CN102633881A - 针对her-3的抗体及其用途 - Google Patents
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Abstract
Description
链 | VH | D | J | 恒定区 | ORF |
重链 | VH4-34 | D1-20 | JH2 | γ | 是 |
重链 | VH2-5 | D6-6 | JH4b | Mu | 是 |
轻链 | A3 | JK2 | κ | 是 | |
轻链 | A20 | JK3 | κ | 是 | |
轻链 | B3 | JK1 | κ | 是 | |
轻链 | A27 | JK3 | κ | 否 |
Bin#1 | Bin#2 | Bin#3 | Bin#4 | Bin#5 |
U1-42 | U1-48 | U1-52 | U1-38 | U1-45 |
U1-44 | U1-50 | U1-39 | U1-40 | |
U1-62 | U1-51 | U1-41 | ||
U1-46 | U1-43 | |||
U1-47 | U1-49 | U1-61 | ||
U1-58 | U1-53 | |||
U1-55 | ||||
H1-H2-L1-L2-L3 | 计数 |
1-1-3-1-1 | 2 |
1-1-4-1*-1 | 1 |
1-2-2-1-1 | 4 |
1-2-8-1-1 | 1 |
1-3-2-1-1 | 3 |
1-3-4-1-1 | 1 |
3-1-2-1-1 | 21 |
3-1-4-1-1 | 5 |
3-1-8-1-1 | 2 |
3-s 18-2-1-1 | 1 |
Claims (30)
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US75510305P | 2005-12-30 | 2005-12-30 | |
US60/755,103 | 2005-12-30 |
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CN2006800498877A Active CN101365723B (zh) | 2005-12-30 | 2006-12-29 | 针对her-3的抗体及其用途 |
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US (6) | US7705130B2 (zh) |
EP (4) | EP3950715A1 (zh) |
JP (3) | JP5207979B2 (zh) |
KR (1) | KR101418606B1 (zh) |
CN (3) | CN102633881B (zh) |
AR (1) | AR056857A1 (zh) |
AU (1) | AU2006332065B2 (zh) |
BR (1) | BRPI0620803B8 (zh) |
CA (1) | CA2633222C (zh) |
CL (1) | CL2014001334A1 (zh) |
CR (1) | CR10082A (zh) |
CY (2) | CY1118979T1 (zh) |
DK (2) | DK1984402T3 (zh) |
EA (1) | EA015782B1 (zh) |
ES (3) | ES2621546T3 (zh) |
HK (3) | HK1133266A1 (zh) |
HR (2) | HRP20170558T1 (zh) |
HU (2) | HUE032209T2 (zh) |
IL (2) | IL225372A (zh) |
LT (2) | LT1984402T (zh) |
MX (1) | MX2008008248A (zh) |
MY (2) | MY153751A (zh) |
NO (1) | NO346160B1 (zh) |
NZ (3) | NZ596317A (zh) |
PL (2) | PL2993187T3 (zh) |
PT (2) | PT2993187T (zh) |
RS (2) | RS59100B1 (zh) |
SG (2) | SG174017A1 (zh) |
SI (1) | SI2993187T1 (zh) |
TW (2) | TWI523865B (zh) |
UA (1) | UA97473C2 (zh) |
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Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2023208216A1 (en) * | 2022-04-29 | 2023-11-02 | Sichuan Kelun-Biotech Biopharmaceutical Co., Ltd. | Antibody-drug conjugates and preparation methods and use thereof |
Families Citing this family (158)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2002051438A2 (en) | 2000-12-22 | 2002-07-04 | MAX-PLANCK-Gesellschaft zur Förderung der Wissenschaften e.V. | Use of repulsive guidance molecule (rgm) and its modulators |
EP1228766A1 (en) * | 2001-01-31 | 2002-08-07 | Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V. | PYK2 phosphorylation by HER3 induces tumor invasion |
TWI229650B (en) * | 2002-11-19 | 2005-03-21 | Sharp Kk | Substrate accommodating tray |
EP1868647A4 (en) * | 2005-03-24 | 2009-04-01 | Millennium Pharm Inc | OV064 BINDING ANTIBODIES AND METHOD FOR THEIR USE |
US8759490B2 (en) | 2005-03-24 | 2014-06-24 | Millennium Pharamaceuticals, Inc. | Antibodies that bind OV064 and methods of use therefor |
EP1928905B1 (de) | 2005-09-30 | 2015-04-15 | AbbVie Deutschland GmbH & Co KG | Bindungsdomänen von proteinen der repulsive guidance molecule (rgm) proteinfamilie und funktionale fragmente davon sowie deren verwendung |
AU2015201263B2 (en) * | 2005-12-30 | 2017-01-12 | Amgen Inc. | Material and methods for treating or preventing her-3 associated diseases |
AR056857A1 (es) | 2005-12-30 | 2007-10-24 | U3 Pharma Ag | Anticuerpos dirigidos hacia her-3 (receptor del factor de crecimiento epidérmico humano-3) y sus usos |
US20100047829A1 (en) * | 2006-11-28 | 2010-02-25 | U3 Pharma Gmbh | Activated her3 as a marker for predicting therapeutic efficacy |
EP3248617A3 (en) | 2007-02-16 | 2018-02-21 | Merrimack Pharmaceuticals, Inc. | Antibodies against erbb3 and uses thereof |
JP5779350B2 (ja) | 2007-03-27 | 2015-09-16 | シー レーン バイオテクノロジーズ, エルエルシー | 抗体代替軽鎖配列を含む構築物およびライブラリー |
EP1997830A1 (en) * | 2007-06-01 | 2008-12-03 | AIMM Therapeutics B.V. | RSV specific binding molecules and means for producing them |
