することにより腫瘍細胞を処置する方法 |
| EP0435911B1 (en) | 1988-09-23 | 1996-03-13 | Cetus Oncology Corporation | Cell culture medium for enhanced cell growth, culture longevity and product expression |
| DE68929151T2 (de) | 1988-10-28 | 2000-07-20 | Genentech, Inc. | Verfahren zum nachweis von aktiven domänen und aminosäureresten in polypeptiden und hormonvarianten |
| WO1990005144A1 (en) | 1988-11-11 | 1990-05-17 | Medical Research Council | Single domain ligands, receptors comprising said ligands, methods for their production, and use of said ligands and receptors |
| US5530101A (en) * | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| DE3920358A1 (de) | 1989-06-22 | 1991-01-17 | Behringwerke Ag | Bispezifische und oligospezifische, mono- und oligovalente antikoerperkonstrukte, ihre herstellung und verwendung |
| CA2026147C (en) | 1989-10-25 | 2006-02-07 | Ravi J. Chari | Cytotoxic agents comprising maytansinoids and their therapeutic use |
| US5208020A (en) * | 1989-10-25 | 1993-05-04 | Immunogen Inc. | Cytotoxic agents comprising maytansinoids and their therapeutic use |
| US5427908A (en) * | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| US5723286A (en) * | 1990-06-20 | 1998-03-03 | Affymax Technologies N.V. | Peptide library and screening systems |
| GB9015198D0 (en) * | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| US6172197B1 (en) * | 1991-07-10 | 2001-01-09 | Medical Research Council | Methods for producing members of specific binding pairs |
| ES2139598T3 (es) | 1990-07-10 | 2000-02-16 | Medical Res Council | Procedimientos para la produccion de miembros de parejas de union especifica. |
| US5122469A (en) * | 1990-10-03 | 1992-06-16 | Genentech, Inc. | Method for culturing Chinese hamster ovary cells to improve production of recombinant proteins |
| US5508192A (en) * | 1990-11-09 | 1996-04-16 | Board Of Regents, The University Of Texas System | Bacterial host strains for producing proteolytically sensitive polypeptides |
| US5264365A (en) * | 1990-11-09 | 1993-11-23 | Board Of Regents, The University Of Texas System | Protease-deficient bacterial strains for production of proteolytically sensitive polypeptides |
| WO1992009690A2 (en) | 1990-12-03 | 1992-06-11 | Genentech, Inc. | Enrichment method for variant proteins with altered binding properties |
| EP1471142B1 (en) * | 1991-04-10 | 2008-11-19 | The Scripps Research Institute | Heterodimeric receptor libraries using phagemids |
| WO1994004679A1 (en) * | 1991-06-14 | 1994-03-03 | Genentech, Inc. | Method for making humanized antibodies |
| CA2103059C (en) * | 1991-06-14 | 2005-03-22 | Paul J. Carter | Method for making humanized antibodies |
| JP3951062B2 (ja) * | 1991-09-19 | 2007-08-01 | ジェネンテック・インコーポレーテッド | 少なくとも遊離のチオールとして存在するシステインを有する抗体フラグメントの大腸菌での発現、２官能性Ｆ（ａｂ’）２抗体の産生のための使用 |
| EP0605522B1 (en) | 1991-09-23 | 1999-06-23 | Medical Research Council | Methods for the production of humanized antibodies |
| US5362852A (en) * | 1991-09-27 | 1994-11-08 | Pfizer Inc. | Modified peptide derivatives conjugated at 2-hydroxyethylamine moieties |
| US5270170A (en) * | 1991-10-16 | 1993-12-14 | Affymax Technologies N.V. | Peptide library and screening method |
| EP1136556B1 (en) | 1991-11-25 | 2005-06-08 | Enzon, Inc. | Method of producing multivalent antigen-binding proteins |
| WO1993011236A1 (en) | 1991-12-02 | 1993-06-10 | Medical Research Council | Production of anti-self antibodies from antibody segment repertoires and displayed on phage |
| US5733743A (en) * | 1992-03-24 | 1998-03-31 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| JP3507073B2 (ja) | 1992-03-24 | 2004-03-15 | ケンブリッジ アンティボディー テクノロジー リミティド | 特異的結合対の成員の製造方法 |
| ZA932522B (en) | 1992-04-10 | 1993-12-20 | Res Dev Foundation | Immunotoxins directed against c-erbB-2(HER/neu) related surface antigens |
| US6083713A (en) * | 1992-08-31 | 2000-07-04 | Bristol-Myers Squibb Company | Cloning and expression of βAPP-C100 receptor (C100-R) |
| PT752248E (pt) | 1992-11-13 | 2001-01-31 | Idec Pharma Corp | Aplicacao terapeutica de anticorpos quimericos e marcados radioactivamente contra antigenios de diferenciacao restrita de linfocitos b humanos para o tratamento do linfoma de celulas b |
