JP2008520586A - 免疫グロブリン可変領域カセット交換 - Google Patents
免疫グロブリン可変領域カセット交換 Download PDFInfo
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Classifications
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- C—CHEMISTRY; METALLURGY
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- C07K16/46—Hybrid immunoglobulins
- C07K16/461—Igs containing Ig-regions, -domains or -residues form different species
- C07K16/464—Igs containing CDR-residues from one specie grafted between FR-residues from another
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/1072—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides by covalent attachment of residues or functional groups
- C07K1/1075—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides by covalent attachment of residues or functional groups by covalent attachment of amino acids or peptide residues
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/005—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies constructed by phage libraries
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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
- C07K2317/21—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
- C07K2317/20—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
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/565—Complementarity determining region [CDR]
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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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| JP2008520586A true JP2008520586A (ja) | 2008-06-19 |
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Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2013513620A (ja) * | 2009-12-11 | 2013-04-22 | アイアールエム・リミテッド・ライアビリティ・カンパニー | Ｐｃｓｋ９アンタゴニスト |
| JP2013514794A (ja) * | 2009-12-22 | 2013-05-02 | エフ．ホフマン−ラ ロシュ アーゲー | 配列依存性の凝集 |
| JP2017073995A (ja) * | 2015-10-13 | 2017-04-20 | 株式会社バイオピーク | ターゲットを認識するタンパク質の発現スクリーニング法 |
Families Citing this family (59)
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|---|---|---|---|---|
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| JP2010520748A (ja) | 2007-02-20 | 2010-06-17 | アナプティスバイオ インコーポレイティッド | 体細胞超変異系 |
| PT3199180T (pt) * | 2007-03-08 | 2022-04-01 | Univ Monash | Anticorpos epha3 para o tratamento de tumores sólidos |
| AU2008251943B2 (en) * | 2007-03-14 | 2013-09-05 | Alexion Pharmaceuticals, Inc. | Humaneered anti-factor B antibody |
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| JO3076B1 (ar) | 2007-10-17 | 2017-03-15 | Janssen Alzheimer Immunotherap | نظم العلاج المناعي المعتمد على حالة apoe |
| EA201000903A1 (ru) | 2007-11-30 | 2011-02-28 | Калобиос Фармасьютикалс, Инк. | Антитела к pcrv-антигену pseudomonas aeruginosa |
| US9873957B2 (en) | 2008-03-13 | 2018-01-23 | Dyax Corp. | Libraries of genetic packages comprising novel HC CDR3 designs |
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| EA201001691A1 (ru) | 2008-04-28 | 2011-10-31 | Калобайос Фармасьютикалз, Инк. | Антитела к гранулоцитарно-макрофагальному колониестимулирующему фактору |
| CA2751433A1 (en) | 2009-02-04 | 2010-08-12 | Kalobios Pharmaceuticals, Inc. | Combination antibiotic and antibody therapy for the treatment of pseudomonas aeruginosa infection |
| US9079942B2 (en) | 2009-02-09 | 2015-07-14 | Epitomics, Inc. | CDR-anchored amplification method |
