MX2014008157A - Anticuerpos anti-lrp5 y metodos de uso. - Google Patents
Anticuerpos anti-lrp5 y metodos de uso.Info
- Publication number
- MX2014008157A MX2014008157A MX2014008157A MX2014008157A MX2014008157A MX 2014008157 A MX2014008157 A MX 2014008157A MX 2014008157 A MX2014008157 A MX 2014008157A MX 2014008157 A MX2014008157 A MX 2014008157A MX 2014008157 A MX2014008157 A MX 2014008157A
- Authority
- MX
- Mexico
- Prior art keywords
- antibody
- seq
- amino acid
- norrin
- hvr
- Prior art date
Links
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Classifications
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- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
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- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/68—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment
- A61K47/6835—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment the modifying agent being an antibody or an immunoglobulin bearing at least one antigen-binding site
- A61K47/6849—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment the modifying agent being an antibody or an immunoglobulin bearing at least one antigen-binding site the antibody targeting a receptor, a cell surface antigen or a cell surface determinant
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- C07—ORGANIC CHEMISTRY
- C07H—SUGARS; DERIVATIVES THEREOF; NUCLEOSIDES; NUCLEOTIDES; NUCLEIC ACIDS
- C07H21/00—Compounds containing two or more mononucleotide units having separate phosphate or polyphosphate groups linked by saccharide radicals of nucleoside groups, e.g. nucleic acids
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- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
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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
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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
- C07K2317/24—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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- 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
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- C07K2317/567—Framework region [FR]
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- 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
- C07K2317/75—Agonist effect on antigen
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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)
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- Bioinformatics & Cheminformatics (AREA)
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- Chemical Kinetics & Catalysis (AREA)
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- Biophysics (AREA)
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- Ophthalmology & Optometry (AREA)
- Vascular Medicine (AREA)
- Urology & Nephrology (AREA)
- Heart & Thoracic Surgery (AREA)
- Cardiology (AREA)
- Cell Biology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201261588100P | 2012-01-18 | 2012-01-18 | |
| PCT/US2013/022045 WO2013109819A1 (en) | 2012-01-18 | 2013-01-18 | Anti-lrp5 antibodies and methods of use |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| MX2014008157A true MX2014008157A (es) | 2014-10-06 |
