TWI832808B - 中和抗tl1a之單株抗體 - Google Patents
中和抗tl1a之單株抗體 Download PDFInfo
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- TWI832808B TWI832808B TW106136987A TW106136987A TWI832808B TW I832808 B TWI832808 B TW I832808B TW 106136987 A TW106136987 A TW 106136987A TW 106136987 A TW106136987 A TW 106136987A TW I832808 B TWI832808 B TW I832808B
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- antibody
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- tl1a
- antibodies
- chain variable
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- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
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- C—CHEMISTRY; METALLURGY
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- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
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- C07K2317/565—Complementarity determining region [CDR]
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- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
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- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
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| AU2020275413A1 (en) | 2019-05-14 | 2021-12-23 | Cedars-Sinai Medical Center | TL1A patient selection methods, systems, and devices |
| KR20220103721A (ko) * | 2019-10-24 | 2022-07-22 | 프로메테우스 바이오사이언시즈, 인크. | Tnf 유사 리간드 1a(tl1a)에 대한 인간화 항체 및 그의 용도 |
| KR20230025898A (ko) * | 2020-06-26 | 2023-02-23 | 화이자 인코포레이티드 | Tl1a 항체를 사용하여 염증성 장 질환을 치료하는 방법 |
| WO2022235295A1 (en) * | 2021-05-07 | 2022-11-10 | Kiromic BioPharma, Inc. | Mesothelin isoform binding molecules and chimeric pd1 receptor molecules, cells containing the same and uses thereof |
| AU2024273758A1 (en) | 2023-05-17 | 2025-12-04 | Genentech, Inc. | Anti-tl1a antibody therapeutic methods |
| WO2025038473A1 (en) * | 2023-08-11 | 2025-02-20 | Paragon Therapeutics, Inc. | Tl1a binding antibodies and methods of use |
| US12473370B2 (en) | 2023-10-03 | 2025-11-18 | Absci Corporation | TL1A associated antibody compositions and methods of use |
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| WO2025240922A1 (en) | 2024-05-17 | 2025-11-20 | Genentech, Inc. | Methods for treatment of inflammatory bowel disease with an anti-tl1a antibody |
| CN119390843B (zh) * | 2025-01-03 | 2025-04-15 | 华润生物医药有限公司 | 抗tl1a抗体及其制备方法和应用 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2014106602A1 (en) * | 2013-01-02 | 2014-07-10 | Glenmark Pharmaceuticals S.A. | Antibodies that bind to tl1a and their uses |
| US20160053007A1 (en) * | 2007-01-10 | 2016-02-25 | The Usa, As Represented By The Secretary, Dept. Of Health And Human Services | Antibodies that bind to tl1a and methods of treating inflammatory or autoimmune disease comprising administering such antibodies |
Family Cites Families (86)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4737462A (en) | 1982-10-19 | 1988-04-12 | Cetus Corporation | Structural genes, plasmids and transformed cells for producing cysteine depleted muteins of interferon-β |
| US4518584A (en) | 1983-04-15 | 1985-05-21 | Cetus Corporation | Human recombinant interleukin-2 muteins |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| US4946778A (en) | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| EP0307434B2 (en) | 1987-03-18 | 1998-07-29 | Scotgen Biopharmaceuticals, Inc. | Altered antibodies |
| GB8823869D0 (en) | 1988-10-12 | 1988-11-16 | Medical Res Council | Production of antibodies |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| 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 |
| US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| JP2938569B2 (ja) | 1990-08-29 | 1999-08-23 | ジェンファーム インターナショナル，インコーポレイティド | 異種免疫グロブリンを作る方法及びトランスジェニックマウス |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| 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 |
