ZA200005506B - FAP α-Specific antibody with improved producibility. - Google Patents
FAP α-Specific antibody with improved producibility. Download PDFInfo
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- ZA200005506B ZA200005506B ZA200005506A ZA200005506A ZA200005506B ZA 200005506 B ZA200005506 B ZA 200005506B ZA 200005506 A ZA200005506 A ZA 200005506A ZA 200005506 A ZA200005506 A ZA 200005506A ZA 200005506 B ZA200005506 B ZA 200005506B
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- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/40—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against enzymes
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- 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
-
- 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
- C07K2317/567—Framework region [FR]
-
- 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
- C07K2317/732—Antibody-dependent cellular cytotoxicity [ADCC]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- 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
- C12N2799/00—Uses of viruses
- C12N2799/02—Uses of viruses as vector
- C12N2799/021—Uses of viruses as vector for the expression of a heterologous nucleic acid
- C12N2799/026—Uses of viruses as vector for the expression of a heterologous nucleic acid where the vector is derived from a baculovirus
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Immunology (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Medicinal Preparation (AREA)
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
EP98107925A EP0953639A1 (de) | 1998-04-30 | 1998-04-30 | FAPalpha-spezifischer Antikörper mit verbesserter Produzierbarkeit |
Publications (1)
Publication Number | Publication Date |
---|---|
ZA200005506B true ZA200005506B (en) | 2002-05-14 |
Family
ID=8231860
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
ZA200005506A ZA200005506B (en) | 1998-04-30 | 2000-10-09 | FAP α-Specific antibody with improved producibility. |
Country Status (27)
Country | Link |
---|---|
EP (2) | EP0953639A1 (de) |
JP (1) | JP4421779B2 (de) |
KR (1) | KR100580936B1 (de) |
CN (1) | CN1303430A (de) |
AR (1) | AR016243A1 (de) |
AT (1) | ATE356873T1 (de) |
AU (1) | AU760305B2 (de) |
BG (1) | BG65034B1 (de) |
BR (1) | BR9910577A (de) |
CA (1) | CA2327586C (de) |
CO (1) | CO5050255A1 (de) |
DE (1) | DE69935516T2 (de) |
EA (1) | EA005401B1 (de) |
EE (1) | EE200000642A (de) |
ES (1) | ES2283114T3 (de) |
HU (1) | HUP0101501A3 (de) |
ID (1) | ID26555A (de) |
IL (1) | IL138701A0 (de) |
NO (1) | NO20005412L (de) |
NZ (1) | NZ508456A (de) |
PL (1) | PL358087A1 (de) |
SK (1) | SK16192000A3 (de) |
TR (1) | TR200003181T2 (de) |
UA (1) | UA73276C2 (de) |
WO (1) | WO1999057151A2 (de) |
YU (1) | YU66300A (de) |
ZA (1) | ZA200005506B (de) |
Families Citing this family (77)
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---|---|---|---|---|
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US8530627B2 (en) | 2002-08-14 | 2013-09-10 | Macrogenics, Inc. | FcγRIIB specific antibodies and methods of use thereof |
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US8968730B2 (en) | 2002-08-14 | 2015-03-03 | Macrogenics Inc. | FcγRIIB specific antibodies and methods of use thereof |
US8946387B2 (en) | 2002-08-14 | 2015-02-03 | Macrogenics, Inc. | FcγRIIB specific antibodies and methods of use thereof |
US8193318B2 (en) | 2002-08-14 | 2012-06-05 | Macrogenics, Inc. | FcγRIIB specific antibodies and methods of use thereof |
US8187593B2 (en) | 2002-08-14 | 2012-05-29 | Macrogenics, Inc. | FcγRIIB specific antibodies and methods of use thereof |
US7384744B2 (en) | 2002-11-29 | 2008-06-10 | Boehringer Ingelheim Pharma Gmbh & Co., Kg | Expression vector, methods for the production of heterologous gene products and for the selection of recombinant cells producing high levels of such products |
US7960512B2 (en) | 2003-01-09 | 2011-06-14 | Macrogenics, Inc. | Identification and engineering of antibodies with variant Fc regions and methods of using same |
EP2368578A1 (de) | 2003-01-09 | 2011-09-28 | Macrogenics, Inc. | Identifizierung und Herstellung von Antikörpern mit abweichenden FC-Regionen und Anwendungsverfahren dafür |
CN1774500B (zh) * | 2003-02-14 | 2011-03-02 | 比奥根艾迪克Ma公司 | 用于瞬时或稳定表达外源分子的表达盒和载体 |
KR101297146B1 (ko) | 2004-05-10 | 2013-08-21 | 마크로제닉스, 인크. | 인간화 FcγRIIB 특이적 항체 및 그의 사용 방법 |
EP1810035A4 (de) | 2004-11-10 | 2010-03-17 | Macrogenics Inc | Erzeugung von fc-antikörperregionen für effektorfunktion |
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CN101848936B (zh) * | 2007-08-20 | 2017-05-03 | 葛兰素集团有限公司 | 生产方法 |
