JP2003527832A - ヒト抗体 - Google Patents
ヒト抗体Info
- Publication number
- JP2003527832A JP2003527832A JP2001528642A JP2001528642A JP2003527832A JP 2003527832 A JP2003527832 A JP 2003527832A JP 2001528642 A JP2001528642 A JP 2001528642A JP 2001528642 A JP2001528642 A JP 2001528642A JP 2003527832 A JP2003527832 A JP 2003527832A
- Authority
- JP
- Japan
- Prior art keywords
- human
- library
- antibody
- target
- nucleic acid
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
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Classifications
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- C—CHEMISTRY; METALLURGY
- C40—COMBINATORIAL TECHNOLOGY
- C40B—COMBINATORIAL CHEMISTRY; LIBRARIES, e.g. CHEMICAL LIBRARIES
- C40B40/00—Libraries per se, e.g. arrays, mixtures
- C40B40/02—Libraries contained in or displayed by microorganisms, e.g. bacteria or animal cells; Libraries contained in or displayed by vectors, e.g. plasmids; Libraries containing only microorganisms or vectors
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K67/00—Rearing or breeding animals, not otherwise provided for; New or modified breeds of animals
- A01K67/027—New or modified breeds of vertebrates
- A01K67/0275—Genetically modified vertebrates, e.g. transgenic
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- 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
- C07K16/24—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
- C07K16/244—Interleukins [IL]
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1034—Isolating an individual clone by screening libraries
- C12N15/1037—Screening libraries presented on the surface of microorganisms, e.g. phage display, E. coli display
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/85—Vectors or expression systems specially adapted for eukaryotic hosts for animal cells
- C12N15/8509—Vectors or expression systems specially adapted for eukaryotic hosts for animal cells for producing genetically modified animals, e.g. transgenic
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- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2207/00—Modified animals
- A01K2207/15—Humanized animals
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2217/00—Genetically modified animals
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2217/00—Genetically modified animals
- A01K2217/05—Animals comprising random inserted nucleic acids (transgenic)
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2227/00—Animals characterised by species
- A01K2227/10—Mammal
- A01K2227/105—Murine
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- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2267/00—Animals characterised by purpose
- A01K2267/01—Animal expressing industrially exogenous proteins
-
- 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
Landscapes
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- Health & Medical Sciences (AREA)
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- General Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
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- Proteomics, Peptides & Aminoacids (AREA)
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- Environmental Sciences (AREA)
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- Biodiversity & Conservation Biology (AREA)
- Animal Behavior & Ethology (AREA)
- Animal Husbandry (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Virology (AREA)
- Crystallography & Structural Chemistry (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US15741599P | 1999-10-02 | 1999-10-02 | |
