ES2600854T3 - Proteínas de unión a antígeno de TNF-alfa con unión a FcRn incrementada para su uso en terapia - Google Patents
Proteínas de unión a antígeno de TNF-alfa con unión a FcRn incrementada para su uso en terapia Download PDFInfo
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- ES2600854T3 ES2600854T3 ES12738101.0T ES12738101T ES2600854T3 ES 2600854 T3 ES2600854 T3 ES 2600854T3 ES 12738101 T ES12738101 T ES 12738101T ES 2600854 T3 ES2600854 T3 ES 2600854T3
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- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
Classifications
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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
- C07K16/241—Tumor Necrosis Factors
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
- A61K39/39591—Stabilisation, fragmentation
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- 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
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/40—Immunoglobulins specific features characterized by post-translational modification
- C07K2317/41—Glycosylation, sialylation, or fucosylation
-
- 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
- C07K2317/565—Complementarity determining region [CDR]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/71—Decreased effector function due to an Fc-modification
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/72—Increased effector function due to an Fc-modification
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
-
- 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
-
- 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
-
- 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
- C07K2317/94—Stability, e.g. half-life, pH, temperature or enzyme-resistance
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Medicinal Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Microbiology (AREA)
- Rheumatology (AREA)
- Mycology (AREA)
- Epidemiology (AREA)
- Physical Education & Sports Medicine (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Pain & Pain Management (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicinal Preparation (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB201112429 | 2011-07-19 | ||
| GBGB1112429.4A GB201112429D0 (en) | 2011-07-19 | 2011-07-19 | Antigen-binding proteins with increased FcRn binding |
| PCT/EP2012/064129 WO2013011076A2 (en) | 2011-07-19 | 2012-07-19 | Antigen-binding proteins with increased fcrn binding |
Publications (1)
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| ES2600854T3 true ES2600854T3 (es) | 2017-02-13 |
Family
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Family Applications (1)
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| EP (2) | EP2734548B1 (enExample) |
| JP (1) | JP2014524748A (enExample) |
| KR (1) | KR20140054085A (enExample) |
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| BR (1) | BR112014000341A2 (enExample) |
| CA (1) | CA2841105A1 (enExample) |
| CL (1) | CL2014000134A1 (enExample) |
| CO (1) | CO6862106A2 (enExample) |
| CR (1) | CR20140029A (enExample) |
| DO (1) | DOP2014000007A (enExample) |
| EA (1) | EA201391789A1 (enExample) |
| ES (1) | ES2600854T3 (enExample) |
| GB (1) | GB201112429D0 (enExample) |
