NO324181B1 - Monoklonalt antistoff spesifikt for human IL-5 og fragmenter derav, hybridoma cellelinjer, endret antistoff, immunolglobulin-tungkjede-komplementaritetsbestemmende region, nukleinsyremolekyl, kimaert antistoff, farmasoytisk preparat omfattende endret antistoff, anvendelse av antistoff, isolert nukleinsyresekvens, rekombinant plasmid, vertcelle, fremgangsmate for a fremstille et endret antistoff og metoder for a bestemme human IL-50. - Google Patents

Monoklonalt antistoff spesifikt for human IL-5 og fragmenter derav, hybridoma cellelinjer, endret antistoff, immunolglobulin-tungkjede-komplementaritetsbestemmende region, nukleinsyremolekyl, kimaert antistoff, farmasoytisk preparat omfattende endret antistoff, anvendelse av antistoff, isolert nukleinsyresekvens, rekombinant plasmid, vertcelle, fremgangsmate for a fremstille et endret antistoff og metoder for a bestemme human IL-50. Download PDF

Info

Publication number: NO324181B1
Authority: NO; Norway
Prior art keywords: antibody; seq; human; nucleic acid; acid sequence
Prior art date: 1994-12-23

Application number

NO19972913A

Other languages

English (en)

Norwegian (no)

Other versions

NO972913L (no

NO972913D0 (no

Inventor

Mitchell Stuart Gross

Stephen Dudley Holmes

Robert S Ames

Edward Robert Appelbaum

Irwin M Chaiken

Richard M Cook

Lynette Jane Mcmillan

Timothy Wayne Theisen

Original Assignee

Smithkline Beecham Corp

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1994-12-23

Filing date

1997-06-20

Publication date

2007-09-03

Family has litigation

First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=27408594&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=NO324181(B1) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.

1995-06-06 Priority claimed from US08/467,420 external-priority patent/US5683892A/en

1997-06-20 Application filed by Smithkline Beecham Corp filed Critical Smithkline Beecham Corp

1997-06-20 Publication of NO972913D0 publication Critical patent/NO972913D0/no

1997-08-19 Publication of NO972913L publication Critical patent/NO972913L/no

2007-09-03 Publication of NO324181B1 publication Critical patent/NO324181B1/no

Links

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- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6863—Cytokines, i.e. immune system proteins modifying a biological response such as cell growth proliferation or differentiation, e.g. TNF, CNF, GM-CSF, lymphotoxin, MIF or their receptors
- G01N33/6869—Interleukin
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
- 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
- C07K2317/55—Fab or Fab'
- C—CHEMISTRY; METALLURGY
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- 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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- C07—ORGANIC CHEMISTRY
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- C07K2317/00—Immunoglobulins specific features
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- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/565—Complementarity determining region [CDR]
- 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
- 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
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
- 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
- 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
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- 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

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NO19972913A 1994-12-23 1997-06-20 Monoklonalt antistoff spesifikt for human IL-5 og fragmenter derav, hybridoma cellelinjer, endret antistoff, immunolglobulin-tungkjede-komplementaritetsbestemmende region, nukleinsyremolekyl, kimaert antistoff, farmasoytisk preparat omfattende endret antistoff, anvendelse av antistoff, isolert nukleinsyresekvens, rekombinant plasmid, vertcelle, fremgangsmate for a fremstille et endret antistoff og metoder for a bestemme human IL-50. NO324181B1 (no)

Applications Claiming Priority (4)

Application Number	Priority Date	Filing Date	Title
US36313194A	1994-12-23	1994-12-23
US08/467,420 US5683892A (en)	1994-12-23	1995-06-06	DNA encoding recombinant IL-5 antagonists useful in treatment of IL-5 mediated disorders
US08/470,110 US5693323A (en)	1994-12-23	1995-06-06	Recombinant IL-5 antagonists useful in treatment of IL-5 mediated disorders
PCT/US1995/017082 WO1996021000A2 (en)	1994-12-23	1995-12-22	Recombinant il-5 antagonists useful in treatment of il-5 mediated disorders

Publications (3)

Publication Number	Publication Date
NO972913D0 NO972913D0 (no)	1997-06-20
NO972913L NO972913L (no)	1997-08-19
NO324181B1 true NO324181B1 (no)	2007-09-03

Family

ID=27408594

Family Applications (2)

