CA2856216C - Albumin binding antibodies and binding fragments thereof - Google Patents
Albumin binding antibodies and binding fragments thereof Download PDFInfo
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- CA2856216C CA2856216C CA2856216A CA2856216A CA2856216C CA 2856216 C CA2856216 C CA 2856216C CA 2856216 A CA2856216 A CA 2856216A CA 2856216 A CA2856216 A CA 2856216A CA 2856216 C CA2856216 C CA 2856216C
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Classifications
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- C—CHEMISTRY; METALLURGY
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- 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
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2878—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the NGF-receptor/TNF-receptor superfamily, e.g. CD27, CD30, CD40, CD95
-
- 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
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/31—Immunoglobulins specific features characterized by aspects of specificity or valency multispecific
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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
- C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
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- C07K2317/624—Disulfide-stabilized antibody (dsFv)
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Public Health (AREA)
- Chemical Kinetics & Catalysis (AREA)
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- Proteomics, Peptides & Aminoacids (AREA)
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- Pulmonology (AREA)
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- Physical Education & Sports Medicine (AREA)
- Biomedical Technology (AREA)
- Neurology (AREA)
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- Gastroenterology & Hepatology (AREA)
- Otolaryngology (AREA)
- Vascular Medicine (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Pain & Pain Management (AREA)
- Urology & Nephrology (AREA)
- Transplantation (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201161558559P | 2011-11-11 | 2011-11-11 | |
| US61/558,559 | 2011-11-11 | ||
| PCT/EP2012/072335 WO2013068571A1 (en) | 2011-11-11 | 2012-11-09 | Albumin binding antibodies and binding fragments thereof |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CA2856216A1 CA2856216A1 (en) | 2013-05-16 |
| CA2856216C true CA2856216C (en) | 2021-01-12 |
Family
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2856216A Active CA2856216C (en) | 2011-11-11 | 2012-11-09 | Albumin binding antibodies and binding fragments thereof |
Country Status (24)
| Country | Link |
|---|---|
| US (2) | US9803004B2 (en:Method) |
| EP (1) | EP2776466B1 (en:Method) |
| JP (1) | JP6411214B2 (en:Method) |
| KR (1) | KR102048382B1 (en:Method) |
| CN (1) | CN103946237B (en:Method) |
| AU (1) | AU2012335496B2 (en:Method) |
| BR (1) | BR112014011304B1 (en:Method) |
| CA (1) | CA2856216C (en:Method) |
| CY (1) | CY1119647T1 (en:Method) |
| DK (1) | DK2776466T3 (en:Method) |
| EA (1) | EA033766B1 (en:Method) |
| ES (1) | ES2649098T3 (en:Method) |
| HR (1) | HRP20171608T1 (en:Method) |
| HU (1) | HUE037142T2 (en:Method) |
| IL (1) | IL232226B (en:Method) |
| IN (1) | IN2014DN03451A (en:Method) |
| LT (1) | LT2776466T (en:Method) |
| MX (1) | MX351502B (en:Method) |
| NO (1) | NO2839445T3 (en:Method) |
| PL (1) | PL2776466T3 (en:Method) |
| PT (1) | PT2776466T (en:Method) |
| SG (1) | SG11201401649VA (en:Method) |
| SI (1) | SI2776466T1 (en:Method) |
| WO (1) | WO2013068571A1 (en:Method) |
Families Citing this family (46)
| Publication number | Priority date | Publication date | Assignee | Title |
