AU2006338198B2 - Binding polypeptides and uses thereof - Google Patents
Binding polypeptides and uses thereof Download PDFInfo
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- AU2006338198B2 AU2006338198B2 AU2006338198A AU2006338198A AU2006338198B2 AU 2006338198 B2 AU2006338198 B2 AU 2006338198B2 AU 2006338198 A AU2006338198 A AU 2006338198A AU 2006338198 A AU2006338198 A AU 2006338198A AU 2006338198 B2 AU2006338198 B2 AU 2006338198B2
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Families Citing this family (34)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8679490B2 (en) | 2005-11-07 | 2014-03-25 | Genentech, Inc. | Binding polypeptides with diversified and consensus VH/VL hypervariable sequences |
| WO2007064919A2 (en) * | 2005-12-02 | 2007-06-07 | Genentech, Inc. | Binding polypeptides with restricted diversity sequences |
| EP3753947A1 (en) * | 2007-09-14 | 2020-12-23 | Adimab, LLC | Rationally designed, synthetic antibody libraries and uses therefor |
| US8877688B2 (en) | 2007-09-14 | 2014-11-04 | Adimab, Llc | Rationally designed, synthetic antibody libraries and uses therefor |
| JP2011527886A (ja) | 2007-12-11 | 2011-11-10 | ザ スクリプス リサーチ インスティチュート | メタノール資化性酵母ピキア・パストリスにおけるインビボ非天然アミノ酸発現 |
| WO2009088924A2 (en) | 2007-12-31 | 2009-07-16 | Xoma Technology Ltd. | Methods and materials for targeted affinity enhancement |
| 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 |
| MX2011000891A (es) * | 2008-07-21 | 2011-06-01 | Immunomedics Inc | Variantes estructurales de anticuerpos para caracteristicas terapeuticas mejoradas. |
| 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 |
| CA2779436A1 (en) | 2008-10-31 | 2010-05-06 | Biogen Idec Ma Inc. | Light targeting molecules and uses thereof |
| US20090197339A1 (en) * | 2008-12-10 | 2009-08-06 | The Scripps Research Institute | In vivo unnatural amino acid expression in the methylotrophic yeast pichia pastoris |
| US8609383B2 (en) | 2008-12-10 | 2013-12-17 | The Scripps Research Institute | Production of carrier-peptide conjugates using chemically reactive unnatural amino acids |
| EP2464220A4 (en) | 2009-08-13 | 2014-05-07 | Crystal Bioscience Inc | Transgenic animal for the production of antibodies with minimal complementarity-determining regions |
| JP2013505944A (ja) * | 2009-09-24 | 2013-02-21 | シアトル ジェネティックス， インコーポレイテッド | Ｄｒ５リガンド薬物結合体 |
| US8937159B2 (en) | 2009-12-16 | 2015-01-20 | Abbvie Biotherapeutics Inc. | Anti-HER2 antibodies and their uses |
| DK3345615T3 (da) | 2010-03-01 | 2020-01-20 | Bayer Healthcare Llc | Optimerede monoklonale antistoffer mod inhibitor af vævsfaktoraktiveringsvejen (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 |
| PE20131376A1 (es) | 2010-08-27 | 2013-11-25 | Gilead Biologics Inc | Anticuerpos para metaloproteinasa-9 de matriz |
| US20140121123A1 (en) * | 2010-10-29 | 2014-05-01 | Kevin Caili Wang | Methods for diversifying antibodies, antibodies derived therefrom and uses thereof |
| AU2012212047A1 (en) * | 2011-02-03 | 2013-08-22 | Xoma Technology Ltd. | Methods and materials for enhancing functional protein expression in bacteria |
| US8940517B2 (en) * | 2011-04-21 | 2015-01-27 | Baxter International Inc. | Methods for isolating and quantifying antigen from vaccines |
| DK2702146T3 (en) * | 2011-04-28 | 2019-03-11 | Univ Leland Stanford Junior | IDENTIFICATION OF POLYNUCLEOTIDES CONNECTED WITH A SAMPLE |
| US9550836B2 (en) * | 2012-02-29 | 2017-01-24 | Gilead Biologics, Inc. | Method of detecting human matrix metalloproteinase 9 using antibodies |
| EP2819697A4 (en) | 2012-02-29 | 2016-03-09 | Gilead Biologics Inc | ANTIBODIES AGAINST METALLOPROTEINASE 9 OF MATRIX |
| KR101505157B1 (ko) * | 2012-05-08 | 2015-03-24 | 주식회사 종근당 | 항―ＥｒｂＢ２ 항체 변이체 |
| CN107108723B (zh) * | 2014-07-08 | 2021-11-12 | 瑞华药业集团 | 精氨基琥珀酸合成酶的抗体和相关方法 |