| US6277969B1 (en) | 1991-03-18 | 2001-08-21 | New York University | Anti-TNF antibodies and peptides of human tumor necrosis factor |
| CA2103059C (en) | 1991-06-14 | 2005-03-22 | Paul J. Carter | Method for making humanized antibodies |
| WO1993011236A1 (en) | 1991-12-02 | 1993-06-10 | Medical Research Council | Production of anti-self antibodies from antibody segment repertoires and displayed on phage |
| GB9325182D0 (en) | 1993-12-08 | 1994-02-09 | T Cell Sciences Inc | Humanized antibodies or binding proteins thereof specific for t cell subpopulations exhibiting select beta chain variable regions |
| JP4046349B2 (ja) | 1994-11-07 | 2008-02-13 | ヒューマン ジノーム サイエンシーズ， インコーポレイテッド | 腫瘍壊死因子−γ |
| US7820798B2 (en) | 1994-11-07 | 2010-10-26 | Human Genome Sciences, Inc. | Tumor necrosis factor-gamma |
| US20030129189A1 (en) | 1994-11-07 | 2003-07-10 | Guo-Liang Yu | Tumor necrosis factor-gamma |
| US6824767B2 (en) | 1994-11-07 | 2004-11-30 | Human Genome Sciences, Inc. | Tumor necrosis factor-gamma |
| US6599719B2 (en) | 1994-11-07 | 2003-07-29 | Human Genome Sciences, Inc. | Nucleic acid molecules encoding tumor necrosis factor-gamma-alpha |
| US7597886B2 (en) | 1994-11-07 | 2009-10-06 | Human Genome Sciences, Inc. | Tumor necrosis factor-gamma |
| US20030198640A1 (en) | 1994-11-07 | 2003-10-23 | Human Genome Sciences, Inc. | Methods and compositions for treating inflammatory bowel diseases relating to human tumor necrosis factor-gamma-beta |
| WO2000066608A1 (en) | 1999-04-30 | 2000-11-09 | Human Genome Sciences, Inc. | Tumor necrosis factor-gamma |
| US7264963B1 (en) | 1995-08-18 | 2007-09-04 | Morphosys Ag | Protein(poly)peptide libraries |
| ES2176484T3 (es) | 1995-08-18 | 2002-12-01 | Morphosys Ag | Bancos de proteinas/(poli)peptidos. |
| US6632976B1 (en) | 1995-08-29 | 2003-10-14 | Kirin Beer Kabushiki Kaisha | Chimeric mice that are produced by microcell mediated chromosome transfer and that retain a human antibody gene |
| US7357927B2 (en) | 1996-03-12 | 2008-04-15 | Human Genome Sciences, Inc. | Death domain containing receptors |
| ATE531812T1 (de) | 1997-12-05 | 2011-11-15 | Scripps Research Inst | Humanisierung von nager-antikörpern |
| US6297367B1 (en) | 1997-12-30 | 2001-10-02 | Chiron Corporation | Polynucleotide encoding TNFL1 |
| WO1999045959A1 (en) | 1998-03-13 | 1999-09-16 | Dana-Farber Cancer Institute, Inc. | Humanized antibody and uses thereof |
| US6737056B1 (en) | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| ATE482275T1 (de) | 1999-07-02 | 2010-10-15 | Morphosys Ag | Erzeugung spezifischer bindungspartner die an von genomischen dns-fragmenten oder ests kodierten (poly)peptiden binden |
| US6399857B1 (en) * | 1999-09-22 | 2002-06-04 | Paradigm Genetics, Inc. | Modified nucleotide sequence encoding a LexA DNA binding domain optimized for arabidopsis species |
| US20110131679A2 (en) * | 2000-04-19 | 2011-06-02 | Thomas La Rosa | Rice Nucleic Acid Molecules and Other Molecules Associated with Plants and Uses Thereof for Plant Improvement |
| US6571638B2 (en) | 2000-06-30 | 2003-06-03 | Sawtek, Inc. | Surface-acoustic-wave pressure sensor and associated methods |
| AU2001277857A1 (en) | 2000-07-07 | 2002-01-21 | Human Genome Sciences, Inc. | Tumor necrosis factor-gamma |
| US6824989B1 (en) | 2000-09-01 | 2004-11-30 | Upstate Biotechnology, Inc. | Recombinant monoclonal antibody to phosphotyrosine-containing proteins |
| CA2391711A1 (en) * | 2001-06-26 | 2002-12-26 | University Of Guelph | Non-radioactive assay of lipopolysaccharide kinases |
| SI2301965T1 (sl) * | 2002-10-16 | 2015-07-31 | Purdue Pharma L.P. | Protitelesa, ki vežejo celično- povezan CA 125 / O722P in metode uporabe le-teh |
| AU2003293096B9 (en) * | 2002-11-27 | 2011-09-29 | Biogen Ma Inc. | Humanized antibodies against monocyte chemotactic proteins |