| MA (1) | MA35345B1 (enExample) |
| MX (1) | MX2014000739A (enExample) |
| PE (1) | PE20141660A1 (enExample) |
| PH (1) | PH12014500167A1 (enExample) |
| SG (1) | SG10201601154QA (enExample) |
| WO (1) | WO2013011076A2 (enExample) |
| ZA (1) | ZA201400062B (enExample) |
Families Citing this family (59)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA2385745C (en) | 2001-06-08 | 2015-02-17 | Abbott Laboratories (Bermuda) Ltd. | Methods of administering anti-tnf.alpha. antibodies |
| UY33679A (es) | 2010-10-22 | 2012-03-30 | Esbatech | Anticuerpos estables y solubles |
| US9062106B2 (en) | 2011-04-27 | 2015-06-23 | Abbvie Inc. | Methods for controlling the galactosylation profile of recombinantly-expressed proteins |
| AP2014007922A0 (en) | 2012-03-07 | 2014-09-30 | Cadila Healthcare Ltd | Pharmaceutical formulations of TNF-alpha antibodies |
| US9067990B2 (en) | 2013-03-14 | 2015-06-30 | Abbvie, Inc. | Protein purification using displacement chromatography |
| US9181572B2 (en) | 2012-04-20 | 2015-11-10 | Abbvie, Inc. | Methods to modulate lysine variant distribution |
| WO2013158275A1 (en) * | 2012-04-20 | 2013-10-24 | Abbvie Inc. | Cell culture methods to reduce acidic species |
| US9334319B2 (en) | 2012-04-20 | 2016-05-10 | Abbvie Inc. | Low acidic species compositions |
| US9249182B2 (en) | 2012-05-24 | 2016-02-02 | Abbvie, Inc. | Purification of antibodies using hydrophobic interaction chromatography |
| US20150150982A1 (en) * | 2012-06-12 | 2015-06-04 | Boehringer Ingelheim International Gmbh | Pharmaceutical formulation for a therapeutic antibody |
| US9512214B2 (en) | 2012-09-02 | 2016-12-06 | Abbvie, Inc. | Methods to control protein heterogeneity |
| EP2890782A1 (en) | 2012-09-02 | 2015-07-08 | AbbVie Inc. | Methods to control protein heterogeneity |
| PE20191815A1 (es) | 2012-09-07 | 2019-12-27 | Coherus Biosciences Inc | Formulaciones acuosas estables de adalimumab |
| WO2014096672A1 (fr) * | 2012-12-17 | 2014-06-26 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Utilisation d'anticorps monoclonaux pour le traitement de l'inflammation et d'infections bacteriennes |
| FR2999431B1 (fr) * | 2012-12-17 | 2016-03-18 | Lfb Biotechnologies | Utilisation d'anticorps monoclonaux pour le traitement de l'inflammation et d'infections bacteriennes |
| AU2014209994B2 (en) * | 2013-01-24 | 2017-03-16 | Glaxosmithkline Intellectual Property Development Limited | TNF-alpha antigen-binding proteins |
| SG11201507230PA (en) | 2013-03-12 | 2015-10-29 | Abbvie Inc | Human antibodies that bind human tnf-alpha and methods of preparing the same |
| WO2014151878A2 (en) | 2013-03-14 | 2014-09-25 | Abbvie Inc. | Methods for modulating protein glycosylation profiles of recombinant protein therapeutics using monosaccharides and oligosacharides |
| WO2014159579A1 (en) | 2013-03-14 | 2014-10-02 | Abbvie Inc. | MUTATED ANTI-TNFα ANTIBODIES AND METHODS OF THEIR USE |
| WO2014158231A1 (en) * | 2013-03-14 | 2014-10-02 | Abbvie Inc. | Low acidic species compositions and methods for producing and using the same |
| US9017687B1 (en) | 2013-10-18 | 2015-04-28 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same using displacement chromatography |