US8962803B2 (en) * | 2008-02-29 | 2015-02-24 | AbbVie Deutschland GmbH & Co. KG | Antibodies against the RGM A protein and uses thereof |
KR20110014607A (ko) | 2008-04-29 | 2011-02-11 | 아보트 러보러터리즈 | 이원 가변 도메인 면역글로불린 및 이의 용도 |
WO2009151908A1 (en) * | 2008-05-25 | 2009-12-17 | Wyeth | Biomarkers for egfr/her/erbb drug efficacy |
EP2297208A4 (en) | 2008-06-03 | 2012-07-11 | Abbott Lab | DUAL VARIABLE DOMAIN IMMUNOGLOBULINS AND ITS USES |
EP2138511A1 (en) * | 2008-06-27 | 2009-12-30 | Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V. | HER3 as a determinant for the prognosis of melanoma |
CA2729949A1 (en) | 2008-07-08 | 2010-01-14 | Abbott Laboratories | Prostaglandin e2 dual variable domain immunoglobulins and uses thereof |
AU2013202410B2 (en) * | 2008-07-16 | 2014-10-09 | Institute For Research In Biomedicine | Human cytomegalovirus neautralizing antibodies and use thereof |
EP2318548B1 (en) * | 2008-08-15 | 2013-10-16 | Merrimack Pharmaceuticals, Inc. | Methods and systems for predicting response of cells to a therapeutic agent |
US8734795B2 (en) | 2008-10-31 | 2014-05-27 | Biogen Idec Ma Inc. | Light targeting molecules and uses thereof |
WO2010085845A1 (en) * | 2009-01-28 | 2010-08-05 | The University Of Queensland | Cancer therapy and/or diagnosis |
CA2753119A1 (en) * | 2009-02-24 | 2010-09-02 | F. Hoffmann-La Roche Ag | Use of s-erbb-3 as a marker for cancer |
TWI461211B (zh) | 2009-03-20 | 2014-11-21 | Genentech Inc | 抗-her抗體 |
EP2417159A1 (en) | 2009-04-07 | 2012-02-15 | Roche Glycart AG | Bispecific anti-erbb-3/anti-c-met antibodies |
WO2010127181A1 (en) * | 2009-04-29 | 2010-11-04 | Trellis Bioscience, Inc. | Improved antibodies immunoreactive with heregulin-coupled her3 |
CN102482345A (zh) | 2009-05-13 | 2012-05-30 | 航道生物技术有限责任公司 | 针对流感病毒的中和分子 |
WO2011004899A1 (en) * | 2009-07-06 | 2011-01-13 | Takeda Pharmaceutical Company Limited | Cancerous disease modifying antibodies |
BR112012004710A2 (pt) | 2009-09-01 | 2016-08-16 | Abbott Lab | imunoglobulinas de domínio variável duplo e uso das mesmas |
CA2775573A1 (en) * | 2009-10-09 | 2011-04-14 | Merck Sharp & Dohme Corp. | Generation, characterization and uses thereof of anti-her 3 antibodies |
MX2012004415A (es) | 2009-10-15 | 2012-05-08 | Abbott Lab | Inmunoglobulinas de dominio variable doble y usos de las mismas. |
US8785600B2 (en) * | 2009-10-23 | 2014-07-22 | Millennium Pharmaceuticals, Inc. | Anti-GCC antibody molecules and related compositions and methods |
UY32979A (es) | 2009-10-28 | 2011-02-28 | Abbott Lab | Inmunoglobulinas con dominio variable dual y usos de las mismas |
ES2860453T3 (es) | 2009-10-30 | 2021-10-05 | Novartis Ag | Bibliotecas universales del dominio de unión del lado inferior de la fibronectina de tipo III |
TWI630916B (zh) * | 2009-11-13 | 2018-08-01 | 第一三共歐洲公司 | 供治療或預防人表皮生長因子受體-3(her-3)相關疾病之藥料和方法 |
BR112012013734A2 (pt) | 2009-12-08 | 2017-01-10 | Abbott Gmbh & Co Kg | anticorpos monoclonais contra a proteína rgm a para uso no tratamento da degeneração da camada de fibras nervosas da retina. |
MY161909A (en) | 2009-12-22 | 2017-05-15 | Roche Glycart Ag | Anti-her3 antibodies and uses thereof |
EP2543727B1 (en) | 2010-03-02 | 2016-08-31 | Kyowa Hakko Kirin Co., Ltd. | Modified antibody composition |
SG183532A1 (en) | 2010-03-11 | 2012-09-27 | Merrimack Pharmaceuticals Inc | Use of erbb3 inhibitors in the treatment of triple negative and basal-like breast cancers |
ES2566602T3 (es) * | 2010-04-09 | 2016-04-14 | Aveo Pharmaceuticals, Inc. | Anticuerpos anti-ErbB3 |
WO2011144749A1 (en) | 2010-05-20 | 2011-11-24 | Ablynx Nv | Biological materials related to her3 |
AU2011274510A1 (en) | 2010-07-09 | 2013-01-24 | Exelixis, Inc. | Combinations of kinase inhibitors for the treatment of cancer |
CN107903321A (zh) | 2010-07-30 | 2018-04-13 | 诺华有限公司 | 纤连蛋白摇篮分子和其库 |
AU2011285852B2 (en) | 2010-08-03 | 2014-12-11 | Abbvie Inc. | Dual variable domain immunoglobulins and uses thereof |
WO2012019024A2 (en) * | 2010-08-04 | 2012-02-09 | Immunogen, Inc. | Her3-binding molecules and immunoconjugates thereof |