Application Number	Title	Priority Date	Filing Date
NO19972913A NO324181B1 (no)	1994-12-23	1997-06-20	Monoklonalt antistoff spesifikt for human IL-5 og fragmenter derav, hybridoma cellelinjer, endret antistoff, immunolglobulin-tungkjede-komplementaritetsbestemmende region, nukleinsyremolekyl, kimaert antistoff, farmasoytisk preparat omfattende endret antistoff, anvendelse av antistoff, isolert nukleinsyresekvens, rekombinant plasmid, vertcelle, fremgangsmate for a fremstille et endret antistoff og metoder for a bestemme human IL-50.
NO2015027C NO2015027I2 (no)	1994-12-23	2015-12-18	Mepolizumab

Family Applications After (1)

Application Number	Title	Priority Date	Filing Date
NO2015027C NO2015027I2 (no)	1994-12-23	2015-12-18	Mepolizumab

Country Status (22)

Country	Link
US (1)	US6129913A (fi)
EP (1)	EP0800536B1 (fi)
JP (2)	JP2001523083A (fi)
CN (1)	CN100391977C (fi)
AT (1)	ATE346867T1 (fi)
AU (1)	AU708951B2 (fi)
BR (1)	BR9510499B1 (fi)
CA (1)	CA2208503C (fi)
CZ (1)	CZ297045B6 (fi)
DE (1)	DE69535319T2 (fi)
DK (1)	DK0800536T3 (fi)
ES (1)	ES2277336T3 (fi)
FI (1)	FI119374B (fi)
HK (1)	HK1003651A1 (fi)
HU (1)	HU222992B1 (fi)
LU (1)	LU92912I2 (fi)
MX (1)	MX9704779A (fi)
NL (1)	NL300787I2 (fi)
NO (2)	NO324181B1 (fi)
NZ (1)	NZ301916A (fi)
PL (1)	PL194312B1 (fi)
WO (1)	WO1996021000A2 (fi)

Families Citing this family (21)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5693323A (en) *	1994-12-23	1997-12-02	Smithkline Beecham Corporation	Recombinant IL-5 antagonists useful in treatment of IL-5 mediated disorders
US5783184A (en) *	1994-12-23	1998-07-21	Smithkline Beecham Corporation	Method for treatment and diagnosis of IL-5 mediated disorders
CA2369292C (en) *	1999-04-09	2010-09-21	Kyowa Hakko Kogyo Co. Ltd.	Method of modulating the activity of functional immune molecules
US6946292B2 (en)	2000-10-06	2005-09-20	Kyowa Hakko Kogyo Co., Ltd.	Cells producing antibody compositions with increased antibody dependent cytotoxic activity
AU2003220525A1 (en) *	2002-03-29	2003-10-20	Abgenix, Inc.	Human monoclonal antibodies to interleukin-5 and methods and compositions comprising same
US7691568B2 (en)	2002-04-09	2010-04-06	Kyowa Hakko Kirin Co., Ltd	Antibody composition-containing medicament
EP1682571A4 (en) *	2003-10-27	2006-12-06	Medvet Science Pty Ltd	BICOORDIN PATTERN AND METHODS OF USE
KR101206318B1 (ko) *	2004-10-28	2012-11-29	교와 핫꼬 기린 가부시키가이샤	자궁 내막증 치료제
JP2010526088A (ja)	2007-04-30	2010-07-29	グラクソスミスクライン・リミテッド・ライアビリティ・カンパニー	抗ｉｌ−５抗体を投与するための方法
JP4335286B2 (ja)	2008-02-08	2009-09-30	ファナック株式会社	部品保護機能を備えたロボット制御装置及びロボット制御方法
BRPI0910854A2 (pt)	2008-03-28	2015-10-06	Glaxosmithkline Llc	métodos de tratamento
WO2011094259A2 (en) *	2010-01-28	2011-08-04	Glaxo Group Limited	Cd127 binding proteins
US9505826B2 (en)	2010-12-22	2016-11-29	Teva Pharmaceuticals Australia Pty Ltd	Modified antibody with improved half-life
EA037487B1 (ru)	2015-08-24	2021-04-02	Глэксосмитклайн Интеллекчуал Проперти (No.2) Лимитед	Биофармацевтические композиции
US11046782B2 (en) *	2016-03-30	2021-06-29	Musc Foundation For Research Development	Methods for treatment and diagnosis of cancer by targeting glycoprotein A repetitions predominant (GARP) and for providing effective immunotherapy alone or in combination
US11111292B2 (en) *	2016-12-23	2021-09-07	Cephalon, Inc.	Anti-IL-5 antibodies
EA201992802A1 (ru) *	2017-05-26	2020-07-10	Глэксосмитклайн Интеллекчуал Проперти Дивелопмент Лимитед	Биофармацевтические композиции и связанные с ними способы
CN111065651B (zh)	2017-09-29	2023-07-14	江苏恒瑞医药股份有限公司	Il-5抗体、其抗原结合片段及医药用途
CN109942706A (zh) *	2017-12-21	2019-06-28	三生国健药业（上海）股份有限公司	结合人il-5的单克隆抗体、其制备方法和用途
WO2020119728A1 (zh) *	2018-12-12	2020-06-18	尚华科创投资管理（江苏）有限公司	抗人白细胞介素5(il-5)单克隆抗体及其应用
KR20210145187A (ko) *	2019-03-29	2021-12-01	지앙수 헨그루이 메디슨 컴퍼니 리미티드	Il-5에 대한 항체를 함유하는 약학적 조성물 및 이의 용도