| US20050101889A1 (en) | 2003-11-06 | 2005-05-12 | Freeman Gary A. | Using chest velocity to process physiological signals to remove chest compression artifacts |
| US20080287309A1 (en) * | 2004-07-10 | 2008-11-20 | Alexion Pharmaceuticals, Inc. | Methods for Discovering Antibodies Specific to Cancer Cells and Antibodies Discovered Thereby |
| TWI309240B (en) | 2004-09-17 | 2009-05-01 | Hoffmann La Roche | Anti-ox40l antibodies |
| US7531637B2 (en) | 2005-05-06 | 2009-05-12 | Zymogenetics, Inc. | IL-31 monoclonal antibodies |
| JP5339901B2 (ja) | 2005-05-10 | 2013-11-13 | バイオジェン・アイデック・エムエイ・インコーポレイテッド | 炎症傷害の処置および評価 |
| US20090317388A1 (en) * | 2005-05-25 | 2009-12-24 | Linda Burkly | Tl1a in treatment of disease |
| BRPI0611714A2 (pt) * | 2005-06-30 | 2009-01-13 | Abbott Lab | proteÍnas de ligaÇço a il-12/p40 |
| US7612181B2 (en) | 2005-08-19 | 2009-11-03 | Abbott Laboratories | Dual variable domain immunoglobulin and uses thereof |
| CN101253199B (zh) | 2005-08-30 | 2019-06-14 | 迈阿密大学 | 免疫调节肿瘤坏死因子受体25(tnfr25)的激动剂、拮抗剂和免疫毒素 |
| MX380352B (es) | 2006-06-12 | 2025-03-12 | Aptevo Res & Development Llc | Proteinas de union multivalentes monocatenarias con funcion efectora. |
| US7691980B2 (en) | 2007-01-09 | 2010-04-06 | Bio-Rad Laboratories, Inc. | Enhanced capacity and purification of antibodies by mixed mode chromatography in the presence of aqueous-soluble nonionic organic polymers |
| US20110217310A1 (en) | 2007-01-10 | 2011-09-08 | Siegel Richard M | Blockade of tl1a-dr3 interactions to ameliorate t cell mediated disease pathology |
| US20100190162A1 (en) * | 2007-02-26 | 2010-07-29 | Cedars-Sinai Medical Center | Methods of using single nucleotide polymorphisms in the tl1a gene to predict or diagnose inflammatory bowel disease |
| WO2008106579A2 (en) | 2007-02-28 | 2008-09-04 | Cedars-Sinai Medical Center | The role of il-12, il-23 and il-17 receptors in inflammatory bowel disease |
| US8263743B2 (en) | 2007-11-13 | 2012-09-11 | Teva Biopharmaceuticals Usa, Inc. | Humanized antibodies against TL1A |
| CN101469270B (zh) | 2007-12-27 | 2012-08-22 | 牛斌 | 工业连续化塑料裂解器 |
| WO2009092014A1 (en) | 2008-01-18 | 2009-07-23 | Gagnon Peter S | Enhanced purification of antibodies and antibody fragments by apatite chromatography |
| ES2493042T3 (es) | 2008-09-29 | 2014-09-11 | Roche Glycart Ag | Anticuerpos contra la IL-17 humana y usos de los mismos |
| RU2542394C2 (ru) | 2009-03-24 | 2015-02-20 | ТЕВА БИОФАРМАСЬЮТИКАЛЗ ЮЭсЭй, ИНК. | Гуманизированные антитела против light и их применение |
| KR102033276B1 (ko) | 2009-08-03 | 2019-10-16 | 유니버시티 오브 마이애미 | T 조절 세포의 생체 내 확장 방법 |
| WO2011106707A2 (en) | 2010-02-26 | 2011-09-01 | Human Genome Sciences, Inc. | Antibodies that specifically bind to dr3 |
| RU2013110874A (ru) | 2010-08-25 | 2014-09-27 | Ф.Хоффманн-Ля Рош Аг | Антитела против il-18r1 и их применения |
| JP6105472B2 (ja) | 2010-09-16 | 2017-03-29 | バリオファルム・アクチェンゲゼルシャフト | 抗ｈｕＴＮＦＲ１抗体 |
| US8766034B2 (en) * | 2010-09-22 | 2014-07-01 | Cedars-Sinai Medical Center | TL1A model of inflammation fibrosis and autoimmunity |
| JO3375B1 (ar) | 2010-11-08 | 2019-03-13 | Regeneron Pharma | أجسام مضادة بشرية للجين a1 الشبيه بعامل النخر الورمي (tl1a) |
| EP2709664A4 (en) | 2011-05-20 | 2015-06-10 | Us Government | BLOCKADE OF TL1A-DR3 INTERACTIONS FOR THE TREATMENT OF T-CELL-MEDIATED DISEASES AND ANTIBODIES THEREOF |
| LT2714735T (lt) | 2011-06-03 | 2021-12-10 | Xoma Technology Ltd. | Tgf beta specifiniai antikūnai |
| MX2014003689A (es) | 2011-09-30 | 2014-12-05 | Teva Pharmaceuticals Australia Pty Ltd | Anticuerpos contra tl1a y sus usos. |
| WO2014160463A1 (en) | 2013-03-13 | 2014-10-02 | The United States Of America, As Represented By The Secretary, Department Of Health & Human Services | Prefusion rsv f proteins and their use |
| JP6462599B2 (ja) * | 2013-03-15 | 2019-01-30 | シャアメン ユニバーシティ | Ｒｓｖ融合タンパク質のエピトープ及びそのエピトープを認識する抗体 |