WO2012018404A2 (en) * | 2010-08-06 | 2012-02-09 | U3 Pharma Gmbh | Use of her3 binding agents in prostate treatment |
PT2606070T (pt) * | 2010-08-20 | 2017-03-31 | Novartis Ag | Anticorpos para o recetor 3 do fator de crescimento epidérmico (her3) |
PE20140229A1 (es) | 2010-08-26 | 2014-03-27 | Abbvie Inc | Inmunoglobulinas con dominio variable dual y usos de las mismas |
TW201302793A (zh) * | 2010-09-03 | 2013-01-16 | Glaxo Group Ltd | 新穎之抗原結合蛋白 |
IT1402149B1 (it) * | 2010-10-04 | 2013-08-28 | Ist Fisioterap Ospitalroma | Uso di un fosfopeptide in grado di bloccare l interazione her3/p85 per il trattamento dei tumori iperesprimenti her2. |
AU2011317743B2 (en) * | 2010-10-18 | 2015-05-21 | Mediapharma S.R.L. | ErbB3 binding antibody |
EP2635604B1 (en) * | 2010-11-01 | 2016-11-30 | Symphogen A/S | Pan-her antibody composition |
US9155802B2 (en) | 2010-11-01 | 2015-10-13 | Symphogen A/S | Pan-HER antibody composition |
ITRM20100577A1 (it) * | 2010-11-02 | 2012-05-03 | Takis Srl | Immunoterapia contro il recettore erbb-3 |
SG10201602874VA (en) | 2010-12-15 | 2016-05-30 | Kek High Energy Accelerator | Protein production method |
JP6047503B2 (ja) * | 2010-12-29 | 2016-12-21 | エクスプレッション、パソロジー、インコーポレイテッドExpression Pathology, Inc. | Her3タンパク質SRM/MRMアッセイ |
MX2013010379A (es) | 2011-03-11 | 2014-03-27 | Merrimack Pharmaceuticals Inc | Uso de inhibidores de receptores de la familia egfr en el tratamiento de canceres de mama refractarios a hormonas. |
BR112013022887A2 (pt) | 2011-03-15 | 2016-12-06 | Merrimack Pharmaceuticals Inc | superação de resistência a inibidores de via de erbb |
UA117218C2 (uk) | 2011-05-05 | 2018-07-10 | Мерк Патент Гмбх | Поліпептид, спрямований проти il-17a, il-17f та/або il17-a/f |
DK2707391T3 (en) * | 2011-05-13 | 2018-02-05 | Gamamabs Pharma | ANTIBODIES AGAINST HER3 |
CN103890010B (zh) | 2011-05-19 | 2017-04-19 | 法国国家健康医学研究院 | 抗‑人‑her3抗体及其用途 |
JPWO2012176779A1 (ja) * | 2011-06-20 | 2015-02-23 | 協和発酵キリン株式会社 | 抗erbB3抗体 |
CA2842860A1 (en) | 2011-07-28 | 2013-01-31 | Sea Lane Biotechnologies, Llc | Sur-binding proteins |
EP2748197A2 (en) | 2011-08-26 | 2014-07-02 | Merrimack Pharmaceuticals, Inc. | Tandem fc bispecific antibodies |
US9273143B2 (en) | 2011-09-30 | 2016-03-01 | Regeneron Pharmaceuticals, Inc. | Methods and compositions comprising a combination of an anti-ErbB3 antibody and an anti-EGFR antibody |
EP2760893B1 (en) | 2011-09-30 | 2018-09-12 | Regeneron Pharmaceuticals, Inc. | Anti-erbb3 antibodies and uses thereof |
AU2012318541B2 (en) | 2011-10-06 | 2018-04-12 | Aveo Pharmaceuticals, Inc. | Predicting tumor response to anti-ERBB3 antibodies |
JP2015504038A (ja) | 2011-10-31 | 2015-02-05 | ブリストル−マイヤーズ スクイブ カンパニーBristol−Myers Squibb Company | 低減した免疫原性を有するフィブロネクチン結合ドメイン |
JP6149042B2 (ja) * | 2011-11-09 | 2017-06-14 | ザ ユーエービー リサーチ ファンデーション | Her3抗体およびその使用 |
RU2620068C2 (ru) | 2011-11-23 | 2017-05-22 | МЕДИММЬЮН, ЭлЭлСи | Связывающие молекулы, специфичные по отношению к her3, и их применения |
BR112014013495A8 (pt) * | 2011-12-05 | 2017-06-13 | Novartis Ag | anticorpos para o receptor 3 do fator de crescimento epidérmico (her3) direcionados para o domínio iii e domíniuo iv de her3 |
KR20140103135A (ko) * | 2011-12-05 | 2014-08-25 | 노파르티스 아게 | Her3의 도메인 ii에 대해 지시된 표피 성장 인자 수용체 3 (her3)에 대한 항체 |
KR102083957B1 (ko) * | 2011-12-05 | 2020-03-04 | 노파르티스 아게 | 표피 성장 인자 수용체 3 (her3)에 대한 항체 |
ES2710916T3 (es) | 2011-12-22 | 2019-04-29 | I2 Pharmaceuticals Inc | Proteínas de unión sustitutas |
AU2012362326A1 (en) | 2011-12-30 | 2014-07-24 | Abbvie Inc. | Dual variable domain immunoglobulins against IL-13 and/or IL-17 |
IL297229A (en) | 2012-01-27 | 2022-12-01 | Abbvie Inc | The composition and method for the diagnosis and treatment of diseases related to the degeneration of nerve cells |
BR112014020666A2 (pt) * | 2012-02-23 | 2018-09-25 | U3 Pharma Gmbh | usos de um inibidor de her3 |
US20130259867A1 (en) | 2012-03-27 | 2013-10-03 | Genentech, Inc. | Diagnosis and treatments relating to her3 inhibitors |