| WO2010093814A1 (en) | 2009-02-11 | 2010-08-19 | Kalobios Pharmaceuticals, Inc. | Methods of treating dementia using a gm-csf antagonist |
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| CN102459591B (zh) * | 2009-05-20 | 2015-05-13 | 诺维莫尼公司 | 合成性的多肽文库以及用于建立具有天然多样性的多肽变体的方法 |
| AU2010266127B2 (en) | 2009-07-02 | 2015-11-05 | Musc Foundation For Research Development | Methods of stimulating liver regeneration |
| US8293483B2 (en) | 2009-09-11 | 2012-10-23 | Epitomics, Inc. | Method for identifying lineage-related antibodies |
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| EP2673302A1 (en) | 2011-02-11 | 2013-12-18 | Irm Llc | Pcsk9 antagonists |
| ES2926988T3 (es) | 2011-03-15 | 2022-10-31 | X Body Inc | Métodos de cribado de anticuerpos |
| WO2012170607A2 (en) | 2011-06-10 | 2012-12-13 | Novartis Ag | Use of pcsk9 antagonists |
| WO2012168491A1 (en) | 2011-06-10 | 2012-12-13 | Novartis Ag | Pharmaceutical formulations of pcsk9 antagonists |
| US20130109586A1 (en) * | 2011-10-05 | 2013-05-02 | Kalobios Pharmaceuticals, Inc. | Generation of antibodies to an epitope of interest that contains a phosphomimetic amino acid |
| US9790280B2 (en) | 2011-10-26 | 2017-10-17 | Elanco Tiergesundheit Ag | Monoclonal canine CD20 antibodies and methods of use |
| US9803005B2 (en) | 2012-05-24 | 2017-10-31 | Alexion Pharmaceuticals, Inc. | Humaneered anti-factor B antibody |
| WO2014084859A1 (en) | 2012-11-30 | 2014-06-05 | Novartis Ag | Molecules and methods for modulating tmem16a activities |
| AR096601A1 (es) | 2013-06-21 | 2016-01-20 | Novartis Ag | Anticuerpos del receptor 1 de ldl oxidado similar a lectina y métodos de uso |
| SMT201900714T1 (it) | 2013-12-09 | 2020-01-14 | Allakos Inc | Anticorpi anti-siglec-8 e loro metodi d'impiego |
| EP4014995A1 (en) | 2014-02-28 | 2022-06-22 | Allakos Inc. | Methods and compositions for treating siglec-8 associated diseases |
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| MA41044A (fr) | 2014-10-08 | 2017-08-15 | Novartis Ag | Compositions et procédés d'utilisation pour une réponse immunitaire accrue et traitement contre le cancer |
| US10774145B2 (en) | 2015-06-17 | 2020-09-15 | Allakos Inc. | Methods and compositions for treating fibrotic diseases |
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| EA201992626A1 (ru) | 2017-05-05 | 2020-04-24 | Аллакос Инк. | Способы и композиции для лечения аллергических заболеваний глаз |
| IL322309A (en) | 2017-05-24 | 2025-09-01 | Novartis Ag | IL2 antibody grafted proteins and methods of use in cancer treatment |
| JOP20190271A1 (ar) | 2017-05-24 | 2019-11-21 | Novartis Ag | بروتينات مطعّمة بسيتوكين- الجسم المضاد وطرق الاستخدام للاضطرابات المتعلقة بالمناعة |
| US20200362058A1 (en) | 2017-05-24 | 2020-11-19 | Novartis Ag | Antibody-cytokine engrafted proteins and methods of use |
| WO2018215937A1 (en) | 2017-05-24 | 2018-11-29 | Novartis Ag | Interleukin-7 antibody cytokine engrafted proteins and methods of use in the treatment of cancer |
| US10870703B2 (en) | 2017-10-02 | 2020-12-22 | Humanigen, Inc. | Methods of treating immunotherapy-related toxicity using a GM-CSF antagonist |
| US11130805B2 (en) | 2017-10-02 | 2021-09-28 | Humanigen, Inc. | Methods of treating CART-T cell therapy-induced neuroinflammation using a GM-CSF antagonist |
| US10927168B2 (en) | 2017-10-02 | 2021-02-23 | Humanicen, Inc. | Method of reducing tumor relapse rate in immunotherapy by administration of lenzilumab |