| PT3702373T (pt) | 2013-09-13 | 2022-09-27 | Beigene Switzerland Gmbh | Anticorpos anti-pd1 e a sua utilização como agentes terapêuticos e de diagnóstico |
| SG11201602671WA (en) | 2013-11-13 | 2016-05-30 | Pfizer | Tumor necrosis factor-like ligand 1a specific antibodies and compositions and uses thereof |
| ES2936810T3 (es) | 2014-05-16 | 2023-03-22 | Pfizer | Anticuerpos biespecíficos con interfaces CH1-CL de ingeniería |
| US10160805B2 (en) | 2014-07-11 | 2018-12-25 | New York University | Methods of treating inflammatory bowel disease by administering tumor necrosis factor-like ligand 1A or an agonistic death-domain receptor 3 antibody |
| TWI757803B (zh) | 2014-11-14 | 2022-03-11 | 瑞士商赫孚孟拉羅股份公司 | 包含tnf家族配位三聚體之抗原結合分子 |
| TWI703158B (zh) | 2015-09-18 | 2020-09-01 | 美商希佛隆公司 | 特異性結合tl1a之抗體 |
| WO2017077715A1 (en) | 2015-11-02 | 2017-05-11 | La Jolla Institute For Allergy & Immunology | Method and medicament for treating airway and/or lung diseases |
| CR20180365A (es) | 2015-12-16 | 2018-09-28 | Amgen Inc | PROTEÍNAS DE UNIÓN AL ANTÍGENO BISPECÍFICO DE ANTI-TL1A/ANTI-TNF-a Y SUS USOS |
| CA3023678A1 (en) | 2016-05-09 | 2017-11-16 | Bristol-Myers Squibb Company | Tl1a antibodies and uses thereof |
| US10274751B2 (en) * | 2016-07-05 | 2019-04-30 | Bausch & Lomb Incorporated | Prism ballasted contact lens |
| ES2994244T3 (en) | 2016-07-25 | 2025-01-21 | Cephalon Llc | Affinity chromatography wash buffer |
| JP7194104B2 (ja) * | 2016-10-26 | 2022-12-21 | シーダーズ―シナイ メディカル センター | 抗ｔｌ１ａモノクローナル抗体の中和 |
| KR102763158B1 (ko) * | 2018-04-25 | 2025-02-04 | 프로메테우스 바이오사이언시즈, 인크. | 최적화된 항tl1a 항체 |
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- 2017-10-24 MY MYPI2019002368A patent/MY191324A/en unknown
- 2017-10-24 US US15/792,266 patent/US10322174B2/en active Active
- 2017-10-25 AR ARP170102965A patent/AR109882A1/es unknown
- 2017-10-26 TW TW106136987A patent/TWI832808B/zh active
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2019
- 2019-04-15 US US16/384,521 patent/US20190247498A1/en not_active Abandoned
- 2019-04-25 PH PH12019500946A patent/PH12019500946A1/en unknown
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2020
- 2020-11-23 US US17/102,189 patent/US20210093718A1/en not_active Abandoned
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2022
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2023
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2024
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20160053007A1 (en) * | 2007-01-10 | 2016-02-25 | The Usa, As Represented By The Secretary, Dept. Of Health And Human Services | Antibodies that bind to tl1a and methods of treating inflammatory or autoimmune disease comprising administering such antibodies |
| WO2014106602A1 (en) * | 2013-01-02 | 2014-07-10 | Glenmark Pharmaceuticals S.A. | Antibodies that bind to tl1a and their uses |
Also Published As
| Publication number | Publication date |
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| US20230381308A1 (en) | 2023-11-30 |
| US10322174B2 (en) | 2019-06-18 |
| TW201829461A (zh) | 2018-08-16 |
| US20210093718A1 (en) | 2021-04-01 |
| WO2018081074A1 (en) | 2018-05-03 |
| US20180110855A1 (en) | 2018-04-26 |
| PH12019500946A1 (en) | 2019-08-19 |
| EP3532489A4 (en) | 2020-07-08 |
| SG11201903737PA (en) | 2019-05-30 |
| MY191324A (en) | 2022-06-15 |
| CN110121509B (zh) | 2024-05-07 |
| CN110121509A (zh) | 2019-08-13 |
| KR20190082815A (ko) | 2019-07-10 |
| JP2023002562A (ja) | 2023-01-10 |
| JP2024161402A (ja) | 2024-11-19 |
| JP2020504076A (ja) | 2020-02-06 |
| US20190247498A1 (en) | 2019-08-15 |
| EP3532489A1 (en) | 2019-09-04 |
| KR20240128132A (ko) | 2024-08-23 |
| JP7194104B2 (ja) | 2022-12-21 |
| AR109882A1 (es) | 2019-01-30 |
| TW202432597A (zh) | 2024-08-16 |
| CN118240830A (zh) | 2024-06-25 |
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