Family
ID=47604271
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| MX2014008157A MX2014008157A (es) | 2012-01-18 | 2013-01-18 | Anticuerpos anti-lrp5 y metodos de uso. |
Country Status (24)
| Country | Link |
|---|---|
| US (4) | US9200072B2 (enExample) |
| EP (1) | EP2804629A1 (enExample) |
| JP (1) | JP6242813B2 (enExample) |
| KR (1) | KR20140116490A (enExample) |
| CN (1) | CN104066449B (enExample) |
| AR (1) | AR089752A1 (enExample) |
| AU (1) | AU2013209707A1 (enExample) |
| BR (1) | BR112014017518A2 (enExample) |
| CA (1) | CA2862422A1 (enExample) |
| CL (1) | CL2014001888A1 (enExample) |
| CO (1) | CO7000747A2 (enExample) |
| CR (1) | CR20140382A (enExample) |
| EA (1) | EA028202B1 (enExample) |
| IL (1) | IL233317A0 (enExample) |
| IN (1) | IN2014DN05885A (enExample) |
| MA (1) | MA35898B1 (enExample) |
| MX (1) | MX2014008157A (enExample) |
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Families Citing this family (20)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP5859307B2 (ja) * | 2008-09-10 | 2016-02-10 | ジェネンテック， インコーポレイテッド | 眼の血管新生を阻害する方法 |
| JP5861469B2 (ja) * | 2012-01-23 | 2016-02-16 | 日本電気硝子株式会社 | ガラス管の清浄切断装置と清浄切断方法 |
| WO2016007775A1 (en) | 2014-07-11 | 2016-01-14 | Genentech, Inc. | Notch pathway inhibition |
| EP4219564A1 (en) | 2014-09-12 | 2023-08-02 | The Board of Trustees of the Leland Stanford Junior University | Wnt signaling agonist molecules |
| JP6933379B2 (ja) * | 2015-09-24 | 2021-09-08 | ザ ユニバーシティ オブ ノース カロライナ アット チャペル ヒル | 転移を低減するための方法および組成物 |
| CN106367517A (zh) * | 2016-09-28 | 2017-02-01 | 湖北工业大学 | 一种低密度脂蛋白受体相关蛋白5基因突变检测的试剂及应用 |
| JP2020518675A (ja) * | 2017-05-05 | 2020-06-25 | レチナール ソリューションズ エルエルシー | ノリン誘発性の遺伝子発現および疾患を処置するためのその使用 |
| AR111840A1 (es) | 2017-05-31 | 2019-08-21 | Boehringer Ingelheim Int | Polipéptidos que antagonizan la señalización wnt en células tumorales |
| CN111699003B (zh) | 2017-12-19 | 2024-05-03 | 瑟罗泽恩奥普瑞汀公司 | 抗lrp5/6抗体和使用方法 |
| JP7418332B2 (ja) | 2017-12-19 | 2024-01-19 | スロゼン オペレーティング， インコーポレイテッド | 抗フリズルド抗体及び使用方法 |
| CN111727203B (zh) | 2017-12-19 | 2024-04-26 | 瑟罗泽恩奥普瑞汀公司 | Wnt替代分子和其用途 |
| CN111511400B (zh) * | 2017-12-29 | 2025-08-29 | 豪夫迈·罗氏有限公司 | 抗vegf抗体及其使用方法 |
| CA3147827A1 (en) * | 2019-08-14 | 2021-02-18 | Modmab Therapeutics Inc. | Antibodies that bind to lrp5 proteins and methods of use |
| WO2021225954A1 (en) * | 2020-05-04 | 2021-11-11 | The Regents Of The University Of California | Inhibiting anti-enpp1 antibodies |
| CN111909935B (zh) * | 2020-07-17 | 2022-11-15 | 武汉纽福斯生物科技有限公司 | 重组人卷曲蛋白受体4(fzd4)的表达载体及其应用 |
| KR102536092B1 (ko) * | 2020-09-29 | 2023-05-24 | 조선대학교산학협력단 | Lrp5 발현 또는 활성 억제제를 포함하는 허혈성 심장질환의 예방 또는 치료용 약학적 조성물 |
| WO2023250402A2 (en) * | 2022-06-22 | 2023-12-28 | Antlera Therapeutics Inc. | Tetravalent fzd and wnt co-receptor binding antibody molecules and uses thereof |
| EP4263618A4 (en) | 2020-12-18 | 2024-11-20 | Antlera Therapeutics Inc. | TETRAVALENT WNT AND FZD CO-RECEPTOR BINDING ANTIBODY MOLECULES AND THEIR USES |
| WO2025149667A1 (en) | 2024-01-12 | 2025-07-17 | Pheon Therapeutics Ltd | Antibody drug conjugates and uses thereof |
| CN118599000A (zh) * | 2024-05-11 | 2024-09-06 | 中山大学附属第三医院 | Lrp5作为靶向分子在治疗糖尿病肾病中的应用 |