| US60/157,415 | 1999-10-02 | ||
| US09/453,234 US6794132B2 (en) | 1999-10-02 | 1999-12-01 | Human antibodies |
| US09/453,234 | 1999-12-01 | ||
| PCT/US2000/027237 WO2001025492A1 (en) | 1999-10-02 | 2000-10-02 | Human antibodies |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2003527832A true JP2003527832A (ja) | 2003-09-24 |
| JP2003527832A5 JP2003527832A5 (enExample) | 2007-11-22 |
Family
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2001528642A Pending JP2003527832A (ja) | 1999-10-02 | 2000-10-02 | ヒト抗体 |
Country Status (6)
| Country | Link |
|---|---|
| US (1) | US6794132B2 (enExample) |
| EP (1) | EP1222314A4 (enExample) |
| JP (1) | JP2003527832A (enExample) |
| AU (1) | AU783276B2 (enExample) |
| CA (1) | CA2385709A1 (enExample) |
| WO (1) | WO2001025492A1 (enExample) |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2008536517A (ja) * | 2005-04-20 | 2008-09-11 | アムゲン・フレモント・インコーポレーテッド | インターロイキン‐８に対する高親和性の完全ヒトモノクローナル抗体、およびそのような抗体のエピトープ |
| JP2009106287A (ja) * | 2005-04-26 | 2009-05-21 | Pfizer Inc | Ｐ−カドヘリン抗体 |
| US7592430B2 (en) | 2003-09-10 | 2009-09-22 | Amgen Fremont | Antibodies to M-CSF |
| EP2311478A1 (en) | 2006-03-20 | 2011-04-20 | Japan Science and Technology Agency | Use of ip3 receptor-binding protein for controlling intracellular pH |
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| Publication number | Priority date | Publication date | Assignee | Title |
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| US6696251B1 (en) * | 1996-05-31 | 2004-02-24 | Board Of Trustees Of The University Of Illinois | Yeast cell surface display of proteins and uses thereof |
| US6969601B2 (en) | 1997-04-03 | 2005-11-29 | Jensenius Jens Chr | MASP-2, a complement-fixing enzyme, and uses for it |
| US6759243B2 (en) * | 1998-01-20 | 2004-07-06 | Board Of Trustees Of The University Of Illinois | High affinity TCR proteins and methods |
| US6303321B1 (en) | 1999-02-11 | 2001-10-16 | North Shore-Long Island Jewish Research Institute | Methods for diagnosing sepsis |
| US20070111259A1 (en) * | 1999-10-02 | 2007-05-17 | Medarex, Inc. | Human antibodies |
| US7135287B1 (en) * | 1999-10-02 | 2006-11-14 | Biosite, Inc. | Human antibodies |
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| EP2523976B1 (en) | 2010-01-11 | 2018-04-25 | Alexion Pharmaceuticals, Inc. | Biomarkers of immunomodulatory effects in humans treated with anti-cd200 antibodies |
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| KR101800913B1 (ko) | 2010-04-30 | 2017-12-20 | 알렉시온 파마슈티칼스, 인코포레이티드 | 항-c5a 항체들과 이 항체들을 이용하는 방법 |
| US20130288910A1 (en) * | 2010-06-16 | 2013-10-31 | Jef D. Boeke | Methods and systems for generating, validating and using monoclonal antibodies |
| EP2585110A4 (en) | 2010-06-22 | 2014-01-22 | Univ Colorado Regents | ANTIBODIES AGAINST THE C3D FRAGMENT OF THE COMPLEMENT COMPONENT 3 |
| CA2804550C (en) * | 2010-07-09 | 2021-01-05 | Bionovion Holding B.V. | Agonistic antibody to cd27 |
| WO2012009568A2 (en) | 2010-07-16 | 2012-01-19 | Adimab, Llc | Antibody libraries |
| US8440195B2 (en) * | 2010-11-12 | 2013-05-14 | National University Corporation Chiba University | Inhibition of CD69 for treatment of inflammatory conditions |
| JP6150734B2 (ja) | 2011-02-03 | 2017-06-21 | アレクシオン ファーマシューティカルズ， インコーポレイテッド | 同種移植片の生存を長期化するための抗ｃｄ２００抗体の使用 |
| KR20220044616A (ko) | 2011-04-08 | 2022-04-08 | 유니버시티 오브 레스터 | Ｍａｓｐ-2 의존적 보체 활성화와 관련된 질병을 치료하는 방법 |