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| UA112203C2 (uk) * | 2011-11-11 | 2016-08-10 | Юсб Фарма С.А. | Злитий білок біоспецифічного антитіла, який зв'язується з ox40 людини та сироватковим альбуміном людини |
| GB201208370D0 (en) | 2012-05-14 | 2012-06-27 | Ucb Pharma Sa | Antibodies |
| GB201223276D0 (en) | 2012-12-21 | 2013-02-06 | Ucb Pharma Sa | Antibodies and methods of producing same |
| PL3039038T3 (pl) * | 2013-08-30 | 2021-04-19 | Aprilbio Co., Ltd | Konstrukt fuzyjny z fab przeciwko albuminie surowicy i ugrupowania efektorowego oraz sposób jego przygotowania |
| GB201320066D0 (en) | 2013-11-13 | 2013-12-25 | Ucb Pharma Sa | Biological products |
| GB201411320D0 (en) * | 2014-06-25 | 2014-08-06 | Ucb Biopharma Sprl | Antibody construct |
| GB201506869D0 (en) * | 2015-04-22 | 2015-06-03 | Ucb Biopharma Sprl | Method |
| GB201506870D0 (en) * | 2015-04-22 | 2015-06-03 | Ucb Biopharma Sprl | Method |
| GB201506868D0 (en) | 2015-04-22 | 2015-06-03 | Ucb Biopharma Sprl | Method for protein purification |
| CN108137686B (zh) | 2015-05-07 | 2022-06-17 | 阿吉纳斯公司 | 抗ox40抗体及其使用方法 |
| GB201508180D0 (en) * | 2015-05-13 | 2015-06-24 | Ucb Biopharma Sprl | Antibodies |
| JP6937289B2 (ja) | 2015-07-06 | 2021-09-22 | ユーシービー バイオファルマ エスアールエル | Ｔａｕ結合抗体 |
| CA2991451A1 (en) | 2015-07-06 | 2017-01-12 | Ucb Biopharma Sprl | Tau-binding antibodies |
| EP3359688B1 (en) | 2015-10-05 | 2021-06-16 | UCB Biopharma SRL | Molecular signatures for use in diagnosis and response to treatment analysis of autoimmune diseases |
| IL299072A (en) | 2015-12-02 | 2023-02-01 | Memorial Sloan Kettering Cancer Center | Antibodies and methods of use thereof |
| GB201602938D0 (en) | 2016-02-19 | 2016-04-06 | Ucb Biopharma Sprl | Protein purification |
| EP3452506B1 (en) * | 2016-05-01 | 2025-04-16 | UCB Biopharma SRL | Affinity engineered serum protein carrier binding domain |
| GB201610198D0 (en) * | 2016-06-10 | 2016-07-27 | Ucb Biopharma Sprl | Anti-ige antibodies |
| EP3538152A4 (en) | 2016-11-09 | 2020-09-30 | Agenus Inc. | ANTI-OX40 ANTIBODIES, ANTI-GITR ANTIBODIES, AND PROCESSES FOR USE |
| MA47106A (fr) | 2016-12-21 | 2019-10-30 | Amgen Inc | Formulations d'anticorps anti-tnf alpha |
| HUE070957T2 (hu) * | 2017-02-16 | 2025-07-28 | Sonnet Biotherapeutics Inc | Albuminkötõ domén fúziós fehérjék |
| CN110709418B (zh) * | 2017-06-05 | 2023-09-26 | 努玛治疗有限公司 | 新型抗hsa抗体 |
| WO2018224439A1 (en) * | 2017-06-05 | 2018-12-13 | Numab Innovation Ag | Novel anti-hsa antibodies |
| GB201711481D0 (en) | 2017-07-17 | 2017-08-30 | Ucb Biopharma Sprl | Protein purification |
| KR102204315B1 (ko) * | 2018-11-16 | 2021-01-18 | 한국세라믹기술원 | 인간 혈청 알부민에 특이적으로 결합하는 어피바디 및 그의 용도 |
| CN114401984B (zh) | 2019-08-02 | 2025-05-06 | Ucb生物制药有限责任公司 | 纯化抗体的方法 |
| CN112409480B (zh) * | 2019-08-20 | 2024-08-27 | 四川科伦博泰生物医药股份有限公司 | 结合血清白蛋白的蛋白及其用途 |
| GB201919058D0 (en) * | 2019-12-20 | 2020-02-05 | Ucb Biopharma Sprl | Multi-specific antibodies |
| GB201919062D0 (en) | 2019-12-20 | 2020-02-05 | Ucb Biopharma Sprl | Antibody |
| GB201919061D0 (en) * | 2019-12-20 | 2020-02-05 | Ucb Biopharma Sprl | Multi-specific antibody |
| GB202001447D0 (en) | 2020-02-03 | 2020-03-18 | Ucb Biopharma Sprl | Antibodies |
| CA3175034A1 (en) | 2020-03-27 | 2021-09-30 | UCB Biopharma SRL | Autonomous knob domain peptides |
| KR102367488B1 (ko) * | 2020-06-29 | 2022-02-25 | 주식회사 프로테인웍스 | 단일사슬항체-알부민 약물 복합체의 분석방법 |
| KR20230087552A (ko) | 2020-10-15 | 2023-06-16 | 유씨비 바이오파마 에스알엘 | Cd45를 다량체화하는 결합 분자 |
| AR124250A1 (es) | 2020-12-07 | 2023-03-01 | UCB Biopharma SRL | Anticuerpos |
| WO2022122654A1 (en) | 2020-12-07 | 2022-06-16 | UCB Biopharma SRL | Multi-specific antibodies and antibody combinations |
| CN115181751A (zh) * | 2021-04-02 | 2022-10-14 | 苏州博腾生物制药有限公司 | 靶向白蛋白的嵌合抗原受体及其使用方法 |