Family Cites Families (95)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4737456A (en) | 1985-05-09 | 1988-04-12 | Syntex (U.S.A.) Inc. | Reducing interference in ligand-receptor binding assays |
| US4676980A (en) | 1985-09-23 | 1987-06-30 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Target specific cross-linked heteroantibodies |
| US6548640B1 (en) | 1986-03-27 | 2003-04-15 | Btg International Limited | Altered antibodies |
| IL85035A0 (en) | 1987-01-08 | 1988-06-30 | Int Genetic Eng | Polynucleotide molecule,a chimeric antibody with specificity for human b cell surface antigen,a process for the preparation and methods utilizing the same |
| AU600575B2 (en) | 1987-03-18 | 1990-08-16 | Sb2, Inc. | Altered antibodies |
| US5606040A (en) | 1987-10-30 | 1997-02-25 | American Cyanamid Company | Antitumor and antibacterial substituted disulfide derivatives prepared from compounds possessing a methyl-trithio group |
| US5770701A (en) | 1987-10-30 | 1998-06-23 | American Cyanamid Company | Process for preparing targeted forms of methyltrithio antitumor agents |
| JP2919890B2 (ja) | 1988-11-11 | 1999-07-19 | メディカル リサーチ カウンスル | 単一ドメインリガンド、そのリガンドからなる受容体、その製造方法、ならびにそのリガンドおよび受容体の使用 |
| DE3920358A1 (de) | 1989-06-22 | 1991-01-17 | Behringwerke Ag | Bispezifische und oligospezifische, mono- und oligovalente antikoerperkonstrukte, ihre herstellung und verwendung |
| CA2026147C (en) | 1989-10-25 | 2006-02-07 | Ravi J. Chari | Cytotoxic agents comprising maytansinoids and their therapeutic use |
| US5208020A (en) | 1989-10-25 | 1993-05-04 | Immunogen Inc. | Cytotoxic agents comprising maytansinoids and their therapeutic use |
| US5959177A (en) | 1989-10-27 | 1999-09-28 | The Scripps Research Institute | Transgenic plants expressing assembled secretory antibodies |
| US6075181A (en) | 1990-01-12 | 2000-06-13 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US6150584A (en) | 1990-01-12 | 2000-11-21 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US5770429A (en) | 1990-08-29 | 1998-06-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| DK0564531T3 (da) | 1990-12-03 | 1998-09-28 | Genentech Inc | Berigelsesfremgangsmåde for variantproteiner med ændrede bindingsegenskaber |
| US5571894A (en) | 1991-02-05 | 1996-11-05 | Ciba-Geigy Corporation | Recombinant antibodies specific for a growth factor receptor |
| CA2103059C (en) | 1991-06-14 | 2005-03-22 | Paul J. Carter | Method for making humanized antibodies |
| GB9114948D0 (en) | 1991-07-11 | 1991-08-28 | Pfizer Ltd | Process for preparing sertraline intermediates |
| WO1993006217A1 (en) | 1991-09-19 | 1993-04-01 | Genentech, Inc. | EXPRESSION IN E. COLI OF ANTIBODY FRAGMENTS HAVING AT LEAST A CYSTEINE PRESENT AS A FREE THIOL, USE FOR THE PRODUCTION OF BIFUNCTIONAL F(ab')2 ANTIBODIES |
| FI941572L (fi) | 1991-10-07 | 1994-05-27 | Oncologix Inc | Anti-erbB-2-monoklonaalisten vasta-aineiden yhdistelmä ja käyttömenetelmä |
| WO1993008829A1 (en) | 1991-11-04 | 1993-05-13 | The Regents Of The University Of California | Compositions that mediate killing of hiv-infected cells |
| EP1514934B1 (en) | 1992-02-06 | 2008-12-31 | Novartis Vaccines and Diagnostics, Inc. | Biosynthetic binding protein for cancer marker |
| RU2139731C1 (ru) | 1992-11-13 | 1999-10-20 | Айдек Фармасьютикалс Корпорейшн (US | Способ лечения, антитела, гибридома |