Family Cites Families (12)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
GB8800397D0 (en) *	1988-01-08	1988-02-10	Sandoz Ltd	Improvements in/relating to organic compounds
US5096704A (en) *	1988-11-03	1992-03-17	Schering Corporation	Method of treating eosinophilia
EP0367596B1 (en) *	1988-11-03	1993-12-22	Schering Corporation	Antagonist to interleukin-5 for preventing or reducing eosinophilia
US5530101A (en) *	1988-12-28	1996-06-25	Protein Design Labs, Inc.	Humanized immunoglobulins
ZA929328B (en) *	1991-12-02	1993-07-20	Fluor Corp	Apparatus and method for economic use of excess compressed air when firing low caloric-value gas in a combustion gas turbine.
HUT67943A (en) *	1992-02-06	1995-05-29	Schering Corp	Design, cloning and expression of humanized monoclonal antibodies against human interleukin-5
JPH06141885A (ja) *	1992-11-05	1994-05-24	Chemo Sero Therapeut Res Inst	モノクローナル抗体
WO1995014040A1 (en) *	1993-11-19	1995-05-26	Baylor College Of Medicine	Monoclonal antibodies specific for human interleukin-5
GB9412230D0 (en) *	1994-06-17	1994-08-10	Celltech Ltd	Interleukin-5 specific recombiant antibodies
US5783184A (en) *	1994-12-23	1998-07-21	Smithkline Beecham Corporation	Method for treatment and diagnosis of IL-5 mediated disorders
US5693323A (en) *	1994-12-23	1997-12-02	Smithkline Beecham Corporation	Recombinant IL-5 antagonists useful in treatment of IL-5 mediated disorders
WO2001012646A1 (en) *	1999-08-19	2001-02-22	Smithkline Beecham Corporation	Sialoadhesin factor-1 agonist and antagonist antibodies

1995
- 1995-12-22 DK DK95944692T patent/DK0800536T3/da active
- 1995-12-22 WO PCT/US1995/017082 patent/WO1996021000A2/en active IP Right Grant
- 1995-12-22 AU AU47450/96A patent/AU708951B2/en not_active Expired
- 1995-12-22 ES ES95944692T patent/ES2277336T3/es not_active Expired - Lifetime
- 1995-12-22 HU HU9901120A patent/HU222992B1/hu active Protection Beyond IP Right Term
- 1995-12-22 MX MX9704779A patent/MX9704779A/es unknown
- 1995-12-22 PL PL95321088A patent/PL194312B1/pl unknown
- 1995-12-22 AT AT95944692T patent/ATE346867T1/de active
- 1995-12-22 BR BRPI9510499-2A patent/BR9510499B1/pt active IP Right Grant
- 1995-12-22 NZ NZ301916A patent/NZ301916A/xx not_active IP Right Cessation
- 1995-12-22 EP EP95944692A patent/EP0800536B1/en not_active Expired - Lifetime
- 1995-12-22 DE DE69535319T patent/DE69535319T2/de not_active Expired - Lifetime
- 1995-12-22 CZ CZ0196397A patent/CZ297045B6/cs not_active IP Right Cessation
- 1995-12-22 CA CA002208503A patent/CA2208503C/en not_active Expired - Lifetime
- 1995-12-22 US US08/637,647 patent/US6129913A/en not_active Expired - Lifetime
- 1995-12-22 JP JP52118996A patent/JP2001523083A/ja not_active Withdrawn
- 1995-12-22 CN CNB951977016A patent/CN100391977C/zh not_active Expired - Lifetime
1997
- 1997-06-20 NO NO19972913A patent/NO324181B1/no not_active IP Right Cessation
- 1997-06-23 FI FI972703A patent/FI119374B/fi not_active IP Right Cessation
1998
- 1998-04-09 HK HK98103015A patent/HK1003651A1/xx not_active IP Right Cessation
2007
- 2007-10-16 JP JP2007269236A patent/JP2008029355A/ja not_active Withdrawn
2015
- 2015-12-16 LU LU92912C patent/LU92912I2/xx unknown
- 2015-12-18 NO NO2015027C patent/NO2015027I2/no unknown
- 2015-12-18 NL NL300787C patent/NL300787I2/nl unknown