| US9644035B2 (en) | 2011-04-08 | 2017-05-09 | Omeros Corporation | Methods for treating conditions associated with MASP-2 dependent complement activation |
| ES2821375T3 (es) * | 2011-06-13 | 2021-04-26 | Tla Targeted Immunotherapies Ab | Tratamiento de afecciones respiratorias |
| US9726666B2 (en) | 2011-06-13 | 2017-08-08 | Tla Targeted Immunotherapies Ab | Diagnosing and treating inflammatory diseases |
| RS58102B1 (sr) | 2011-11-09 | 2019-02-28 | Bristol Myers Squibb Co | Lečenje hematoloških maligniteta sa anti-cxcr4 antitelom |
| KR101566538B1 (ko) | 2012-06-08 | 2015-11-05 | 국립암센터 | 신규한 Ｔｈ17 세포 전환용 에피토프 및 이의 용도 |
| AR091649A1 (es) | 2012-07-02 | 2015-02-18 | Bristol Myers Squibb Co | Optimizacion de anticuerpos que se fijan al gen de activacion de linfocitos 3 (lag-3) y sus usos |
| EP2925878A1 (en) | 2012-11-28 | 2015-10-07 | Abwiz Bio Inc. | Preparation of gene-specific templates for the use in single primer amplification |
| WO2014093786A1 (en) * | 2012-12-14 | 2014-06-19 | Abbvie, Inc. | Methods for increasing the efficiency of hybridoma generation |
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| CN105682683A (zh) | 2013-08-02 | 2016-06-15 | 阿杜罗生物科技控股有限公司 | 结合cd27激动剂以及免疫检查点抑制以用于免疫刺激 |
| JOP20190055A1 (ar) | 2016-09-26 | 2019-03-24 | Merck Sharp & Dohme | أجسام مضادة ضد cd27 |
| CA3052740A1 (en) | 2017-02-10 | 2018-08-16 | Eutilex Co., Ltd. | Ifn-.gamma.-inducible regulatory t cell convertible anti-cancer (irtca) antibody and uses thereof |
| US11572405B2 (en) | 2018-01-12 | 2023-02-07 | Bristol-Myers Squibb Company | Combination therapy with anti-IL-8 antibodies and anti-PD-1 antibodies for treating cancer |
| WO2021050989A1 (en) * | 2019-09-13 | 2021-03-18 | Duke University | Zika antibodies and their use |
Family Cites Families (25)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4376110A (en) | 1980-08-04 | 1983-03-08 | Hybritech, Incorporated | Immunometric assays using monoclonal antibodies |
| US4486530A (en) | 1980-08-04 | 1984-12-04 | Hybritech Incorporated | Immunometric assays using monoclonal antibodies |
| US5173418A (en) | 1985-05-10 | 1992-12-22 | Benzon Pharma, A/S | Production in Escherichia coli of extracellular Serratia spp. hydrolases |
| US5618920A (en) | 1985-11-01 | 1997-04-08 | Xoma Corporation | Modular assembly of antibody genes, antibodies prepared thereby and use |
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| GB8823869D0 (en) | 1988-10-12 | 1988-11-16 | Medical Res Council | Production of antibodies |
| 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 |
| US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5770429A (en) | 1990-08-29 | 1998-06-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| IL99552A0 (en) | 1990-09-28 | 1992-08-18 | Ixsys Inc | Compositions containing procaryotic cells,a kit for the preparation of vectors useful for the coexpression of two or more dna sequences and methods for the use thereof |
| DE69233750D1 (de) | 1991-04-10 | 2009-01-02 | Scripps Research Inst | Bibliotheken heterodimerer Rezeptoren mittels Phagemiden |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| US5667988A (en) | 1992-01-27 | 1997-09-16 | The Scripps Research Institute | Methods for producing antibody libraries using universal or randomized immunoglobulin light chains |
| US5914241A (en) | 1993-01-19 | 1999-06-22 | Biosite Diagnostics, Inc. | Assays and kits for detecting analytes in the presence of cross-reacting substances |
| WO1994026787A1 (en) | 1993-05-07 | 1994-11-24 | The Board Of Trustees Of The Leland Stanford Junior University | Method for generating cell type specific phage antibody libraries |