| US5635483A (en) | 1992-12-03 | 1997-06-03 | Arizona Board Of Regents Acting On Behalf Of Arizona State University | Tumor inhibiting tetrapeptide bearing modified phenethyl amides |
| US5780588A (en) | 1993-01-26 | 1998-07-14 | Arizona Board Of Regents | Elucidation and synthesis of selected pentapeptides |
| WO1994029351A2 (en) | 1993-06-16 | 1994-12-22 | Celltech Limited | Antibodies |
| US5773001A (en) | 1994-06-03 | 1998-06-30 | American Cyanamid Company | Conjugates of methyltrithio antitumor agents and intermediates for their synthesis |
| US5789199A (en) | 1994-11-03 | 1998-08-04 | Genentech, Inc. | Process for bacterial production of polypeptides |
| US5840523A (en) | 1995-03-01 | 1998-11-24 | Genetech, Inc. | Methods and compositions for secretion of heterologous polypeptides |
| US5731168A (en) | 1995-03-01 | 1998-03-24 | Genentech, Inc. | Method for making heteromultimeric polypeptides |
| US5869046A (en) | 1995-04-14 | 1999-02-09 | Genentech, Inc. | Altered polypeptides with increased half-life |
| US5714586A (en) | 1995-06-07 | 1998-02-03 | American Cyanamid Company | Methods for the preparation of monomeric calicheamicin derivative/carrier conjugates |
| US5712374A (en) | 1995-06-07 | 1998-01-27 | American Cyanamid Company | Method for the preparation of substantiallly monomeric calicheamicin derivative/carrier conjugates |
| US6267958B1 (en) | 1995-07-27 | 2001-07-31 | Genentech, Inc. | Protein formulation |
| GB9603256D0 (en) | 1996-02-16 | 1996-04-17 | Wellcome Found | Antibodies |
| US6171586B1 (en) | 1997-06-13 | 2001-01-09 | Genentech, Inc. | Antibody formulation |
| DE69830315T2 (de) | 1997-06-24 | 2006-02-02 | Genentech Inc., San Francisco | Galactosylierte glykoproteine enthaltende zusammensetzungen und verfahren zur deren herstellung |
| US6040498A (en) | 1998-08-11 | 2000-03-21 | North Caroline State University | Genetically engineered duckweed |
| CA2307166A1 (en) | 1997-10-31 | 1999-05-14 | Genentech, Inc. | Methods and compositions comprising glycoprotein glycoforms |
| US6610833B1 (en) | 1997-11-24 | 2003-08-26 | The Institute For Human Genetics And Biochemistry | Monoclonal human natural antibodies |
| CA2312208C (en) | 1997-12-05 | 2011-01-25 | The Scripps Research Institute | Humanization of murine antibody |
| US6194551B1 (en) | 1998-04-02 | 2001-02-27 | Genentech, Inc. | Polypeptide variants |
| CA2323757C (en) | 1998-04-02 | 2011-08-02 | Genentech, Inc. | Antibody variants and fragments thereof |
| PT2180007E (pt) | 1998-04-20 | 2013-11-25 | Roche Glycart Ag | Engenharia de glicosilação de anticorpos para melhorar a citotoxicidade celular dependente de anticorpos |
| US6737056B1 (en) | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| HUP0104865A3 (en) | 1999-01-15 | 2004-07-28 | Genentech Inc | Polypeptide variants with altered effector function |
| DK2270147T4 (da) | 1999-04-09 | 2020-08-31 | Kyowa Kirin Co Ltd | Fremgangsmåde til at kontrollere aktiviteten af immunologisk funktionelt molekyle |
| US7125978B1 (en) | 1999-10-04 | 2006-10-24 | Medicago Inc. | Promoter for regulating expression of foreign genes |
| MXPA02003456A (es) | 1999-10-04 | 2002-10-23 | Medicago Inc | Metodo para regular la transcripcion de genes foraneos. |