| EP3509623A4 (en) * | 2016-09-07 | 2020-06-03 | Saksin Lifesciences PVT Ltd | SYNTHETIC ANTIBODIES TO VEGF AND USES THEREOF |
| 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 |
| JP7366755B2 (ja) * | 2017-05-30 | 2023-10-23 | ザ ボード オブ リージェンツ オブ ザ ユニヴァーシティ オブ オクラホマ | 抗ダブルコルチン様キナーゼ１抗体および使用方法 |
| 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 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2005012359A2 (en) * | 2003-08-01 | 2005-02-10 | Genentech, Inc. | Anti-vegf antibodies |
| WO2005012531A2 (en) * | 2003-08-01 | 2005-02-10 | Genentech, Inc. | Antibody cdr polypeptide sequences with restricted diversity |
Family Cites Families (108)
| 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 | |
| US4307016A (en) * | 1978-03-24 | 1981-12-22 | Takeda Chemical Industries, Ltd. | Demethyl maytansinoids |
| US4265814A (en) * | 1978-03-24 | 1981-05-05 | Takeda Chemical Industries | Matansinol 3-n-hexadecanoate |
| 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 |
| JPS55164687A (en) * | 1979-06-11 | 1980-12-22 | 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 |
| 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 |
| CA1314507C (en) | 1987-04-23 | 1993-03-16 | Edith Yee-Tak Wong | Secretion of insulin-like growth factor-i 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 |
| WO1989006692A1 (en) * | 1988-01-12 | 1989-07-27 | Genentech, Inc. | Method of treating tumor cells by inhibiting growth factor receptor function |
| EP0435911B1 (en) | 1988-09-23 | 1996-03-13 | Cetus Oncology Corporation | Cell culture medium for enhanced cell growth, culture longevity and product expression |
| CA2345497A1 (en) | 1988-10-28 | 1990-04-28 | Genentech, Inc. | Growth hormone variants and method for forming growth hormone variants |
| 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 |
| 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 |
| US5508192A (en) * | 1990-11-09 | 1996-04-16 | Board Of Regents, The University Of Texas System | Bacterial host strains for producing proteolytically sensitive polypeptides |
| WO1992009690A2 (en) * | 1990-12-03 | 1992-06-11 | Genentech, Inc. | Enrichment method for variant proteins with altered binding properties |
| ATE414768T1 (de) * | 1991-04-10 | 2008-12-15 | Scripps Research Inst | Bibliotheken heterodimerer rezeptoren mittels phagemiden |
| DE122004000008I1 (de) * | 1991-06-14 | 2005-06-09 | Genentech Inc | Humanisierter Heregulin Antikörper. |
| WO1994004679A1 (en) * | 1991-06-14 | 1994-03-03 | Genentech, Inc. | Method for making humanized antibodies |
| 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 |
| AU665025B2 (en) | 1991-09-23 | 1995-12-14 | Cambridge Antibody Technology Limited | Production of chimeric antibodies - a combinatorial approach |
| 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 |
| ES2227512T3 (es) | 1991-12-02 | 2005-04-01 | Medical Research Council | Produccion de anticuerpos contra auto-antigenos a partir de repertorios de segmentos de anticuerpos fijados en un fago. |
| DE69333823T2 (de) | 1992-03-24 | 2006-05-04 | Cambridge Antibody Technology Ltd., Melbourn | Verfahren zur herstellung von gliedern von spezifischen bindungspaaren |
| US5733743A (en) * | 1992-03-24 | 1998-03-31 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| 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) |
| EP1005870B1 (en) | 1992-11-13 | 2009-01-21 | Biogen Idec Inc. | Therapeutic application of chimeric antibodies to human B lymphocyte restricted differentiation antigen for treatment of B cell lymphoma |
| ATE199392T1 (de) * | 1992-12-04 | 2001-03-15 | Medical Res Council | Multivalente und multispezifische bindungsproteine, deren herstellung und verwendung |
| EP0714409A1 (en) | 1993-06-16 | 1996-06-05 | Celltech Therapeutics 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) |