NZ701601A (en) | 2012-04-27 | 2016-09-30 | Millennium Pharm Inc | Anti-gcc antibody molecules and use of same to test for susceptibility to gcc-targeted therapy |
AU2013255537B2 (en) | 2012-05-02 | 2018-02-15 | Symphogen A/S | Humanized pan-her antibody compositions |
KR20150076172A (ko) | 2012-09-25 | 2015-07-06 | 그렌마크 파머수티칼스 에스. 아. | 이질-이합체 면역글로불린의 정제 |
CA2928539A1 (en) * | 2012-10-25 | 2014-05-01 | Sorrento Therapeutics, Inc. | Antigen binding proteins that bind erbb3 |
SG11201503412RA (en) | 2012-11-01 | 2015-05-28 | Abbvie Inc | Anti-vegf/dll4 dual variable domain immunoglobulins and uses thereof |
KR20150063565A (ko) | 2012-11-08 | 2015-06-09 | 에프. 호프만-라 로슈 아게 | Her3의 베타-헤어핀 및 her4의 베타-헤어핀에 결합하는 항-her3/her4 항원 결합 단백질 |
WO2014072306A1 (en) | 2012-11-08 | 2014-05-15 | F. Hoffmann-La Roche Ag | Her3 antigen binding proteins binding to the beta-hairpin of her3 |
UY35148A (es) | 2012-11-21 | 2014-05-30 | Amgen Inc | Immunoglobulinas heterodiméricas |
AR094403A1 (es) | 2013-01-11 | 2015-07-29 | Hoffmann La Roche | Terapia de combinación de anticuerpos anti-her3 |
KR20150143458A (ko) | 2013-03-06 | 2015-12-23 | 메리맥 파마슈티컬즈, 인크. | 항-C-MET 탠덤 Fc 이중특이적 항체 |
CN105246508A (zh) | 2013-03-14 | 2016-01-13 | 基因泰克公司 | Mek抑制剂化合物与her3/egfr抑制剂化合物的组合及使用方法 |
CN105209493B (zh) * | 2013-03-14 | 2019-05-03 | 德克萨斯州大学系统董事会 | 用于诊断和治疗用途的her3特异性单克隆抗体 |
JP2016522793A (ja) | 2013-03-15 | 2016-08-04 | アッヴィ・インコーポレイテッド | IL−1βおよび/またはIL−17に対して指向された二重特異的結合タンパク質 |
US9708375B2 (en) | 2013-03-15 | 2017-07-18 | Amgen Inc. | Inhibitory polypeptides specific to WNT inhibitors |
EP2821071A1 (en) | 2013-07-04 | 2015-01-07 | Institut d'Investigació Biomèdica de Bellvitge (IDIBELL) | Compounds for breast cancer treatment |
TW201605896A (zh) * | 2013-08-30 | 2016-02-16 | 安美基股份有限公司 | Gitr抗原結合蛋白 |
JP6668241B2 (ja) | 2013-09-05 | 2020-03-18 | アムジエン・インコーポレーテツド | 予測可能で、一貫性のある、且つ再現可能な糖型特性を示すFc含有分子 |
WO2015048008A2 (en) | 2013-09-24 | 2015-04-02 | Medimmune, Llc | Binding molecules specific for her3 and uses thereof |
US10519247B2 (en) * | 2013-11-01 | 2019-12-31 | Board Of Regents,The University Of Texas System | Targeting HER2 and HER3 with bispecific antibodies in cancerous cells |
WO2015067986A1 (en) | 2013-11-07 | 2015-05-14 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Neuregulin allosteric anti-her3 antibody |
WO2015100459A2 (en) | 2013-12-27 | 2015-07-02 | Merrimack Pharmaceuticals, Inc. | Biomarker profiles for predicting outcomes of cancer therapy with erbb3 inhibitors and/or chemotherapies |
BR112016020752B1 (pt) | 2014-03-11 | 2023-11-14 | Regeneron Pharmaceuticals, Inc | Anticorpo isolado ou fragmento de ligação a antígeno do mesmo, composição farmacêutica, e, uso de uma composição farmacêutica |
ES2859648T3 (es) | 2014-04-10 | 2021-10-04 | Daiichi Sankyo Co Ltd | Conjugado anticuerpo-fármaco anti-HER3 |
US10745490B2 (en) | 2014-04-11 | 2020-08-18 | Celldex Therapeutics, Inc. | Anti-ErbB antibodies and methods of use thereof |
FR3020063A1 (fr) | 2014-04-16 | 2015-10-23 | Gamamabs Pharma | Anticorps humain anti-her4 |
WO2015173250A1 (en) | 2014-05-14 | 2015-11-19 | F. Hoffmann-La Roche Ag | Anti-her3 antibodies binding to the beta-hairpin of her3 |
JP6671298B2 (ja) | 2014-05-16 | 2020-03-25 | アムジェン インコーポレイテッド | Th1及びth2細胞集団を検出するためのアッセイ |
WO2016059602A2 (en) | 2014-10-16 | 2016-04-21 | Glaxo Group Limited | Methods of treating cancer and related compositions |
WO2016094881A2 (en) | 2014-12-11 | 2016-06-16 | Abbvie Inc. | Lrp-8 binding proteins |
MY178919A (en) | 2015-03-09 | 2020-10-23 | Agensys Inc | Antibody drug conjugates (adc) that bind to flt3 proteins |
EP3091033A1 (en) | 2015-05-06 | 2016-11-09 | Gamamabs Pharma | Anti-human-her3 antibodies and uses thereof |
US10184006B2 (en) | 2015-06-04 | 2019-01-22 | Merrimack Pharmaceuticals, Inc. | Biomarkers for predicting outcomes of cancer therapy with ErbB3 inhibitors |
TW201710286A (zh) | 2015-06-15 | 2017-03-16 | 艾伯維有限公司 | 抗vegf、pdgf及/或其受體之結合蛋白 |
