NO330538B1 - Anvendelse av hydrofob ladningsinduksjonskromatografi for fremstilling av renset IL-18-bindende protein samt fremgangsmate for fremstilling av renset IL -18-bindende protein - Google Patents

Anvendelse av hydrofob ladningsinduksjonskromatografi for fremstilling av renset IL-18-bindende protein samt fremgangsmate for fremstilling av renset IL -18-bindende protein Download PDF

Info

Publication number: NO330538B1
Authority: NO; Norway
Prior art keywords: chromatography; column; purified; resin; hydrophobic
Prior art date: 2003-11-05

Application number

NO20062545A

Other languages

English (en)

Norwegian (no)

Other versions

NO20062545L (no

Inventor

Mara Rossi

Thierry Ziegler

Laure Valognes

Original Assignee

Ares Trading Sa

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.)

2003-11-05

Filing date

2006-06-02

Publication date

2011-05-09

2006-06-02 Application filed by Ares Trading Sa filed Critical Ares Trading Sa

2006-08-03 Publication of NO20062545L publication Critical patent/NO20062545L/no

2011-05-09 Publication of NO330538B1 publication Critical patent/NO330538B1/no

Links

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Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/715—Receptors; Cell surface antigens; Cell surface determinants for cytokines; for lymphokines; for interferons
- C07K14/7155—Receptors; Cell surface antigens; Cell surface determinants for cytokines; for lymphokines; for interferons for interleukins [IL]

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Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Organic Chemistry (AREA)
Biochemistry (AREA)
Genetics & Genomics (AREA)
Gastroenterology & Hepatology (AREA)
Toxicology (AREA)
Immunology (AREA)
Biophysics (AREA)
General Health & Medical Sciences (AREA)
Zoology (AREA)
Medicinal Chemistry (AREA)
Molecular Biology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Cell Biology (AREA)
Peptides Or Proteins (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)

NO20062545A 2003-11-05 2006-06-02 Anvendelse av hydrofob ladningsinduksjonskromatografi for fremstilling av renset IL-18-bindende protein samt fremgangsmate for fremstilling av renset IL -18-bindende protein NO330538B1 (no)

Applications Claiming Priority (3)

Application Number	Priority Date	Filing Date	Title
US51744703P	2003-11-05	2003-11-05
EP03104092		2003-11-05
PCT/EP2004/052807 WO2005049649A1 (fr)	2003-11-05	2004-11-04	Procede de purification de la proteine de liaison il-18

Publications (2)

Publication Number	Publication Date
NO20062545L NO20062545L (no)	2006-08-03
NO330538B1 true NO330538B1 (no)	2011-05-09

Family

ID=34924126

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
NO20062545A NO330538B1 (no)	2003-11-05	2006-06-02	Anvendelse av hydrofob ladningsinduksjonskromatografi for fremstilling av renset IL-18-bindende protein samt fremgangsmate for fremstilling av renset IL -18-bindende protein

Country Status (19)

Country	Link
US (1)	US7820800B2 (fr)
EP (1)	EP1689777B1 (fr)
JP (1)	JP4741504B2 (fr)
AT (1)	ATE360647T1 (fr)
AU (1)	AU2004291341B2 (fr)
CA (1)	CA2544146C (fr)
CY (1)	CY1106683T1 (fr)
DE (1)	DE602004006157T2 (fr)
DK (1)	DK1689777T3 (fr)
ES (1)	ES2285543T3 (fr)
HR (1)	HRP20070196T3 (fr)
IL (1)	IL175431A (fr)
ME (1)	ME01198B (fr)
NO (1)	NO330538B1 (fr)
PL (1)	PL1689777T3 (fr)
PT (1)	PT1689777E (fr)
RS (1)	RS50516B (fr)
SI (1)	SI1689777T1 (fr)
WO (1)	WO2005049649A1 (fr)