| AU2014291970B2 (en) * | 2013-07-19 | 2017-09-28 | Hexal Ag | Methods and formulations which allow the modulation of immune responses related to the administration of a biopharmaceutical drug |
| WO2015051293A2 (en) | 2013-10-04 | 2015-04-09 | Abbvie, Inc. | Use of metal ions for modulation of protein glycosylation profiles of recombinant proteins |
| CA2926588C (en) | 2013-10-16 | 2020-07-21 | Oncobiologics, Inc. | Buffer formulations for enhanced antibody stability |
| US9085618B2 (en) | 2013-10-18 | 2015-07-21 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same |
| US9181337B2 (en) | 2013-10-18 | 2015-11-10 | Abbvie, Inc. | Modulated lysine variant species compositions and methods for producing and using the same |
| US8946395B1 (en) | 2013-10-18 | 2015-02-03 | Abbvie Inc. | Purification of proteins using hydrophobic interaction chromatography |
| US20150139988A1 (en) | 2013-11-15 | 2015-05-21 | Abbvie, Inc. | Glycoengineered binding protein compositions |
| ES2572919T3 (es) | 2014-05-23 | 2016-06-03 | Ares Trading S.A. | Composición farmacéutica líquida |
| LT2946765T (lt) | 2014-05-23 | 2016-11-25 | Ares Trading S.A. | Skysta farmacinė kompozicija |
| ES2607489T3 (es) | 2014-05-23 | 2017-03-31 | Ares Trading S.A. | Composición farmacéutica líquida |
| CA2959629C (en) * | 2014-09-03 | 2023-10-31 | Boehringer Ingelheim International Gmbh | Compound targeting il-23a and tnf-alpha and uses thereof |
| HUP1400510A1 (hu) * | 2014-10-28 | 2016-05-30 | Richter Gedeon Nyrt | Gyógyászati TNFalfa ellenes antitest készítmény |
| EP3247718B1 (en) | 2015-01-21 | 2021-09-01 | Outlook Therapeutics, Inc. | Modulation of charge variants in a monoclonal antibody composition |
| EP3250598A1 (en) * | 2015-01-28 | 2017-12-06 | Mabxience S.A. | Pharmaceutical formulations for anti-tnf-alpha antibodies |
| WO2016189491A1 (en) * | 2015-05-28 | 2016-12-01 | Glaxosmithkline Intellectual Property Development Limited | Novel formulation |
| US11229702B1 (en) | 2015-10-28 | 2022-01-25 | Coherus Biosciences, Inc. | High concentration formulations of adalimumab |
| GB201522394D0 (en) | 2015-12-18 | 2016-02-03 | Ucb Biopharma Sprl | Antibodies |
| WO2017110980A1 (ja) * | 2015-12-25 | 2017-06-29 | 中外製薬株式会社 | 増強された活性を有する抗体及びその改変方法 |
| WO2017136433A1 (en) | 2016-02-03 | 2017-08-10 | Oncobiologics, Inc. | Buffer formulations for enhanced antibody stability |
| EP3430039B1 (en) | 2016-03-14 | 2025-10-22 | Universitetet I Oslo | Engineered immunoglobulins with altered fcrn binding |
| WO2017184880A1 (en) | 2016-04-20 | 2017-10-26 | Coherus Biosciences, Inc. | A method of filling a container with no headspace |
| JP7320943B2 (ja) | 2016-04-28 | 2023-08-04 | 中外製薬株式会社 | 抗体含有製剤 |
| KR102777127B1 (ko) | 2016-08-02 | 2025-03-07 | 비스테라, 인크. | 조작된 폴리펩티드 및 그의 용도 |
| TWI778985B (zh) | 2016-10-20 | 2022-10-01 | 法商賽諾菲公司 | 抗chikv抗體及其用途 |
| US10980881B2 (en) * | 2017-01-11 | 2021-04-20 | Celltrion Inc. | Stable liquid formula having an anti-TNFalpha antibody, acetate buffer and glycine |
| JP6974500B2 (ja) * | 2017-01-13 | 2021-12-01 | ハンクス バイオファーマシューティクス，インコーポレイテッド | ＦｃＲｎに対するＩｇＧ様抗体の結合親和性を増加し、その血清半減期を延長させる方法 |
| US11608357B2 (en) | 2018-08-28 | 2023-03-21 | Arecor Limited | Stabilized antibody protein solutions |
| EP3372241A1 (en) | 2017-03-06 | 2018-09-12 | Ares Trading S.A. | Liquid pharmaceutical composition |