ES2938186T3 (es) | 2015-06-29 | 2023-04-05 | Daiichi Sankyo Co Ltd | Procedimiento de fabricación selectiva de un conjugado anticuerpo-fármaco |
TW201716439A (zh) | 2015-07-20 | 2017-05-16 | 美國禮來大藥廠 | Her3抗體 |
MA43416A (fr) | 2015-12-11 | 2018-10-17 | Regeneron Pharma | Méthodes pour ralentir ou empêcher la croissance de tumeurs résistantes au blocage de l'egfr et/ou d'erbb3 |
MX2018011054A (es) | 2016-03-15 | 2019-01-21 | Merrimack Pharmaceuticals Inc | Metodos para tratar cancer de mama er+, her2-, hrg+ usando terapias de combinacion que comprenden un anticuerpo anti-erbb3. |
AU2017235571B2 (en) * | 2016-03-18 | 2024-05-16 | Georgetown University | Targeting tumor cells with chemotherapeutic agents conjugated to anti-matriptase antibodies by in vivo cleavable linking moieties |
WO2018107125A1 (en) | 2016-12-09 | 2018-06-14 | Seattle Genetics, Inc. | Bivalent antibodies masked by coiled coils |
CA3046293A1 (en) | 2016-12-12 | 2018-06-21 | Daiichi Sankyo Company, Limited | Combination of antibody-drug conjugate and immune checkpoint inhibitor |
EP3572428A4 (en) | 2017-01-17 | 2020-12-30 | Daiichi Sankyo Company, Limited | ANTI-GPR20 ANTIBODY AND ANTI-GPR20 ANTIBODY MEDICINAL CONJUGATE |
TW201834696A (zh) | 2017-02-28 | 2018-10-01 | 學校法人近畿大學 | 藉由投予抗her3抗體-藥物複合體之egfr-tki抗性之非小細胞肺癌的治療方法 |
CA3056011A1 (en) | 2017-03-14 | 2018-09-20 | Amgen Inc. | Control of total afucosylated glycoforms of antibodies produced in cell culture |
TW202330036A (zh) | 2017-05-15 | 2023-08-01 | 日商第一三共股份有限公司 | 抗體-藥物結合物之製造方法 |
EP3673918A4 (en) | 2017-08-23 | 2021-05-19 | Daiichi Sankyo Company, Limited | ANTIBODY-DRUG CONJUGATE PREPARATION AND ASSOCIATED LYOPHILIZATION |
WO2019044947A1 (ja) | 2017-08-31 | 2019-03-07 | 第一三共株式会社 | 抗体-薬物コンジュゲートの改良製造方法 |
CN117838881A (zh) | 2017-08-31 | 2024-04-09 | 第一三共株式会社 | 制备抗体-药物缀合物的新方法 |
EP3758751A4 (en) | 2018-02-28 | 2021-11-17 | Wuxi Biologics Ireland Limited. | MONOCLONAL ANTIBODIES AGAINST HUMAN LAG-3, METHOD OF MANUFACTURING AND USING THEREOF |
JP7328983B2 (ja) | 2018-03-22 | 2023-08-17 | サーフィス オンコロジー インコーポレイテッド | 抗il-27抗体及びその使用 |
US20210079065A1 (en) | 2018-03-26 | 2021-03-18 | Amgen Inc. | Total afucosylated glycoforms of antibodies produced in cell culture |
WO2019210144A1 (en) * | 2018-04-27 | 2019-10-31 | Vanderbilt University | Broadly neutralizing antibodies against hepatitis c virus |
EP4257611A3 (en) | 2018-05-18 | 2024-03-06 | Glycotope GmbH | Anti-muc1 antibody |
AU2019311557A1 (en) | 2018-07-25 | 2021-02-04 | Daiichi Sankyo Company, Limited | Effective method for manufacturing antibody-drug conjugate |
EP3831853A4 (en) | 2018-07-27 | 2022-06-01 | Daiichi Sankyo Company, Limited | ANTIBODY-DRUG CONJUGATE PROTEIN-RECOGNIZING DRUG UNIT |
BR112021001509A2 (pt) | 2018-07-31 | 2021-04-27 | Daiichi Sankyo Company, Limited | agente terapêutico para um tumor de cérebro metastásico |
CN112512587A (zh) | 2018-08-06 | 2021-03-16 | 第一三共株式会社 | 抗体药物缀合物和微管蛋白抑制剂的组合 |
EP3842546A4 (en) | 2018-08-23 | 2022-06-29 | Daiichi Sankyo Company, Limited | Sensitivity marker for antibody-drug conjugate |
KR20210062005A (ko) | 2018-09-20 | 2021-05-28 | 다이이찌 산쿄 가부시키가이샤 | 항 her3 항체-약물 콘쥬게이트 투여에 의한 her3 변이암의 치료 |
CN111289748A (zh) * | 2018-12-08 | 2020-06-16 | 惠州市中大惠亚医院 | ErbB3蛋白在制备膀胱癌无创诊断产品中的应用 |
KR20210102341A (ko) | 2018-12-11 | 2021-08-19 | 다이이찌 산쿄 가부시키가이샤 | 항체-약물 컨쥬게이트와 parp 저해제의 조합 |
MA54469A (fr) * | 2018-12-13 | 2021-10-20 | Surface Oncology Inc | Anticorps anti-il-27 et leurs utilisations |
US20220040324A1 (en) | 2018-12-21 | 2022-02-10 | Daiichi Sankyo Company, Limited | Combination of antibody-drug conjugate and kinase inhibitor |
WO2021062372A1 (en) | 2019-09-26 | 2021-04-01 | Amgen Inc. | Methods of producing antibody compositions |
CN114846028A (zh) * | 2019-11-01 | 2022-08-02 | 美真达治疗公司 | 抗cd45抗体及其结合物 |
KR20210095781A (ko) | 2020-01-24 | 2021-08-03 | 주식회사 에이프릴바이오 | 항원결합 단편 및 생리활성 이펙터 모이어티로 구성된 융합 컨스트럭트를 포함하는 다중결합항체 및 이를 포함하는 약학조성물 |
JP2023517889A (ja) * | 2020-03-10 | 2023-04-27 | マサチューセッツ インスティテュート オブ テクノロジー | NPM1c陽性がんの免疫療法のための組成物および方法 |