Families Citing this family (32)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
ATE399872T1 (de)	2003-03-11	2008-07-15	Serono Lab	Expressionvektoren, die den promotor des ie2-gens des maus cytomegalovirus enthalten
DK1622939T3 (da) *	2003-05-13	2012-04-10	Merck Serono Sa	Aktive varianter af det IL-18-bindende protein og medicinske anvendelser deraf
ATE484591T1 (de) *	2003-10-21	2010-10-15	Merck Serono Sa	Minimale dna sequenz, die als chromatin-isolator wirkt, und deren verwendung für die protein- expression
US7968684B2 (en)	2003-11-12	2011-06-28	Abbott Laboratories	IL-18 binding proteins
DE602005002829T2 (de) *	2004-03-01	2008-07-10	Ares Trading S.A.	Verwendung eines serumfreien zellkulturmediums zur produktion von il-18bp in säugerzellen
AU2005259269B2 (en)	2004-06-29	2010-12-09	Ares Trading S.A.	Process for the purification of IL-18 binding protein
US8129508B2 (en)	2005-04-11	2012-03-06	Medarex, Inc.	Protein purification using HCIC and ion exchange chromatography
ES2385639T3 (es)	2005-06-03	2012-07-27	Ares Trading S.A.	Producción de una proteína de unión a IL-18 recombinante
AU2006256763B2 (en) *	2005-06-10	2012-08-02	Ares Trading S.A.	Process for the purification of IL-18 binding protein
CN101874042B9 (zh)	2007-09-26	2019-01-01	中外制药株式会社	利用cdr的氨基酸取代来改变抗体等电点的方法
AU2009204998B2 (en)	2008-01-18	2014-03-27	F. Hoffmann-La Roche Ag	Purification of non-glycosylated proteins
EP2275443B1 (fr)	2008-04-11	2015-12-02	Chugai Seiyaku Kabushiki Kaisha	Molécule de liaison à l antigène capable de se lier à deux molécules d antigène ou plus de manière répétée
TWI440469B (zh)	2008-09-26	2014-06-11	Chugai Pharmaceutical Co Ltd	Improved antibody molecules
WO2011156369A2 (fr) *	2010-06-07	2011-12-15	Dr. Reddy's Laboratories Ltd.	Purification de cytokines modifiées
TWI654204B (zh)	2010-11-30	2019-03-21	Chugai Seiyaku Kabushiki Kaisha	具有鈣依存性的抗原結合能力之抗體
CA2827923C (fr)	2011-02-25	2021-11-23	Chugai Seiyaku Kabushiki Kaisha	Anticorps fc specifique de fcgriib
JP6147726B2 (ja)	2011-03-29	2017-06-14	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ＧｌａｘｏＳｍｉｔｈＫｌｉｎｅＬＬＣ	タンパク質精製のためのバッファー系
TW201817744A (zh)	2011-09-30	2018-05-16	日商中外製藥股份有限公司	具有促進抗原清除之ＦｃＲｎ結合域的治療性抗原結合分子
US20150050269A1 (en)	2011-09-30	2015-02-19	Chugai Seiyaku Kabushiki Kaisha	Antigen-binding molecule promoting disappearance of antigens having plurality of biological activities
CA3233142A1 (fr)	2011-11-30	2013-06-06	Chugai Seiyaku Kabushiki Kaisha	Support contenant des medicaments dans une cellule pour former un complexe immunitaire
WO2013125667A1 (fr)	2012-02-24	2013-08-29	中外製薬株式会社	MOLÉCULE DE LIAISON D'ANTIGÈNE DESTINÉE À FAVORISER LA DISPARITION D'ANTIGÈNE VIA LE RÉCEPTEUR FcγRIIB
TWI636062B (zh)	2013-04-02	2018-09-21	中外製藥股份有限公司	Fc region variant
SI3116891T1 (sl) *	2014-03-10	2020-07-31	Richter Gedeon Nyrt.	Čiščenje imunoglobulina z uporabo predčistilnih stopenj
CN107001411B (zh) *	2014-12-15	2021-07-23	默克专利股份公司	从粗溶液捕获靶分子
NZ730607A (en)	2014-12-19	2022-07-01	Chugai Pharmaceutical Co Ltd	Anti-myostatin antibodies, polypeptides containing variant fc regions, and methods of use
SG10201710322VA (en)	2014-12-19	2018-02-27	Chugai Pharmaceutical Co Ltd	Anti-c5 antibodies and methods of use
WO2016125495A1 (fr)	2015-02-05	2016-08-11	Chugai Seiyaku Kabushiki Kaisha	Anticorps comprenant un domaine se liant à l'antigène dépendant de la concentration d'ions, variants de la région fc, anticorps se liant à l'il-8, et leurs utilisations
TWI873632B (zh)	2015-02-27	2025-02-21	日商中外製藥股份有限公司	Il-6受體抗體用於製備醫藥組成物的用途
WO2017110981A1 (fr)	2015-12-25	2017-06-29	Chugai Seiyaku Kabushiki Kaisha	Anticorps anti-myostatine et procédés d'utilisation
BR112019001902A2 (pt)	2016-08-05	2019-07-09	Chugai Seiyaku Kabushiki Kaisha	composição para profilaxia ou tratamento de doenças relacionadas à il-8
JP7191833B2 (ja)	2017-01-30	2022-12-19	中外製薬株式会社	抗スクレロスチン抗体およびその使用
US11851486B2 (en)	2017-05-02	2023-12-26	National Center Of Neurology And Psychiatry	Method for predicting and evaluating therapeutic effect in diseases related to IL-6 and neutrophils