| US5731168A (en) * | 1995-03-01 | 1998-03-24 | Genentech, Inc. | Method for making heteromultimeric polypeptides |
| US5840523A (en) * | 1995-03-01 | 1998-11-24 | Genetech, Inc. | Methods and compositions for secretion of heterologous 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 |
| CN100415772C (zh) | 1996-10-18 | 2008-09-03 | 基因技术股份有限公司 | 抗ErbB2抗体 |
| US6072047A (en) | 1997-02-13 | 2000-06-06 | Immunex Corporation | Receptor that binds trail |
| ES2293682T5 (es) | 1997-05-15 | 2011-11-17 | Genentech, Inc. | Anticuerpo anti-apo2. |
| 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 |
| DE69937291T2 (de) | 1998-04-02 | 2008-07-10 | Genentech, Inc., South San Francisco | Antikörpervarianten und fragmente davon |
| KR101155191B1 (ko) | 1999-01-15 | 2012-06-13 | 제넨테크, 인크. | 효과기 기능이 변화된 폴리펩티드 변이체 |
| 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 |
| IL148266A0 (en) | 1999-09-15 | 2002-09-12 | Genentech Inc | Apo-2 receptor antibodies |
| WO2001045746A2 (en) | 1999-12-24 | 2001-06-28 | Genentech, Inc. | Methods and compositions for prolonging elimination half-times of bioactive compounds |
| DK1355919T3 (da) | 2000-12-12 | 2011-03-14 | Medimmune Llc | Molekyler med længere halveringstider, sammensætninger og anvendelser deraf |
| US20030119056A1 (en) * | 2000-12-18 | 2003-06-26 | Ladner Robert Charles | Focused libraries of genetic packages |
| JP2005522514A (ja) * | 2002-04-10 | 2005-07-28 | ジェネンテック・インコーポレーテッド | 抗ｈｅｒ２抗体改変体 |
| 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 |
| MXPA05005726A (es) * | 2002-11-27 | 2005-08-16 | Irm Llc | Metodos y composiciones para inducir apoptosis en celulas de cancer. |
| WO2004065416A2 (en) * | 2003-01-16 | 2004-08-05 | Genentech, Inc. | Synthetic antibody phage libraries |
| KR20070010046A (ko) | 2004-04-06 | 2007-01-19 | 제넨테크, 인크. | Ｄｒ5 항체 및 그의 용도 |
| US8679490B2 (en) * | 2005-11-07 | 2014-03-25 | Genentech, Inc. | Binding polypeptides with diversified and consensus VH/VL hypervariable sequences |
-
2006
- 2006-12-01 CA CA2631327A patent/CA2631327C/en active Active
- 2006-12-01 RU RU2008126948/10A patent/RU2470941C2/ru active
- 2006-12-01 AU AU2006338198A patent/AU2006338198B2/en not_active Expired - Fee Related
- 2006-12-01 WO PCT/US2006/046046 patent/WO2007094842A2/en not_active Ceased
- 2006-12-01 KR KR1020087016105A patent/KR101434682B1/ko active Active
- 2006-12-01 JP JP2008543499A patent/JP5808070B2/ja active Active
- 2006-12-01 EP EP06849911A patent/EP1957540B1/en active Active
- 2006-12-01 US US11/566,120 patent/US8957187B2/en active Active
- 2006-12-01 ES ES06849911T patent/ES2388932T3/es active Active
-
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- 2008-06-10 ZA ZA2008/05045A patent/ZA200805045B/en unknown
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2005012359A2 (en) * | 2003-08-01 | 2005-02-10 | Genentech, Inc. | Anti-vegf antibodies |
| WO2005012531A2 (en) * | 2003-08-01 | 2005-02-10 | Genentech, Inc. | Antibody cdr polypeptide sequences with restricted diversity |
Non-Patent Citations (1)
| Title |
|---|
| Fellouse, F.A. et al 2005 J. Mol. Biol. vol. 348, pp. 1153-1162 * |
Also Published As
| Publication number | Publication date |
|---|---|
| WO2007094842A3 (en) | 2008-02-28 |
| AU2006338198A1 (en) | 2007-08-23 |
| CA2631327A1 (en) | 2007-08-23 |
| EP1957540A2 (en) | 2008-08-20 |
| EP1957540B1 (en) | 2012-06-13 |
| US8957187B2 (en) | 2015-02-17 |
| KR20080077246A (ko) | 2008-08-21 |
| US20070202552A1 (en) | 2007-08-30 |
| ZA200805045B (en) | 2009-12-30 |
| RU2008126948A (ru) | 2010-01-10 |
| HK1121470A1 (en) | 2009-04-24 |
| WO2007094842A2 (en) | 2007-08-23 |
| KR101434682B1 (ko) | 2014-08-27 |
| JP2009518011A (ja) | 2009-05-07 |
| RU2470941C2 (ru) | 2012-12-27 |
| ES2388932T3 (es) | 2012-10-19 |
| JP5808070B2 (ja) | 2015-11-10 |
| CA2631327C (en) | 2015-10-13 |
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