| DK1231268T3 (da) | 1994-01-31 | 2005-11-21 | Univ Boston | Polyklonale antistofbiblioteker |
| JP4312259B2 (ja) | 1995-04-27 | 2009-08-12 | アムジェン フレモント インク． | 免疫したゼノマウス（ＸｅｎｏＭｏｕｓｅ）に由来するヒト抗体 |
| US5766905A (en) | 1996-06-14 | 1998-06-16 | Associated Universities Inc. | Cytoplasmic bacteriophage display system |
| DE19632549A1 (de) | 1996-08-13 | 1998-02-19 | Merck Patent Gmbh | Arylalkanoylpyridazine |
| US6057098A (en) * | 1997-04-04 | 2000-05-02 | Biosite Diagnostics, Inc. | Polyvalent display libraries |
| AU8755798A (en) | 1997-04-04 | 1998-11-13 | Biosite Diagnostics Incorporated | Polyvalent and polyclonal libraries |
| CA2253633A1 (en) | 1997-12-03 | 1999-06-03 | Boehringer Mannheim Corporation | Complex specific antibodies, method of preparation and uses thereof |
| US5939807A (en) | 1997-12-16 | 1999-08-17 | Reliance Electric Industrial Company | Cap mounted drive for a brushless DC motor |
| US20020029391A1 (en) * | 1998-04-15 | 2002-03-07 | Claude Geoffrey Davis | Epitope-driven human antibody production and gene expression profiling |
-
1999
- 1999-12-01 US US09/453,234 patent/US6794132B2/en not_active Expired - Fee Related
-
2000
- 2000-10-02 AU AU78496/00A patent/AU783276B2/en not_active Ceased
- 2000-10-02 CA CA002385709A patent/CA2385709A1/en not_active Abandoned
- 2000-10-02 WO PCT/US2000/027237 patent/WO2001025492A1/en not_active Ceased
- 2000-10-02 EP EP00968612A patent/EP1222314A4/en not_active Withdrawn
- 2000-10-02 JP JP2001528642A patent/JP2003527832A/ja active Pending
Non-Patent Citations (4)
| Title |
|---|
| JPN7010002883, Ｃｕｒｒｅｎｔ Ｏｐｉｎｉｏｎ ｉｎ Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ｖｏｌ．８， ｐｐ．５０３−５０８ （１９９７） * |
| JPN7010002884, Ａｎｎｕａｌ Ｒｅｖｉｅｗ ｏｆ Ｉｍｍｕｎｏｌｏｇｙ， ｖｏｌ．１２， ｐｐ．４３３−４５５ （１９９４） * |
| JPN7010002885, Ｎａｔｕｒｅ Ｇｅｎｅｔｉｃｓ， ｖｏｌ．１５， ｐｐ．１４６−１５６ （１９９７） * |
| JPN7010002886, Ｎａｔｕｒｅ Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ｖｏｌ．１４， ｐｐ．８４５−８５１ （１９９６） * |
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7592430B2 (en) | 2003-09-10 | 2009-09-22 | Amgen Fremont | Antibodies to M-CSF |
| US7728113B2 (en) | 2003-09-10 | 2010-06-01 | Amgen Fremont Inc. | Methods of treating arthritic conditions with antibodies to M-CSF |
| US8188249B2 (en) | 2003-09-10 | 2012-05-29 | Amgen Fremont Inc. | Nucleic acid molecules encoding antibodies to M-CSF |
| US9718883B2 (en) | 2003-09-10 | 2017-08-01 | Amgen Fremont Inc. | Antibodies to M-CSF |
| US10280219B2 (en) | 2003-09-10 | 2019-05-07 | Amgen Fremont Inc. | Antibodies to M-CSF |
| JP2008536517A (ja) * | 2005-04-20 | 2008-09-11 | アムゲン・フレモント・インコーポレーテッド | インターロイキン‐８に対する高親和性の完全ヒトモノクローナル抗体、およびそのような抗体のエピトープ |
| JP2009106287A (ja) * | 2005-04-26 | 2009-05-21 | Pfizer Inc | Ｐ−カドヘリン抗体 |
| EP2311478A1 (en) | 2006-03-20 | 2011-04-20 | Japan Science and Technology Agency | Use of ip3 receptor-binding protein for controlling intracellular pH |
| EP2311477A1 (en) | 2006-03-20 | 2011-04-20 | Japan Science and Technology Agency | Use of ip3 receptor-binding protein for controlling phosphatidylinositol metabolism |
Also Published As
| Publication number | Publication date |
|---|---|
| EP1222314A4 (en) | 2006-07-12 |
| US20030091995A1 (en) | 2003-05-15 |
| US6794132B2 (en) | 2004-09-21 |
| WO2001025492A1 (en) | 2001-04-12 |
| AU7849600A (en) | 2001-05-10 |
| EP1222314A1 (en) | 2002-07-17 |
| AU783276B2 (en) | 2005-10-06 |
| CA2385709A1 (en) | 2001-04-12 |
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