EP4162257A1 (en) | 2020-06-04 | 2023-04-12 | Amgen Inc. | Assessment of cleaning procedures of a biotherapeutic manufacturing process |
US20240026028A1 (en) | 2020-10-14 | 2024-01-25 | Jiangsu Hengrui Pharmaceuticals Co., Ltd. | Anti-her3 antibody and anti-her3 antibody-drug conjugate and medical use thereof |
CA3197930A1 (en) | 2020-10-15 | 2022-04-21 | Amgen Inc. | Relative unpaired glycans in antibody production methods |
WO2022102634A1 (ja) | 2020-11-11 | 2022-05-19 | 第一三共株式会社 | 抗体-薬物コンジュゲートと抗SIRPα抗体の組み合わせ |
KR20230164128A (ko) | 2021-03-31 | 2023-12-01 | 디디바이오. 코포레이션 엘티디.,(상하이) | 기능성 항원 결합 단백질 선별을 위한 벡터 및 방법 |
TW202308701A (zh) | 2021-04-29 | 2023-03-01 | 大陸商上海匯連生物醫藥有限公司 | 抗體偶聯藥物的製備方法及應用 |
CA3222409A1 (en) | 2021-06-07 | 2022-12-15 | Amgen Inc. | Using fucosidase to control afucosylation level of glycosylated proteins |
WO2023024949A1 (zh) | 2021-08-24 | 2023-03-02 | 昆山新蕴达生物科技有限公司 | 一种由可断裂连接子偶联的抗体偶联药物 |
WO2023059607A1 (en) | 2021-10-05 | 2023-04-13 | Amgen Inc. | Fc-gamma receptor ii binding and glycan content |
WO2023103854A1 (zh) | 2021-12-09 | 2023-06-15 | 昆山新蕴达生物科技有限公司 | 一种亲和力改善的抗体-药物偶联物、其制备方法及应用 |
WO2023165475A1 (zh) * | 2022-03-03 | 2023-09-07 | 四川科伦博泰生物医药股份有限公司 | Her3结合蛋白及其用途 |
TW202400140A (zh) | 2022-04-27 | 2024-01-01 | 日商第一三共股份有限公司 | 抗體-藥物結合物與ezh1及/或ezh2抑制劑之組合 |
WO2023215725A1 (en) | 2022-05-02 | 2023-11-09 | Fred Hutchinson Cancer Center | Compositions and methods for cellular immunotherapy |
WO2023218378A1 (en) | 2022-05-11 | 2023-11-16 | Daiichi Sankyo Company, Limited | Combination of an antibody specific for a tumor antigen and a cd47 inhibitor |
Citations (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1998050433A2 (en) * | 1997-05-05 | 1998-11-12 | Abgenix, Inc. | Human monoclonal antibodies to epidermal growth factor receptor |
US20020064805A1 (en) * | 1996-03-27 | 2002-05-30 | Genentech, Inc. | Isolated nucleic acids, vectors and host cells encoding ErbB3 antibodies |
WO2003013602A1 (en) * | 2001-08-09 | 2003-02-20 | MAX-PLANCK-Gesellschaft zur Förderung der Wissenschaften e.V. | Inhibitors of her3 activity |
WO2003080835A1 (en) * | 2002-03-26 | 2003-10-02 | Zensun (Shanghai) Sci-Tech. Ltd. | Erbb3 based methods and compositions for treating neoplasms |
US20040071696A1 (en) * | 2002-04-05 | 2004-04-15 | The Regents Of The University Of California | Bispecific single chain Fv antibody molecules and methods of use thereof |
Family Cites Families (73)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US3180193A (en) | 1963-02-25 | 1965-04-27 | Benedict David | Machines for cutting lengths of strip material |
US4399216A (en) | 1980-02-25 | 1983-08-16 | The Trustees Of Columbia University | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
JPS58166634A (ja) | 1982-03-29 | 1983-10-01 | Toshiba Corp | 有機溶媒電池用正極 |
JPS58166633A (ja) | 1982-03-29 | 1983-10-01 | Toshiba Corp | 有機溶媒電池用正極 |
GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
US4740461A (en) | 1983-12-27 | 1988-04-26 | Genetics Institute, Inc. | Vectors and methods for transformation of eucaryotic cells |
JPS62170639A (ja) | 1986-01-22 | 1987-07-27 | 株式会社システムメンテナンス | 防蟻板の取付け工法 |
US4959455A (en) | 1986-07-14 | 1990-09-25 | Genetics Institute, Inc. | Primate hematopoietic growth factors IL-3 and pharmaceutical compositions |
US4912040A (en) | 1986-11-14 | 1990-03-27 | Genetics Institute, Inc. | Eucaryotic expression system |
FR2625508B1 (fr) | 1987-12-30 | 1992-05-22 | Charbonnages Ste Chimique | Compositions polymeres ignifugees et leur application au revetement de cables electriques |
GB8823869D0 (en) | 1988-10-12 | 1988-11-16 | Medical Res Council | Production of antibodies |
US5175384A (en) | 1988-12-05 | 1992-12-29 | Genpharm International | Transgenic mice depleted in mature t-cells and methods for making transgenic mice |
US5183884A (en) | 1989-12-01 | 1993-02-02 | United States Of America | Dna segment encoding a gene for a receptor related to the epidermal growth factor receptor |