| US20240254224A1 (en) | 2021-05-03 | 2024-08-01 | UCB Biopharma SRL | Antibodies |
| TW202313685A (zh) * | 2021-06-07 | 2023-04-01 | 大陸商上海濟煜醫藥科技有限公司 | 抗人血清白蛋白的抗原結合蛋白 |
| GB202111905D0 (en) | 2021-08-19 | 2021-10-06 | UCB Biopharma SRL | Antibodies |
| CA3259309A1 (en) | 2022-06-15 | 2023-12-21 | UCB Biopharma SRL | Fusion protein for the prevention, treatment or improvement of kidney disease |
| AR129610A1 (es) | 2022-06-15 | 2024-09-11 | UCB Biopharma SRL | Proteínas de fusión |
| GB202318820D0 (en) | 2023-12-08 | 2024-01-24 | UCB Biopharma SRL | Antibodies |
| US12134635B1 (en) | 2023-12-29 | 2024-11-05 | Sonnet BioTherapeutics, Inc. | Interleukin 18 (IL-18) variants and fusion proteins comprising same |
| WO2025238135A2 (en) | 2024-05-17 | 2025-11-20 | UCB Biopharma SRL | Antibody with binding specificity for il-11 |
| WO2025238133A1 (en) | 2024-05-17 | 2025-11-20 | UCB Biopharma SRL | Multispecific antibody with binding specificity for il-11 and il-17 |
Family Cites Families (64)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US5677425A (en) | 1987-09-04 | 1997-10-14 | Celltech Therapeutics Limited | Recombinant antibody |
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| WO1990002809A1 (en) | 1988-09-02 | 1990-03-22 | Protein Engineering Corporation | Generation and selection of recombinant varied binding proteins |
| GB8823869D0 (en) | 1988-10-12 | 1988-11-16 | Medical Res Council | Production of antibodies |
| 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 |
| US6267964B1 (en) | 1989-08-01 | 2001-07-31 | Affibody Technology Sweden Ab | Stabilized protein or peptide conjugates able to bond albumin having extended biological half-lives |
| SE509359C2 (sv) | 1989-08-01 | 1999-01-18 | Cemu Bioteknik Ab | Användning av stabiliserade protein- eller peptidkonjugat för framställning av ett läkemedel |
| GB8928874D0 (en) | 1989-12-21 | 1990-02-28 | Celltech Ltd | Humanised antibodies |
| US5780225A (en) | 1990-01-12 | 1998-07-14 | Stratagene | Method for generating libaries of antibody genes comprising amplification of diverse antibody DNAs and methods for using these libraries for the production of diverse antigen combining molecules |
| AU7247191A (en) | 1990-01-11 | 1991-08-05 | Molecular Affinities Corporation | Production of antibodies using gene libraries |
| EP0463151B1 (en) | 1990-01-12 | 1996-06-12 | Cell Genesys, Inc. | Generation of xenogeneic antibodies |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| WO1992002551A1 (en) | 1990-08-02 | 1992-02-20 | B.R. Centre Limited | Methods for the production of proteins with a desired function |
| US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
| US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic 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 |
| DE69133476T2 (de) | 1990-08-29 | 2006-01-05 | GenPharm International, Inc., Palo Alto | Transgene Mäuse fähig zur Produktion heterologer Antikörper |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| US5698426A (en) | 1990-09-28 | 1997-12-16 | Ixsys, Incorporated | Surface expression libraries of heteromeric receptors |
| CA2405246A1 (en) | 1990-12-03 | 1992-06-11 | Genentech, Inc. | Enrichment method for variant proteins with alterred binding properties |
| DE69233367T2 (de) | 1991-04-10 | 2005-05-25 | The Scripps Research Institute, La Jolla | Bibliotheken heterodimerer rezeptoren mittels phagemiden |
| GB9112536D0 (en) | 1991-06-11 | 1991-07-31 | Celltech Ltd | Chemical compounds |
| GB9113120D0 (en) | 1991-06-18 | 1991-08-07 | Kodak Ltd | Photographic processing apparatus |
| PT1024191E (pt) | 1991-12-02 | 2008-12-22 | Medical Res Council | Produção de auto-anticorpos a partir de reportórios de segmentos de anticorpo e exibidos em fagos |