| US10899831B2 (en) | 2017-10-02 | 2021-01-26 | Humanigen, Inc. | Method of reducing the level of non-GM-CSF cytokines/chemokines in immunotherapy-related toxicity |
| BR112021012631A2 (pt) | 2018-12-26 | 2021-12-14 | Xilio Dev Inc | Anticorpos anti-ctla4 e métodos de uso dos mesmos |
| CN116917325A (zh) | 2021-03-01 | 2023-10-20 | 西里欧发展公司 | 用于治疗癌症的被掩蔽的ctla4和pd1/pdl1抗体的组合 |
| EP4301467A1 (en) | 2021-03-01 | 2024-01-10 | Xilio Development, Inc. | Combination of ctla4 and pd1/pdl1 antibodies for treating cancer |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2003099999A2 (en) * | 2002-05-20 | 2003-12-04 | Abmaxis, Inc. | Generation and selection of protein library in silico |
Family Cites Families (32)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3742105A (en) | 1970-05-05 | 1973-06-26 | S Kuroda | Method for producing a seamless tubing |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US5225539A (en) * | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| US6548640B1 (en) * | 1986-03-27 | 2003-04-15 | Btg International Limited | Altered antibodies |
| US5132405A (en) | 1987-05-21 | 1992-07-21 | Creative Biomolecules, Inc. | Biosynthetic antibody binding sites |
| US5091513A (en) | 1987-05-21 | 1992-02-25 | Creative Biomolecules, Inc. | Biosynthetic antibody binding sites |
| JPS6412935A (en) | 1987-07-02 | 1989-01-17 | Mitsubishi Electric Corp | Constant-speed travel device for vehicle |
| 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 |
| US6969586B1 (en) * | 1989-05-16 | 2005-11-29 | Scripps Research Institute | Method for tapping the immunological repertoire |
| US5859205A (en) * | 1989-12-21 | 1999-01-12 | Celltech Limited | Humanised antibodies |
| DK0531472T3 (da) | 1991-03-06 | 2003-12-01 | Merck Patent Gmbh | Humaniserede monoklonale antistoffer |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| US5714350A (en) * | 1992-03-09 | 1998-02-03 | Protein Design Labs, Inc. | Increasing antibody affinity by altering glycosylation in the immunoglobulin variable region |
| US5733743A (en) | 1992-03-24 | 1998-03-31 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| EP0672142B1 (en) * | 1992-12-04 | 2001-02-28 | Medical Research Council | Multivalent and multispecific binding proteins, their manufacture and use |
| US6309636B1 (en) * | 1995-09-14 | 2001-10-30 | Cancer Research Institute Of Contra Costa | Recombinant peptides derived from the Mc3 anti-BA46 antibody, methods of use thereof, and methods of humanizing antibody peptides |
| CA2229043C (en) * | 1995-08-18 | 2016-06-07 | Morphosys Gesellschaft Fur Proteinoptimierung Mbh | Protein/(poly)peptide libraries |
| JP4460155B2 (ja) * | 1997-12-05 | 2010-05-12 | ザ・スクリプス・リサーチ・インステイチユート | マウス抗体のヒト化 |
| ATE321870T1 (de) | 2000-06-05 | 2006-04-15 | Corixa Corp | Leader-anteile zur erhöhung der sekretion von rekombinanten proteine aus einer wirtzelle |
| AU2001268545A1 (en) | 2000-06-21 | 2002-01-08 | Alexion Pharmaceuticals, Inc. | Libraries displaying human antibody fragments with hybrid complementarity determining regions |
| WO2004006955A1 (en) * | 2001-07-12 | 2004-01-22 | Jefferson Foote | Super humanized antibodies |
| JP4213586B2 (ja) | 2001-09-13 | 2009-01-21 | 株式会社抗体研究所 | ラクダ抗体ライブラリーの作製方法 |
| US20030219839A1 (en) * | 2001-09-20 | 2003-11-27 | Katherine Bowdish | Anti-PDGF antibodies and methods for producing engineered antibodies |