| EP1229125A4 (en) | 1999-10-19 | 2005-06-01 | Kyowa Hakko Kogyo Kk | PROCESS FOR PREPARING A POLYPEPTIDE |
| WO2001044463A1 (en) | 1999-12-15 | 2001-06-21 | Genentech, Inc. | Shotgun scanning, a combinatorial method for mapping functional protein epitopes |
| PT1242438E (pt) | 1999-12-29 | 2007-02-28 | Immunogen Inc | Agentes citotóxicos compreendendo dixorrubicinas e daunorrubicinas modificadas e seu uso terapêutico |
| US20020004587A1 (en) | 2000-04-11 | 2002-01-10 | Genentech, Inc. | Multivalent antibodies and uses therefor |
| US6946292B2 (en) | 2000-10-06 | 2005-09-20 | Kyowa Hakko Kogyo Co., Ltd. | Cells producing antibody compositions with increased antibody dependent cytotoxic activity |
| DK2314686T4 (da) | 2000-10-06 | 2023-08-21 | Kyowa Kirin Co Ltd | Celler, der danner antistofsammensætninger |
| US7064191B2 (en) | 2000-10-06 | 2006-06-20 | Kyowa Hakko Kogyo Co., Ltd. | Process for purifying antibody |
| US6596541B2 (en) | 2000-10-31 | 2003-07-22 | Regeneron Pharmaceuticals, Inc. | Methods of modifying eukaryotic cells |
| CN101940189A (zh) | 2000-11-30 | 2011-01-12 | 米德列斯公司 | 用于生产人类抗体的转基因转染色体啮齿动物 |
| CA2455365C (en) | 2001-08-03 | 2014-07-29 | Glycart Biotechnology Ag | Antibody glycosylation variants having increased antibody-dependent cellular cytotoxicity |
| WO2003035835A2 (en) | 2001-10-25 | 2003-05-01 | Genentech, Inc. | Glycoprotein compositions |
| US20040093621A1 (en) | 2001-12-25 | 2004-05-13 | Kyowa Hakko Kogyo Co., Ltd | Antibody composition which specifically binds to CD20 |
| US20040110704A1 (en) | 2002-04-09 | 2004-06-10 | Kyowa Hakko Kogyo Co., Ltd. | Cells of which genome is modified |
| US20040259150A1 (en) | 2002-04-09 | 2004-12-23 | Kyowa Hakko Kogyo Co., Ltd. | Method of enhancing of binding activity of antibody composition to Fcgamma receptor IIIa |
| DE60336548D1 (de) | 2002-04-09 | 2011-05-12 | Kyowa Hakko Kirin Co Ltd | Zelle mit erniedrigter oder deletierter aktivität eines am gdp-fucosetransport beteiligten proteins |
| EP1500400A4 (en) | 2002-04-09 | 2006-10-11 | Kyowa Hakko Kogyo Kk | MEDICAMENT CONTAINING ANTIBODY COMPOSITION |
| WO2003085118A1 (en) | 2002-04-09 | 2003-10-16 | Kyowa Hakko Kogyo Co., Ltd. | Process for producing antibody composition |
| US20050031613A1 (en) | 2002-04-09 | 2005-02-10 | Kazuyasu Nakamura | Therapeutic agent for patients having human FcgammaRIIIa |
| JP4753578B2 (ja) | 2002-06-03 | 2011-08-24 | ジェネンテック， インコーポレイテッド | 合成抗体ファージライブラリー |
| US7361740B2 (en) | 2002-10-15 | 2008-04-22 | Pdl Biopharma, Inc. | Alteration of FcRn binding affinities or serum half-lives of antibodies by mutagenesis |
| ES2347241T3 (es) | 2002-12-16 | 2010-10-27 | Genentech, Inc. | Variantes de inmunoglobulina y sus utilizaciones. |
| EP1585767A2 (en) | 2003-01-16 | 2005-10-19 | Genentech, Inc. | Synthetic antibody phage libraries |
| US7871607B2 (en) | 2003-03-05 | 2011-01-18 | Halozyme, Inc. | Soluble glycosaminoglycanases and methods of preparing and using soluble glycosaminoglycanases |
| US20060104968A1 (en) | 2003-03-05 | 2006-05-18 | Halozyme, Inc. | Soluble glycosaminoglycanases and methods of preparing and using soluble glycosaminogly ycanases |
| CA2542046A1 (en) | 2003-10-08 | 2005-04-21 | Kyowa Hakko Kogyo Co., Ltd. | Fused protein composition |