| US5733743A (en) | 1992-03-24 | 1998-03-31 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| DE69334275D1 (de) | 1992-08-21 | 2009-05-20 | Univ Bruxelles | Immunoglobuline ohne Leichtkette |
| EP0733070A1 (en) | 1993-12-08 | 1996-09-25 | Genzyme Corporation | Process for generating specific antibodies |
| PT1231268E (pt) | 1994-01-31 | 2005-11-30 | Univ Boston | Bancos de anticorpos policlonais |
| US5516637A (en) | 1994-06-10 | 1996-05-14 | Dade International Inc. | Method involving display of protein binding pairs on the surface of bacterial pili and bacteriophage |
| JP2978435B2 (ja) | 1996-01-24 | 1999-11-15 | チッソ株式会社 | アクリロキシプロピルシランの製造方法 |
| DE69731289D1 (de) | 1996-03-18 | 2004-11-25 | Univ Texas | Immunglobulinähnliche domäne mit erhöhten halbwertszeiten |
| GB9625640D0 (en) | 1996-12-10 | 1997-01-29 | Celltech Therapeutics Ltd | Biological products |
| DE19653722C2 (de) | 1996-12-10 | 2000-06-29 | Brose Fahrzeugteile | Beidseitig wirkende Verstellvorrichtung |
| BR9807464A (pt) | 1997-02-21 | 2000-05-09 | Genentech Inc | Conjugado, composição, molécula de ácido nucleico, vetor de expressão, célula hospedeira, método para produzir um polipeptìdeo e polipeptìdeo. |
| GB9720054D0 (en) | 1997-09-19 | 1997-11-19 | Celltech Therapeutics Ltd | Biological products |
| PT1049787E (pt) | 1998-01-23 | 2005-04-29 | Vlaams Interuniv Inst Biotech | Derivados de anticorpos multipropositos |
| GB9812545D0 (en) | 1998-06-10 | 1998-08-05 | Celltech Therapeutics Ltd | Biological products |
| ATE337403T1 (de) | 1999-12-24 | 2006-09-15 | Genentech Inc | Verfahren und verbindungen zur verlängerung der halbwertzeiten bei der ausscheidung von biowirksamen verbindungen |
| JP4336771B2 (ja) | 2001-03-09 | 2009-09-30 | モルフォシス アーゲー | 血清アルブミン結合部分 |
| CA2490009A1 (en) | 2002-06-21 | 2003-12-31 | Dyax Corporation | Serum protein-associated target-specific ligands and identification method therefor |
| CN1678634A (zh) | 2002-06-28 | 2005-10-05 | 多曼蒂斯有限公司 | 免疫球蛋白单个变体抗原结合区及其特异性构建体 |
| US9321832B2 (en) | 2002-06-28 | 2016-04-26 | Domantis Limited | Ligand |
| EP1570267B1 (en) | 2002-12-03 | 2011-10-12 | UCB Pharma, S.A. | Assay for identifying antibody producing cells |
| GB0312481D0 (en) | 2003-05-30 | 2003-07-09 | Celltech R&D Ltd | Antibodies |
| GB0315450D0 (en) | 2003-07-01 | 2003-08-06 | Celltech R&D Ltd | Biological products |
| GB0315457D0 (en) | 2003-07-01 | 2003-08-06 | Celltech R&D Ltd | Biological products |
| HRP20151252T4 (hr) | 2003-07-01 | 2018-11-30 | Ucb Biopharma Sprl | Modificirani fab ulomci protutijela |
| GB0411186D0 (en) | 2004-05-19 | 2004-06-23 | Celltech R&D Ltd | Biological products |
| KR20070039911A (ko) | 2004-06-01 | 2007-04-13 | 도만티스 리미티드 | 증강된 혈청 반감기를 가지는 이특이성 융합 항체 |
| CA2588292C (en) | 2004-12-01 | 2019-01-15 | Health Protection Agency | Non-cytotoxic protein conjugates |
| GB0506912D0 (en) | 2005-04-05 | 2005-05-11 | Celltech R&D Ltd | Biological products |
| ES2667729T3 (es) | 2007-09-26 | 2018-05-14 | Ucb Biopharma Sprl | Fusiones de anticuerpos con doble especificidad |
| EA201100527A1 (ru) | 2008-09-26 | 2011-10-31 | Юсб Фарма С.А. | Биологические продукты |
| HRP20181932T1 (hr) | 2009-02-17 | 2019-01-25 | Ucb Biopharma Sprl | Molekule protutijela koje imaju specifičnost za ljudski ox40 |
| CA2768462A1 (en) | 2009-07-16 | 2011-01-20 | Glaxo Group Ltd. | Improved anti-serum albumin binding single variable domains |
| WO2011030107A1 (en) * | 2009-09-10 | 2011-03-17 | Ucb Pharma S.A. | Multivalent antibodies |
| GB201005063D0 (en) * | 2010-03-25 | 2010-05-12 | Ucb Pharma Sa | Biological products |
| GB0920127D0 (en) * | 2009-11-17 | 2009-12-30 | Ucb Pharma Sa | Antibodies |
| GB201000467D0 (en) | 2010-01-12 | 2010-02-24 | Ucb Pharma Sa | Antibodies |
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