DK2310413T3 - Camelide-derived antigen-binding polypeptides - Google Patents
Camelide-derived antigen-binding polypeptides Download PDFInfo
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- DK2310413T3 DK2310413T3 DK09772912.3T DK09772912T DK2310413T3 DK 2310413 T3 DK2310413 T3 DK 2310413T3 DK 09772912 T DK09772912 T DK 09772912T DK 2310413 T3 DK2310413 T3 DK 2310413T3
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- binding polypeptide
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- 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]
- C07K16/245—IL-1
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- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
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- C07—ORGANIC CHEMISTRY
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- C07K16/46—Hybrid immunoglobulins
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- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
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- 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
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
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- 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
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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
- C07K2317/22—Immunoglobulins specific features characterized by taxonomic origin from camelids, e.g. camel, llama or dromedary
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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
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/55—Fab or Fab'
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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
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
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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
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- C07K—PEPTIDES
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- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/567—Framework region [FR]
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Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US7773008P | 2008-07-02 | 2008-07-02 | |
| GB0812120A GB2461546B (en) | 2008-07-02 | 2008-07-02 | Antigen binding polypeptides |
| US11016108P | 2008-10-31 | 2008-10-31 | |
| PCT/IB2009/006329 WO2010001251A2 (en) | 2008-07-02 | 2009-07-02 | Antigen binding polypeptides |
Publications (1)
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Families Citing this family (77)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8444976B2 (en) | 2008-07-02 | 2013-05-21 | Argen-X B.V. | Antigen binding polypeptides |
| GB2476681B (en) * | 2010-01-04 | 2012-04-04 | Argen X Bv | Humanized camelid VH, VK and VL immunoglobulin domains |
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| NZ604003A (en) | 2010-05-27 | 2015-04-24 | Genmab As | Monoclonal antibodies against her2 |
| ES2617446T3 (es) | 2010-09-27 | 2017-06-19 | Morphosys Ag | Anticuerpo anti-cd38 y lenalidomida o bortezomib para el tratamiento del mieloma múltiple y nhl |
| EP3165538A1 (en) | 2010-11-03 | 2017-05-10 | Argen-X Nv | Anti c-met antibodies |
| AU2011352207B2 (en) * | 2010-12-31 | 2016-03-03 | Bioatla, Llc | Comprehensive monoclonal antibody generation |
| CN103596979B (zh) * | 2011-03-16 | 2018-01-26 | 阿尔金-X有限公司 | 针对cd70的抗体 |
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| MA50516A (fr) | 2017-10-31 | 2020-09-09 | Staten Biotechnology B V | Anticorps anti-apoc3 et leurs procédés d'utilisation |
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| CN118696057A (zh) | 2021-06-14 | 2024-09-24 | 阿根思有限公司 | 抗il-9抗体及其使用方法 |
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| CN117310163B (zh) * | 2023-11-23 | 2024-02-13 | 北京贝思泰生物科技有限公司 | 一种基于重组抗体的呼吸道合胞病毒检测方法 |
| CN117986360B (zh) * | 2024-02-01 | 2024-08-27 | 生物岛实验室 | Il18蛋白的特异性抗体及其制备方法与应用 |
| CN119591719B (zh) * | 2024-11-25 | 2025-10-21 | 江苏集萃崛创生物科技研究所有限公司 | 靶向fap的纳米抗体、car-t细胞及其应用 |
| CN119708213B (zh) * | 2024-12-25 | 2025-12-12 | 河北科技师范学院 | 针对猪流行性腹泻病毒的纳米抗体或抗原结合片段及其应用 |
Family Cites Families (10)
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|---|---|---|---|---|
| ATE452975T1 (de) * | 1992-08-21 | 2010-01-15 | Univ Bruxelles | Immunoglobuline ohne leichte ketten |
| GB9926084D0 (en) * | 1999-11-03 | 2000-01-12 | King S College London | Recombinant fusion molecules |
| US7754208B2 (en) * | 2001-01-17 | 2010-07-13 | Trubion Pharmaceuticals, Inc. | Binding domain-immunoglobulin fusion proteins |
| US20050037420A1 (en) * | 2001-09-14 | 2005-02-17 | Mei-Yun Zhang | Immunoglobulin having particular framework scaffold and methods of making and using |
| ES2694247T3 (es) * | 2005-05-20 | 2018-12-19 | Ablynx N.V. | NanobodiesTM mejorados para el tratamiento de trastornos mediados por agregación |
| US20070269442A1 (en) * | 2006-05-19 | 2007-11-22 | Robert J. Webber | Chimeric monoclonal antibody recognizing iNOS |
| US8796429B2 (en) * | 2006-05-31 | 2014-08-05 | Lpath, Inc. | Bioactive lipid derivatives, and methods of making and using same |
| US7829674B2 (en) * | 2006-10-27 | 2010-11-09 | Lpath, Inc. | Compositions and methods for binding sphingosine-1-phosphate |
| US7732195B2 (en) * | 2006-11-01 | 2010-06-08 | Facet Biotech Corporation | Tethered vectors for cell surface immunoglobulin display |
| US8455626B2 (en) * | 2006-11-30 | 2013-06-04 | Abbott Laboratories | Aβ conformer selective anti-aβ globulomer monoclonal antibodies |
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| EP2310413A2 (en) | 2011-04-20 |
| EP3061768A1 (en) | 2016-08-31 |
| CN102216328A (zh) | 2011-10-12 |
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| GB2461546B (en) | 2010-07-07 |
| GB0812120D0 (en) | 2008-08-06 |
| CA2728076C (en) | 2020-05-19 |
| WO2010001251A3 (en) | 2010-03-11 |
| AU2009265278B2 (en) | 2015-03-19 |
| WO2010001251A2 (en) | 2010-01-07 |
| GB2461546A (en) | 2010-01-06 |
| EP2310413B1 (en) | 2017-03-01 |
| CN107739405A (zh) | 2018-02-27 |
| JP6216940B2 (ja) | 2017-10-25 |
| JP2011526493A (ja) | 2011-10-13 |
| AU2009265278A1 (en) | 2010-01-07 |
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