Family Cites Families (14)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
IL121860A0 (en) *	1997-08-14	1998-02-22	Yeda Res & Dev	Interleukin-18 binding proteins their preparation and use
CA2340579A1 (fr) *	1998-09-01	2000-03-09	Kabushiki Kaisha Hayashibara Seibutsu Kagaku Kenkyujo	Proteine de liaison de l'interleukine 18
JP4216950B2 (ja) *	1998-09-01	2009-01-28	株式会社林原生物化学研究所	インターロイキン−１８結合蛋白質
US20020052475A1 (en) *	2000-07-20	2002-05-02	Schering Ag	High affinity soluble interleukin-18 receptor
DK1392830T3 (da) *	2001-03-08	2006-05-08	Ares Trading Sa	Interleukin-18 mutanter, deres fremstilling og anvendelse
CA2451955C (fr) *	2001-06-26	2015-09-29	Abgenix, Inc.	Anticorps opgl
EP1495055B1 (fr) *	2002-04-18	2013-08-14	Genencor International, Inc.	Production d'anticorps fonctionnels dans des champignons filamenteux
ATE399872T1 (de)	2003-03-11	2008-07-15	Serono Lab	Expressionvektoren, die den promotor des ie2-gens des maus cytomegalovirus enthalten
DK1622939T3 (da)	2003-05-13	2012-04-10	Merck Serono Sa	Aktive varianter af det IL-18-bindende protein og medicinske anvendelser deraf
ATE484591T1 (de)	2003-10-21	2010-10-15	Merck Serono Sa	Minimale dna sequenz, die als chromatin-isolator wirkt, und deren verwendung für die protein- expression
DE602005002829T2 (de)	2004-03-01	2008-07-10	Ares Trading S.A.	Verwendung eines serumfreien zellkulturmediums zur produktion von il-18bp in säugerzellen
AU2005259269B2 (en)	2004-06-29	2010-12-09	Ares Trading S.A.	Process for the purification of IL-18 binding protein
ES2385639T3 (es) *	2005-06-03	2012-07-27	Ares Trading S.A.	Producción de una proteína de unión a IL-18 recombinante
AU2006256763B2 (en)	2005-06-10	2012-08-02	Ares Trading S.A.	Process for the purification of IL-18 binding protein

2004
- 2004-11-04 ES ES04798163T patent/ES2285543T3/es not_active Expired - Lifetime
- 2004-11-04 EP EP04798163A patent/EP1689777B1/fr not_active Expired - Lifetime
- 2004-11-04 CA CA2544146A patent/CA2544146C/fr not_active Expired - Lifetime
- 2004-11-04 AU AU2004291341A patent/AU2004291341B2/en not_active Expired
- 2004-11-04 HR HR20070196T patent/HRP20070196T3/xx unknown
- 2004-11-04 JP JP2006537319A patent/JP4741504B2/ja not_active Expired - Lifetime
- 2004-11-04 PL PL04798163T patent/PL1689777T3/pl unknown
- 2004-11-04 PT PT04798163T patent/PT1689777E/pt unknown
- 2004-11-04 ME MEP-2008-580A patent/ME01198B/fr unknown
- 2004-11-04 US US10/576,372 patent/US7820800B2/en not_active Expired - Lifetime
- 2004-11-04 DK DK04798163T patent/DK1689777T3/da active
- 2004-11-04 SI SI200430322T patent/SI1689777T1/sl unknown
- 2004-11-04 DE DE602004006157T patent/DE602004006157T2/de not_active Expired - Lifetime
- 2004-11-04 RS RSP-2007/0216A patent/RS50516B/sr unknown
- 2004-11-04 WO PCT/EP2004/052807 patent/WO2005049649A1/fr not_active Ceased
- 2004-11-04 AT AT04798163T patent/ATE360647T1/de active
2006
- 2006-05-04 IL IL175431A patent/IL175431A/en active IP Right Grant
- 2006-06-02 NO NO20062545A patent/NO330538B1/no unknown
2007
- 2007-06-28 CY CY20071100852T patent/CY1106683T1/el unknown

Also Published As

Publication number	Publication date
EP1689777A1 (fr)	2006-08-16
AU2004291341A1 (en)	2005-06-02
US20070037734A1 (en)	2007-02-15
DK1689777T3 (da)	2007-06-11
IL175431A (en)	2011-02-28
CA2544146C (fr)	2012-10-02
ATE360647T1 (de)	2007-05-15
PT1689777E (pt)	2007-05-31
DE602004006157D1 (de)	2007-06-06
ES2285543T3 (es)	2007-11-16
CY1106683T1 (el)	2012-05-23
US7820800B2 (en)	2010-10-26
IL175431A0 (en)	2006-09-05
PL1689777T3 (pl)	2007-09-28
ME01198B (fr)	2013-03-20
AU2004291341B2 (en)	2010-08-05
RS50516B (sr)	2010-05-07
SI1689777T1 (sl)	2007-08-31
CA2544146A1 (fr)	2005-06-02
NO20062545L (no)	2006-08-03
WO2005049649A1 (fr)	2005-06-02
JP4741504B2 (ja)	2011-08-03
HRP20070196T3 (hr)	2007-06-30
JP2007533651A (ja)	2007-11-22
EP1689777B1 (fr)	2007-04-25
DE602004006157T2 (de)	2008-01-03

Publication	Publication Date	Title
US7820800B2 (en)	2010-10-26	Process for the purification of IL-18 binding protein
JP6913066B2 (ja)	2021-08-04	高純度および優れた収率の正確に折り畳まれたエタネルセプト
NO331712B1 (no)	2012-03-05	Fremgangsmate for rensing av IL-18 BP samt anvendelse av et vandig tofasesystem for rensing eller innfanging av IL-18BP
NO340957B1 (no)	2017-07-31	Anvendelse av IL-18 bindende protein samt fremgangsmåte for rensing av proteinet