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WO2021005131A1 (en) | 2019-07-08 | 2021-01-14 | 3B Pharmaceuticals Gmbh | Compounds comprising a fibroblast activation protein ligand and use thereof |
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EP4026846A4 (de) * | 2019-09-03 | 2023-09-13 | Bio-Thera Solutions, Ltd. | Anti-tigit-immunosuppressivum und anwendung davon |
CN113512116B (zh) * | 2020-04-10 | 2022-09-20 | 苏州普乐康医药科技有限公司 | 一种抗igf-1r抗体及其应用 |
KR102363980B1 (ko) * | 2020-04-13 | 2022-02-15 | 전남대학교산학협력단 | 전이성 뇌종양의 진단 또는 예후 분석용 바이오마커 및 이를 이용한 진단방법 |
JP2023523977A (ja) * | 2020-04-30 | 2023-06-08 | アイ-マブ バイオファーマ ユーエス リミテッド | 抗cd47抗体を含む医薬組成物 |
CA3180665A1 (en) | 2020-05-19 | 2021-11-25 | Boehringer Ingelheim International Gmbh | Binding molecules for the treatment of cancer |
WO2022007283A1 (zh) * | 2020-07-08 | 2022-01-13 | 深圳霁因生物医药转化研究院 | 用于诊断fap表达异常相关疾病的试剂盒、方法及计算机可读存储介质 |
MX2023007869A (es) | 2021-01-07 | 2023-09-22 | 3B Pharmaceuticals Gmbh | Compuestos que comprenden un ligando de proteina de activacion de fibroblasto y uso del mismo. |
EP4050018A1 (de) | 2021-01-07 | 2022-08-31 | 3B Pharmaceuticals GmbH | Verbindungen mit fibroblasten-aktivierendem proteinligand und deren verwendung |
WO2023031644A1 (en) | 2021-08-31 | 2023-03-09 | Full-Life Technologies Limited | Anti-fibroblast activation protein (fap) single domain antibodies and uses thereof |
WO2023125796A1 (en) * | 2021-12-30 | 2023-07-06 | Concept To Medicine Biotech Co., Ltd. | Human antibodies against fap-alpha |
WO2024027771A1 (zh) * | 2022-08-03 | 2024-02-08 | 南京维立志博生物科技有限公司 | 靶向FAP和TGFβ的抗体融合蛋白及其用途 |
WO2024074727A1 (en) | 2022-10-07 | 2024-04-11 | Genethon | Immunotherapy of skeletal myopathies using anti-fap car-t cells |
CN116589566A (zh) * | 2022-11-18 | 2023-08-15 | 昆明医科大学第一附属医院 | 一种HIV-1中和抗体的改造重组单克隆IgM抗体及其应用 |
Family Cites Families (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5059523A (en) * | 1988-05-02 | 1991-10-22 | Sloan-Kettering Institute For Cancer Research | Cell-surface glycoproteins of human sarcomas |
US5530101A (en) * | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
WO1993005804A1 (en) * | 1991-09-18 | 1993-04-01 | Sloan-Kettering Institute For Cancer Research | Activated stromal fibroblast-specific antibody, f19 and methods of using the same |
ZA936260B (en) * | 1992-09-09 | 1994-03-18 | Smithkline Beecham Corp | Novel antibodies for conferring passive immunity against infection by a pathogen in man |
JP4436457B2 (ja) * | 1995-08-18 | 2010-03-24 | モルフォシス アイピー ゲーエムベーハー | 蛋白質/(ポリ)ペプチドライブラリー |
AU716257B2 (en) * | 1996-05-01 | 2000-02-24 | Genitope Corporation | Vaccines for treatment of lymphoma and leukemia |
-
1998
- 1998-04-30 EP EP98107925A patent/EP0953639A1/de not_active Withdrawn
-
1999
- 1999-04-22 EE EEP200000642A patent/EE200000642A/xx unknown
- 1999-04-22 EP EP99923439A patent/EP1098979B1/de not_active Expired - Lifetime
- 1999-04-22 BR BR9910577-2A patent/BR9910577A/pt not_active IP Right Cessation
- 1999-04-22 HU HU0101501A patent/HUP0101501A3/hu unknown
- 1999-04-22 AU AU40322/99A patent/AU760305B2/en not_active Ceased
- 1999-04-22 WO PCT/EP1999/002711 patent/WO1999057151A2/en not_active Application Discontinuation
- 1999-04-22 PL PL99358087A patent/PL358087A1/xx not_active IP Right Cessation
- 1999-04-22 ID IDW20002198A patent/ID26555A/id unknown
- 1999-04-22 TR TR2000/03181T patent/TR200003181T2/xx unknown
- 1999-04-22 DE DE69935516T patent/DE69935516T2/de not_active Expired - Lifetime
- 1999-04-22 EA EA200001023A patent/EA005401B1/ru not_active IP Right Cessation
- 1999-04-22 CA CA2327586A patent/CA2327586C/en not_active Expired - Lifetime
- 1999-04-22 KR KR1020007011585A patent/KR100580936B1/ko not_active IP Right Cessation
- 1999-04-22 JP JP2000547119A patent/JP4421779B2/ja not_active Expired - Lifetime
- 1999-04-22 CN CN99806582A patent/CN1303430A/zh active Pending
- 1999-04-22 NZ NZ508456A patent/NZ508456A/xx unknown
- 1999-04-22 YU YU66300A patent/YU66300A/sh unknown
- 1999-04-22 ES ES99923439T patent/ES2283114T3/es not_active Expired - Lifetime
- 1999-04-22 UA UA2000116786A patent/UA73276C2/uk unknown
- 1999-04-22 SK SK1619-2000A patent/SK16192000A3/sk unknown
- 1999-04-22 AT AT99923439T patent/ATE356873T1/de active
- 1999-04-22 IL IL13870199A patent/IL138701A0/xx unknown
- 1999-04-29 CO CO99025997A patent/CO5050255A1/es unknown
- 1999-04-30 AR ARP990102015A patent/AR016243A1/es unknown
-
2000
- 2000-10-05 BG BG104828A patent/BG65034B1/bg unknown
- 2000-10-09 ZA ZA200005506A patent/ZA200005506B/en unknown
- 2000-10-27 NO NO20005412A patent/NO20005412L/no not_active Application Discontinuation
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