Also Published As

Publication number	Publication date
EP0800536B1 (en)	2006-11-29
ATE346867T1 (de)	2006-12-15
US6129913A (en)	2000-10-10
ES2277336T3 (es)	2007-07-01
NO972913L (no)	1997-08-19
EP0800536A4 (en)	2004-12-01
DE69535319D1 (de)	2007-01-11
NO2015027I2 (no)	2016-01-04
HU222992B1 (hu)	2004-01-28
NO2015027I1 (no)	2015-12-18
BR9510499B1 (pt)	2009-05-05
EP0800536A2 (en)	1997-10-15
CZ196397A3 (en)	1997-10-15
CZ297045B6 (cs)	2006-08-16
JP2008029355A (ja)	2008-02-14
AU708951B2 (en)	1999-08-19
DE69535319T2 (de)	2007-07-19
NL300787I1 (fi)	2016-04-05
NL300787I2 (fi)	2016-04-05
CA2208503A1 (en)	1996-07-11
WO1996021000A3 (en)	1996-09-06
PL321088A1 (en)	1997-11-24
CN100391977C (zh)	2008-06-04
DK0800536T3 (da)	2007-04-02
NZ301916A (en)	1999-05-28
FI119374B (fi)	2008-10-31
FI972703A0 (fi)	1997-06-23
BR9510499A (pt)	1999-03-30
AU4745096A (en)	1996-07-24
WO1996021000A2 (en)	1996-07-11
NO972913D0 (no)	1997-06-20
JP2001523083A (ja)	2001-11-20
MX9704779A (es)	1997-09-30
HK1003651A1 (en)	1998-11-06
CN1175263A (zh)	1998-03-04
LU92912I2 (fr)	2016-02-16
FI972703L (fi)	1997-08-22
PL194312B1 (pl)	2007-05-31
CA2208503C (en)	2009-12-01
HUT78055A (hu)	1999-07-28

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US7982005B2 (en)	2011-07-19	Recombinant IL-5 antagonists useful in treatment of IL-5 mediated disorders
JP5177444B2 (ja)	2013-04-03	Ｉｌ−５により媒介される疾病の治療に有用な組み換えｉｌ−５アンタゴニスト
JP4954104B2 (ja)	2012-06-13	Ｉｌ−５介在障害を治療および診断するための改良方法
CA2208503C (en)	2009-12-01	Recombinant il-5 antagonists useful in treatment of il-5 mediated disorders
EP1163271B1 (en)	2008-07-23	Recombinant il-18 antibodies and their use
EP1703893B1 (en)	2012-04-11	Novel anti-il 13 antibodies and uses thereof
EP0730609B1 (en)	2005-01-05	Recombinant il4 antibodies useful in treatment of il4 mediated disorders
WO1995001997A1 (en)	1995-01-19	RECOMBINANT AND HUMANIZED IL-1β ANTIBODIES FOR TREATMENT OF IL-1 MEDIATED INFLAMMATORY DISORDERS IN MAN
US7807793B2 (en)	2010-10-05	Recombinant IL4 antibodies useful in treatment of IL4 mediated disorders
NO341384B1 (no)	2017-10-30	IL-17 bindende antistoff for anvendelse ved behandling av inflammatorisk artritt og anvendelse av det IL-17 bindende antistoff for fremstilling av medikament for behandling av ankyloserende spondylitt.
EP1299421A2 (en)	2003-04-09	Antibodies to human mcp-1
AU2001283903A1 (en)	2002-04-11	Antibodies to human MCP-1
WO2014028748A1 (en)	2014-02-20	Interleukin 2 antibodies and antibody complexes
EP1708961B1 (en)	2011-03-09	Anti-ip-10 antibodies
KR100509993B1 (ko)	2006-02-28	Il-5 매개된 질환의 치료에 유용한 재조합 il-5 길항제
RO116809B1 (ro)	2001-06-29	Anticorp recombinant, monoclonal, compozitie farmaceutica si metoda de tratament cu aceasta

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