| AR038568A1 (es) * | 2002-02-20 | 2005-01-19 | Hoffmann La Roche | Anticuerpos anti-a beta y su uso |
| US7538195B2 (en) * | 2002-06-14 | 2009-05-26 | Immunogen Inc. | Anti-IGF-I receptor antibody |
| US7541440B2 (en) * | 2002-09-30 | 2009-06-02 | Immunomedics, Inc. | Chimeric, human and humanized anti-granulocyte antibodies and methods of use |
| WO2004072266A2 (en) * | 2003-02-13 | 2004-08-26 | Kalobios Inc. | Antibody affinity engineering by serial epitope-guided complementarity replacement |
| EP1761561B1 (en) * | 2004-01-20 | 2015-08-26 | KaloBios Pharmaceuticals, Inc. | Antibody specificity transfer using minimal essential binding determinants |
| WO2006055178A2 (en) | 2004-10-25 | 2006-05-26 | Merck & Co., Inc. | Anti-addl antibodies and uses thereof |
| AU2005306502B2 (en) | 2004-11-16 | 2012-11-15 | Humanigen, Inc. | Immunoglobulin variable region cassette exchange |
| US20090175847A1 (en) * | 2007-05-30 | 2009-07-09 | Abbott Laboratories | Humanized antibodies to ab (20-42) globulomer and uses thereof |
-
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- 2005-11-16 ES ES19169135T patent/ES2881353T3/es not_active Expired - Lifetime
- 2005-11-16 PT PT191691351T patent/PT3540062T/pt unknown
- 2005-11-16 ES ES05851809T patent/ES2429541T3/es not_active Expired - Lifetime
- 2005-11-16 DK DK19169135.1T patent/DK3540062T3/da active
- 2005-11-16 EP EP19169135.1A patent/EP3540062B1/en not_active Expired - Lifetime
- 2005-11-16 PT PT10014128T patent/PT2343380T/pt unknown
- 2005-11-16 DK DK10014128.2T patent/DK2343380T3/da active
- 2005-11-16 CA CA2587158A patent/CA2587158C/en not_active Expired - Lifetime
- 2005-11-16 ES ES10014128T patent/ES2744149T3/es not_active Expired - Lifetime
- 2005-11-16 EP EP05851809.3A patent/EP1824987B1/en not_active Revoked
-
2015
- 2015-12-14 US US14/968,709 patent/US10919983B2/en active Active
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2003099999A2 (en) * | 2002-05-20 | 2003-12-04 | Abmaxis, Inc. | Generation and selection of protein library in silico |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2013513620A (ja) * | 2009-12-11 | 2013-04-22 | アイアールエム・リミテッド・ライアビリティ・カンパニー | Ｐｃｓｋ９アンタゴニスト |
| JP2016179979A (ja) * | 2009-12-11 | 2016-10-13 | ノバルティス アーゲー | Ｐｃｓｋ９アンタゴニスト |
| JP2013514794A (ja) * | 2009-12-22 | 2013-05-02 | エフ．ホフマン−ラ ロシュ アーゲー | 配列依存性の凝集 |
| JP2017073995A (ja) * | 2015-10-13 | 2017-04-20 | 株式会社バイオピーク | ターゲットを認識するタンパク質の発現スクリーニング法 |
Also Published As
| Publication number | Publication date |
|---|---|
| EP3540062B1 (en) | 2021-05-12 |
| DK2343380T3 (da) | 2019-09-09 |
| EP2343380B1 (en) | 2019-06-12 |
| PL3540062T3 (pl) | 2021-12-27 |
| US10919983B2 (en) | 2021-02-16 |
| AU2005306502A1 (en) | 2006-05-26 |
| AU2005306502B2 (en) | 2012-11-15 |
| EP2343380A1 (en) | 2011-07-13 |
| EP3540062A1 (en) | 2019-09-18 |
| US20160102152A1 (en) | 2016-04-14 |
| ES2744149T3 (es) | 2020-02-21 |
| ES2881353T3 (es) | 2021-11-29 |
| PT3540062T (pt) | 2021-07-06 |
| US20060134098A1 (en) | 2006-06-22 |
| PT2343380T (pt) | 2019-09-18 |
| WO2006055778A3 (en) | 2006-11-23 |
| EP1824987A4 (en) | 2008-03-19 |
| PL2343380T3 (pl) | 2020-03-31 |
| ES2429541T3 (es) | 2013-11-15 |
| EP1824987A2 (en) | 2007-08-29 |
| CA2587158A1 (en) | 2006-05-26 |
| WO2006055778A2 (en) | 2006-05-26 |
| DK3540062T3 (da) | 2021-06-28 |
| EP1824987B1 (en) | 2013-08-21 |
| CA2587158C (en) | 2016-01-12 |
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