US6673986B1 (en) | 1990-01-12 | 2004-01-06 | Abgenix, Inc. | Generation of xenogeneic antibodies |
US6075181A (en) | 1990-01-12 | 2000-06-13 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
AU633698B2 (en) | 1990-01-12 | 1993-02-04 | Amgen Fremont Inc. | Generation of xenogeneic antibodies |
US6150584A (en) | 1990-01-12 | 2000-11-21 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
FR2664073A1 (fr) | 1990-06-29 | 1992-01-03 | Thomson Csf | Moyens de marquage d'objets, procede de realisation et dispositif de lecture. |
US6255458B1 (en) | 1990-08-29 | 2001-07-03 | Genpharm International | High affinity human antibodies and human antibodies against digoxin |
WO1992003918A1 (en) | 1990-08-29 | 1992-03-19 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
US5789650A (en) | 1990-08-29 | 1998-08-04 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
US5770429A (en) | 1990-08-29 | 1998-06-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
US5877397A (en) | 1990-08-29 | 1999-03-02 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
US5874299A (en) | 1990-08-29 | 1999-02-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
EP0546091B1 (en) | 1990-08-29 | 2007-01-24 | Pharming Intellectual Property BV | Homologous recombination in mammalian cells |
US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
US5814318A (en) | 1990-08-29 | 1998-09-29 | Genpharm International Inc. | Transgenic non-human animals for producing heterologous antibodies |
US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
US6300129B1 (en) | 1990-08-29 | 2001-10-09 | Genpharm International | Transgenic non-human animals for producing heterologous antibodies |
WO1992022670A1 (en) | 1991-06-12 | 1992-12-23 | Genpharm International, Inc. | Early detection of transgenic embryos |
WO1992022645A1 (en) | 1991-06-14 | 1992-12-23 | Genpharm International, Inc. | Transgenic immunodeficient non-human animals |
WO1993004169A1 (en) | 1991-08-20 | 1993-03-04 | Genpharm International, Inc. | Gene targeting in animal cells using isogenic dna constructs |
EP0746609A4 (en) | 1991-12-17 | 1997-12-17 | Genpharm Int | NON-HUMAN TRANSGENIC ANIMALS CAPABLE OF PRODUCING HETEROLOGOUS ANTIBODIES |
CA2135313A1 (en) | 1992-06-18 | 1994-01-06 | Theodore Choi | Methods for producing transgenic non-human animals harboring a yeast artificial chromosome |
NZ255101A (en) | 1992-07-24 | 1997-08-22 | Cell Genesys Inc | A yeast artificial chromosome (yac) vector containing an hprt minigene expressible in murine stem cells and genetically modified rodent therefor |
US5981175A (en) | 1993-01-07 | 1999-11-09 | Genpharm Internation, Inc. | Methods for producing recombinant mammalian cells harboring a yeast artificial chromosome |
EP0754225A4 (en) | 1993-04-26 | 2001-01-31 | Genpharm Int | HETEROLOGIC ANTIBODY-PRODUCING TRANSGENIC NON-HUMAN ANIMALS |
US5625825A (en) | 1993-10-21 | 1997-04-29 | Lsi Logic Corporation | Random number generating apparatus for an interface unit of a carrier sense with multiple access and collision detect (CSMA/CD) ethernet data network |
EP0730646A1 (en) | 1993-11-23 | 1996-09-11 | Genentech, Inc. | PROTEIN TYROSINE KINASES NAMED Rse |
US5643763A (en) | 1994-11-04 | 1997-07-01 | Genpharm International, Inc. | Method for making recombinant yeast artificial chromosomes by minimizing diploid doubling during mating |
US5837815A (en) | 1994-12-15 | 1998-11-17 | Sugen, Inc. | PYK2 related polypeptide products |
CA2219486A1 (en) | 1995-04-28 | 1996-10-31 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
CN101333516A (zh) | 1995-08-29 | 2008-12-31 | 麒麟医药株式会社 | 嵌合体动物及其制备方法 |
PT896586E (pt) | 1996-03-27 | 2007-01-31 | Genentech Inc | Anticorpos de erbb3 |
US6114595A (en) * | 1996-04-11 | 2000-09-05 | The Procter & Gamble Company | Stretchable, extensible composite topsheet for absorbent articles |
US5916771A (en) | 1996-10-11 | 1999-06-29 | Abgenix, Inc. | Production of a multimeric protein by cell fusion method |
CA2616914C (en) | 1996-12-03 | 2012-05-29 | Abgenix, Inc. | Egfr-binding antibody |