| EP0672142B1 (en) * | 1992-12-04 | 2001-02-28 | Medical Research Council | Multivalent and multispecific binding proteins, their manufacture and use |
| WO1994029351A2 (en) | 1993-06-16 | 1994-12-22 | Celltech Limited | Antibodies |
| US5534615A (en) * | 1994-04-25 | 1996-07-09 | Genentech, Inc. | Cardiac hypertrophy factor and uses therefor |
| US5773001A (en) * | 1994-06-03 | 1998-06-30 | American Cyanamid Company | Conjugates of methyltrithio antitumor agents and intermediates for their synthesis |
| US5639635A (en) * | 1994-11-03 | 1997-06-17 | Genentech, Inc. | Process for bacterial production of polypeptides |
| US5770567A (en) * | 1994-11-14 | 1998-06-23 | Genentech, Inc. | Sensory and motor neuron derived factor (SMDF) |
| 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 |
| US5739277A (en) * | 1995-04-14 | 1998-04-14 | Genentech Inc. | Altered polypeptides with increased half-life |
| US5714586A (en) * | 1995-06-07 | 1998-02-03 | American Cyanamid Company | Methods for the preparation of monomeric calicheamicin derivative/carrier conjugates |
| US5712374A (en) * | 1995-06-07 | 1998-01-27 | American Cyanamid Company | Method for the preparation of substantiallly monomeric calicheamicin derivative/carrier conjugates |
| US6027888A (en) * | 1996-04-05 | 2000-02-22 | Board Of Regents, The University Of Texas System | Methods for producing soluble, biologically-active disulfide-bond containing eukaryotic proteins in bacterial cells |
| CA2269204C (en) | 1996-10-18 | 2012-01-24 | Genentech, Inc. | Anti-erbb2 antibodies |
| US6072047A (en) | 1997-02-13 | 2000-06-06 | Immunex Corporation | Receptor that binds trail |
| ATE516354T1 (de) | 1997-05-15 | 2011-07-15 | Genentech Inc | Apo-2-rezeptor |
| US6083715A (en) | 1997-06-09 | 2000-07-04 | Board Of Regents, The University Of Texas System | Methods for producing heterologous disulfide bond-containing polypeptides in bacterial cells |
| DK1068241T3 (da) | 1998-04-02 | 2008-02-04 | Genentech Inc | Antistofvarianter og fragmenter deraf |
| ES2694002T3 (es) | 1999-01-15 | 2018-12-17 | Genentech, Inc. | Polipéptido que comprende una región Fc de IgG1 humana variante |
| US6436401B1 (en) * | 1999-09-14 | 2002-08-20 | Milkhaus Laboratory, Inc. | Methods for alleviating symptoms associated with diabetes and diabetic neuropathy comprising administration of low levels of antibodies |
| EP1226161A2 (en) | 1999-09-15 | 2002-07-31 | Genentech, Inc. | Apo-2 receptor antibodies |
| DE60041564D1 (de) | 1999-12-24 | 2009-03-26 | Genentech Inc | Verfahren und Zusammensetzungen zur Verlängerung der Entsorgungshalbwertszeit von biowirksamen Verbindungen |
| ES2649037T3 (es) | 2000-12-12 | 2018-01-09 | Medimmune, Llc | Moléculas con semividas prolongadas, composiciones y usos de las mismas |
| EP1360288B1 (en) * | 2000-12-18 | 2011-02-16 | Dyax Corp. | Focused libraries of genetic packages |
| ES2401428T3 (es) * | 2002-04-10 | 2013-04-19 | Genentech, Inc. | Variantes de anticuerpos anti-HER2 |
| CA2488441C (en) * | 2002-06-03 | 2015-01-27 | Genentech, Inc. | Synthetic antibody phage libraries |
| EP1391213A1 (en) | 2002-08-21 | 2004-02-25 | Boehringer Ingelheim International GmbH | Compositions and methods for treating cancer using maytansinoid CD44 antibody immunoconjugates and chemotherapeutic agents |
| JP2006514096A (ja) * | 2002-11-27 | 2006-04-27 | アイアールエム・リミテッド・ライアビリティ・カンパニー | 癌細胞においてアポトーシスを誘導するための方法および組成物 |
| WO2004065416A2 (en) | 2003-01-16 | 2004-08-05 | Genentech, Inc. | Synthetic antibody phage libraries |
| US20050106667A1 (en) * | 2003-08-01 | 2005-05-19 | Genentech, Inc | Binding polypeptides with restricted diversity sequences |
| AU2004261980A1 (en) | 2003-08-01 | 2005-02-10 | Genentech, Inc. | Antibody CDR polypeptide sequences with restricted diversity |
| KR20070010046A (ko) | 2004-04-06 | 2007-01-19 | 제넨테크, 인크. | Ｄｒ5 항체 및 그의 용도 |
| ES2577292T3 (es) | 2005-11-07 | 2016-07-14 | Genentech, Inc. | Polipéptidos de unión con secuencias hipervariables de VH/VL diversificadas y consenso |
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| JP5808070B2 (ja) | 2015-11-10 |
| US8957187B2 (en) | 2015-02-17 |
| JP2009518011A (ja) | 2009-05-07 |
| RU2470941C2 (ru) | 2012-12-27 |
| CA2631327C (en) | 2015-10-13 |
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