| EP3372242A1 (en) * | 2017-03-06 | 2018-09-12 | Ares Trading S.A. | Liquid pharmaceutical composition |
| WO2019033087A1 (en) * | 2017-08-11 | 2019-02-14 | Research Development Foundation | MODIFIED FC ANTIBODY VARIANTS FOR ENHANCED SERIAL HALF LIFE |
| KR20190024572A (ko) * | 2017-08-30 | 2019-03-08 | (주)셀트리온 | TNFα 관련 질환을 치료하기 위한 피하 투여 요법 |
| IL273592B2 (en) | 2017-09-29 | 2025-11-01 | Chugai Pharmaceutical Co Ltd | Multispecific antigen-binding molecule having blood coagulation factor viii (fviii) cofactor function-substituting activity, and pharmaceutical formulation containing said molecule as active ingredient |
| MX2020003472A (es) | 2017-11-01 | 2020-08-03 | Chugai Pharmaceutical Co Ltd | Variante e isoforma de anticuerpos con actividad biologica reducida. |
| CN111788221A (zh) * | 2018-01-26 | 2020-10-16 | 建新公司 | 具有与FcRn增强的结合及延长的半衰期的Fc变体 |
| CA3128360A1 (en) * | 2019-03-05 | 2020-09-10 | Yuval CINNAMON | Genome-edited birds |
| CN115770291A (zh) * | 2021-09-08 | 2023-03-10 | 珠海市丽珠单抗生物技术有限公司 | 新型冠状病毒SARS-CoV-2疫苗加强免疫及其应用 |
| CN115770292A (zh) * | 2021-09-08 | 2023-03-10 | 珠海市丽珠单抗生物技术有限公司 | 新型冠状病毒SARS-CoV-2的协同免疫及其用途 |
| AU2022401939A1 (en) * | 2021-11-30 | 2024-05-30 | Jiangsu Hengrui Pharmaceuticals Co., Ltd. | Anti-sost antibody pharmaceutical composition and use thereof |
Family Cites Families (26)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| US6090382A (en) | 1996-02-09 | 2000-07-18 | Basf Aktiengesellschaft | Human antibodies that bind human TNFα |
| DK0929578T3 (da) * | 1996-02-09 | 2003-08-25 | Abbott Lab Bermuda Ltd | Humane antistoffer, der binder human TNFalfa |
| CA2249195A1 (en) | 1996-03-18 | 1997-09-25 | Board Of Regents, The University Of Texas System | Immunoglobin-like domains with increased half lives |
| CN1763097B (zh) | 1999-01-15 | 2011-04-13 | 杰南技术公司 | 具有改变的效应功能的多肽变体 |
| US7658921B2 (en) * | 2000-12-12 | 2010-02-09 | Medimmune, Llc | Molecules with extended half-lives, compositions and uses thereof |
| WO2002060919A2 (en) * | 2000-12-12 | 2002-08-08 | Medimmune, Inc. | Molecules with extended half-lives, compositions and uses thereof |
| US20040033228A1 (en) * | 2002-08-16 | 2004-02-19 | Hans-Juergen Krause | Formulation of human antibodies for treating TNF-alpha associated disorders |
| DE60334141D1 (de) | 2002-10-15 | 2010-10-21 | Facet Biotech Corp | VERÄNDERUNG VON FcRn-BINDUNGSAFFINITÄTEN ODER VON SERUMHALBWERTSZEITEN VON ANTIKÖRPERN MITTELS MUTAGENESE |
| US8367805B2 (en) * | 2004-11-12 | 2013-02-05 | Xencor, Inc. | Fc variants with altered binding to FcRn |
| WO2006130834A2 (en) | 2005-05-31 | 2006-12-07 | Board Of Regents, The University Of Texas System | IGGl ANTIBODIES WITH MUTATED FC PORTION FOR INCREASED BINDING TO FCRN RECEPTOR AND USES THEREOF |
| SG176427A1 (en) * | 2006-10-27 | 2011-12-29 | Abbott Biotech Ltd | Crystalline anti-htnfalpha antibodies |
| JP5592258B2 (ja) | 2007-08-20 | 2014-09-17 | グラクソ グループ リミテッド | 製造方法 |
| GB2468232B (en) * | 2007-11-30 | 2012-10-24 | Glaxo Group Ltd | Antigen-bindng constructs |
| JP5840364B2 (ja) * | 2007-11-30 | 2016-01-06 | アッヴィ バイオテクノロジー リミテッド | タンパク質製剤及びその製造方法 |
| WO2009073805A2 (en) * | 2007-12-04 | 2009-06-11 | Verdezyne, Inc. | Aglycosylated therapeutic antibodies and therapeutic antibody-encoding nucleotide sequences |