| WO2005035778A1 (ja) | 2003-10-09 | 2005-04-21 | Kyowa Hakko Kogyo Co., Ltd. | α1,6-フコシルトランスフェラーゼの機能を抑制するRNAを用いた抗体組成物の製造法 |
| HRP20100303T1 (hr) | 2003-11-05 | 2010-07-31 | Roche Glycart Ag | Cd20 antitijela s povećanim afinitetom vezivanja fc receptora i efektorskim djelovanjem |
| ES2456325T3 (es) | 2003-11-06 | 2014-04-22 | Seattle Genetics, Inc. | Compuestos de monometilvalina capaces de conjugación con ligandos |
| WO2005053742A1 (ja) | 2003-12-04 | 2005-06-16 | Kyowa Hakko Kogyo Co., Ltd. | 抗体組成物を含有する医薬 |
| KR101245983B1 (ko) | 2004-03-31 | 2013-06-28 | 제넨테크, 인크. | 인간화 항-ｔｇｆ-베타 항체 |
| US7785903B2 (en) | 2004-04-09 | 2010-08-31 | Genentech, Inc. | Variable domain library and uses |
| ES2403055T3 (es) | 2004-04-13 | 2013-05-13 | F. Hoffmann-La Roche Ag | Anticuerpos anti-P-selectina |
| TWI380996B (zh) | 2004-09-17 | 2013-01-01 | Hoffmann La Roche | 抗ｏｘ４０ｌ抗體 |
| BRPI0516284A (pt) | 2004-09-23 | 2008-09-02 | Genentech Inc | anticorpo construìdo com cisteìna, método de selecionar anticorpos, compostos conjugados de droga-anticorpo, composição farmacêutica, método para matar ou inibir a proliferação de células de tumor, métodos de inibir a proliferação celular e o crescimento de células de tumor, artigo manufaturado e método para produzir um composto |
| JO3000B1 (ar) | 2004-10-20 | 2016-09-05 | Genentech Inc | مركبات أجسام مضادة . |
| ES2577292T3 (es) | 2005-11-07 | 2016-07-14 | Genentech, Inc. | Polipéptidos de unión con secuencias hipervariables de VH/VL diversificadas y consenso |
| WO2007064919A2 (en) | 2005-12-02 | 2007-06-07 | Genentech, Inc. | Binding polypeptides with restricted diversity sequences |
| TW200812616A (en) | 2006-05-09 | 2008-03-16 | Genentech Inc | Binding polypeptides with optimized scaffolds |
| US10118970B2 (en) | 2006-08-30 | 2018-11-06 | Genentech, Inc. | Multispecific antibodies |
| US20080226635A1 (en) | 2006-12-22 | 2008-09-18 | Hans Koll | Antibodies against insulin-like growth factor I receptor and uses thereof |
| CN100592373C (zh) | 2007-05-25 | 2010-02-24 | 群康科技(深圳)有限公司 | 液晶显示面板驱动装置及其驱动方法 |
| US20090074668A1 (en) * | 2007-09-14 | 2009-03-19 | Farjo Rafal A | Vldlr-/- mouse models and related methods |
| EP3663318A1 (en) | 2008-01-07 | 2020-06-10 | Amgen Inc. | Method for making antibody fc-heterodimeric molecules using electrostatic steering effects |
| JP5859307B2 (ja) | 2008-09-10 | 2016-02-10 | ジェネンテック， インコーポレイテッド | 眼の血管新生を阻害する方法 |
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2013
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- 2013-01-18 JP JP2014553427A patent/JP6242813B2/ja not_active Expired - Fee Related
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- 2013-01-18 WO PCT/US2013/022045 patent/WO2013109819A1/en not_active Ceased
- 2013-01-18 BR BR112014017518A patent/BR112014017518A2/pt not_active IP Right Cessation
- 2013-01-18 KR KR1020147022497A patent/KR20140116490A/ko not_active Withdrawn
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- 2014-07-17 CL CL2014001888A patent/CL2014001888A1/es unknown
- 2014-08-06 MA MA37268A patent/MA35898B1/fr unknown
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- 2015-10-09 US US14/879,702 patent/US9522954B2/en not_active Expired - Fee Related
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