ES2227729T3 (es) | 1996-12-11 | 2005-04-01 | Sugen, Inc. | Metodos de cribaje para compuestos unidos al polipeptido pyk2. |
EP1141722A1 (en) | 1998-12-31 | 2001-10-10 | Sugen, Inc. | Pyk2 (raftk) and inflammation |
US6833268B1 (en) | 1999-06-10 | 2004-12-21 | Abgenix, Inc. | Transgenic animals for producing specific isotypes of human antibodies via non-cognate switch regions |
AUPQ105799A0 (en) * | 1999-06-18 | 1999-07-08 | Victor Chang Cardiac Research Institute, The | Cell growth inhibition |
AU784045B2 (en) | 1999-06-25 | 2006-01-19 | Genentech Inc. | Humanized anti-ErbB2 antibodies and treatment with anti-ErbB2 antibodies |
US6949245B1 (en) | 1999-06-25 | 2005-09-27 | Genentech, Inc. | Humanized anti-ErbB2 antibodies and treatment with anti-ErbB2 antibodies |
US6627196B1 (en) | 1999-08-27 | 2003-09-30 | Genentech, Inc. | Dosages for treatment with anti-ErbB2 antibodies |
FR2817258B1 (fr) * | 2000-11-27 | 2003-01-10 | Atofina | Procede de sulfochloration photochimique d'alcanes gazeux |
US7125680B2 (en) * | 2001-07-27 | 2006-10-24 | The Regents Of The University Of California | Methods and materials for characterizing and modulating interaction between heregulin and HER3 |
ATE443259T1 (de) * | 2001-09-20 | 2009-10-15 | Univ Texas | Bestimmung der zirkulierenden therapeutischen antikörper, antigene sowie antigen-antikörper- komplexe mit elisa-tests |
US7435871B2 (en) | 2001-11-30 | 2008-10-14 | Amgen Fremont Inc. | Transgenic animals bearing human Igλ light chain genes |
EP1554576B9 (en) | 2001-12-03 | 2008-08-20 | Amgen Fremont Inc. | Identification of high affinity molecules by limited dilution screening |
CN1219882C (zh) | 2002-03-18 | 2005-09-21 | 上海泽生科技开发有限公司 | 以erbb-3为基础的用于肿瘤治疗的方法和组合物 |
KR20050025669A (ko) | 2002-07-25 | 2005-03-14 | 아클라라 바이오사이언시스 인코퍼레이티드 | 수용체 올리고머화의 검출 |
ES2347239T3 (es) * | 2002-12-02 | 2010-10-27 | Amgen Fremont Inc. | Anticuerpos dirigidos al factor de necrosis tumoral y usos de los mismos. |
JP2006521821A (ja) | 2003-04-01 | 2006-09-28 | モノグラム バイオサイエンシズ,インコーポレーテッド | バイオマーカーとしての表面受容体複合体 |
JP2005024385A (ja) | 2003-07-02 | 2005-01-27 | Matsushita Electric Ind Co Ltd | 感圧センサ |
AR056857A1 (es) * | 2005-12-30 | 2007-10-24 | U3 Pharma Ag | Anticuerpos dirigidos hacia her-3 (receptor del factor de crecimiento epidérmico humano-3) y sus usos |
TWI630916B (zh) * | 2009-11-13 | 2018-08-01 | 第一三共歐洲公司 | 供治療或預防人表皮生長因子受體-3(her-3)相關疾病之藥料和方法 |
WO2012018404A2 (en) * | 2010-08-06 | 2012-02-09 | U3 Pharma Gmbh | Use of her3 binding agents in prostate treatment |
JP6071725B2 (ja) | 2013-04-23 | 2017-02-01 | カルソニックカンセイ株式会社 | 電気自動車の駆動力制御装置 |
EP3684399A1 (en) * | 2017-12-29 | 2020-07-29 | Cellectis | Method for improving production of car t cells |
US11284893B2 (en) | 2019-04-02 | 2022-03-29 | Covidien Lp | Stapling device with articulating tool assembly |
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Patent Citations (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US20020064805A1 (en) * | 1996-03-27 | 2002-05-30 | Genentech, Inc. | Isolated nucleic acids, vectors and host cells encoding ErbB3 antibodies |
WO1998050433A2 (en) * | 1997-05-05 | 1998-11-12 | Abgenix, Inc. | Human monoclonal antibodies to epidermal growth factor receptor |
WO2003013602A1 (en) * | 2001-08-09 | 2003-02-20 | MAX-PLANCK-Gesellschaft zur Förderung der Wissenschaften e.V. | Inhibitors of her3 activity |
WO2003080835A1 (en) * | 2002-03-26 | 2003-10-02 | Zensun (Shanghai) Sci-Tech. Ltd. | Erbb3 based methods and compositions for treating neoplasms |
US20040071696A1 (en) * | 2002-04-05 | 2004-04-15 | The Regents Of The University Of California | Bispecific single chain Fv antibody molecules and methods of use thereof |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2023208216A1 (en) * | 2022-04-29 | 2023-11-02 | Sichuan Kelun-Biotech Biopharmaceutical Co., Ltd. | Antibody-drug conjugates and preparation methods and use thereof |
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