| HUE024903T2 (en) * | 2007-12-26 | 2016-02-29 | Xencor Inc | Fc variants with altered binding to fcrn |
| JP5570998B2 (ja) * | 2007-12-31 | 2014-08-13 | バイエル・インテレクチュアル・プロパティ・ゲゼルシャフト・ミット・ベシュレンクテル・ハフツング | ＴＮＦαに対する抗体 |
| FR2934599B1 (fr) | 2008-07-29 | 2012-12-21 | Arkema France | Fabrication de polyethylene a partir de matieres renouvelables, polyethylene obtenu et utilisations |
| WO2010077422A2 (en) * | 2008-10-29 | 2010-07-08 | Wyeth Llc | Formulations of single domain antigen binding molecules |
| JP2012518398A (ja) * | 2009-02-24 | 2012-08-16 | グラクソ グループ リミテッド | 抗原結合性構築物 |
| SG10201402960SA (en) * | 2009-03-05 | 2014-08-28 | Abbvie Inc | IL-17 Binding Proteins |
| RU2560701C2 (ru) | 2009-05-04 | 2015-08-20 | Эббви Байотекнолоджи Лтд. | Стабильные композиции с высокими концентрациями белков антител человека против tnf-альфа |
| EP2435075A2 (en) * | 2009-05-28 | 2012-04-04 | Glaxo Group Limited | Antigen-binding proteins |
| WO2011074965A1 (en) * | 2009-12-17 | 2011-06-23 | Stichting Sanquin Bloedvoorziening | Methods and means for counteracting an activity of an fc domain |
| SG2014015069A (en) | 2010-11-11 | 2014-07-30 | Abbvie Biotechnology Ltd | IMPROVED HIGH CONCENTRATION ANTI-TNFα ANTIBODY LIQUID FORMULATIONS |
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2012
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- 2012-07-19 KR KR1020147004161A patent/KR20140054085A/ko not_active Withdrawn
- 2012-07-19 CN CN201280034887.5A patent/CN103748110A/zh active Pending
- 2012-07-19 ES ES12738101.0T patent/ES2600854T3/es active Active
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- 2012-07-19 MX MX2014000739A patent/MX2014000739A/es unknown
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- 2012-07-19 EP EP15197750.1A patent/EP3009450A1/en not_active Withdrawn
- 2012-07-19 AU AU2012285786A patent/AU2012285786B2/en not_active Ceased
- 2012-07-19 US US13/988,400 patent/US20130243764A1/en not_active Abandoned
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2014
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- 2014-01-21 CO CO14011137A patent/CO6862106A2/es not_active Application Discontinuation
- 2014-02-12 MA MA36748A patent/MA35345B1/fr unknown
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| MX2014000739A (es) | 2014-02-19 |
| WO2013011076A2 (en) | 2013-01-24 |
| CN103748110A (zh) | 2014-04-23 |
| EP2734548B1 (en) | 2016-08-17 |
| CA2841105A1 (en) | 2013-01-24 |
| AU2012285786B2 (en) | 2016-05-12 |
| JP2014524748A (ja) | 2014-09-25 |
| PH12014500167A1 (en) | 2019-03-22 |
| EA201391789A1 (ru) | 2014-06-30 |
| KR20140054085A (ko) | 2014-05-08 |
| MA35345B1 (fr) | 2014-08-01 |
| WO2013011076A3 (en) | 2013-04-04 |
| EP3009450A1 (en) | 2016-04-20 |
| US20130243764A1 (en) | 2013-09-19 |
| EP2734548A2 (en) | 2014-05-28 |
| AU2012285786A1 (en) | 2014-02-06 |
| GB201112429D0 (en) | 2011-08-31 |
| CO6862106A2 (es) | 2014-02-10 |
| CR20140029A (es) | 2014-03-05 |
| ZA201400062B (en) | 2017-08-30 |
| CL2014000134A1 (es) | 2014-07-25 |
| PE20141660A1 (es) | 2014-11-21 |
| NZ618897A (en) | 2016-02-26 |
| BR112014000341A2 (pt) | 2017-02-14 |
| SG10201601154QA (en) | 2016-03-30 |
| DOP2014000007A (es) | 2014-04-30 |
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