NO331551B1 - Isolert cytokin-zalpha11-ligand-polypeptid, isolert polynukleotid, ekspresjonsvektor, dyrket celle, fremgangsmate for fremstilling av peptidet, antistoff som binder til peptidet, anvendelse av preparat omfattende peptidet for fremstilling av medikament for behandling av sykdom, fremgangsmate for pavisning av peptidet i en biologisk prove samt polypeptidet for anvendelse innen medisin - Google Patents
Isolert cytokin-zalpha11-ligand-polypeptid, isolert polynukleotid, ekspresjonsvektor, dyrket celle, fremgangsmate for fremstilling av peptidet, antistoff som binder til peptidet, anvendelse av preparat omfattende peptidet for fremstilling av medikament for behandling av sykdom, fremgangsmate for pavisning av peptidet i en biologisk prove samt polypeptidet for anvendelse innen medisin Download PDFInfo
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- NO331551B1 NO331551B1 NO20014364A NO20014364A NO331551B1 NO 331551 B1 NO331551 B1 NO 331551B1 NO 20014364 A NO20014364 A NO 20014364A NO 20014364 A NO20014364 A NO 20014364A NO 331551 B1 NO331551 B1 NO 331551B1
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- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/55—Fusion polypeptide containing a fusion with a toxin, e.g. diphteria toxin
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- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Diabetes (AREA)
- Hematology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- External Artificial Organs (AREA)
- Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Applications Claiming Priority (4)
Application Number | Priority Date | Filing Date | Title |
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US26490899A | 1999-03-09 | 1999-03-09 | |
US26599299A | 1999-03-11 | 1999-03-11 | |
US14201399P | 1999-07-01 | 1999-07-01 | |
PCT/US2000/006067 WO2000053761A2 (en) | 1999-03-09 | 2000-03-09 | Human cytokine as ligand of the zalpha receptor and uses thereof |
Publications (3)
Publication Number | Publication Date |
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NO20014364D0 NO20014364D0 (no) | 2001-09-07 |
NO20014364L NO20014364L (no) | 2001-11-09 |
NO331551B1 true NO331551B1 (no) | 2012-01-23 |
Family
ID=27385745
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO20014364A NO331551B1 (no) | 1999-03-09 | 2001-09-07 | Isolert cytokin-zalpha11-ligand-polypeptid, isolert polynukleotid, ekspresjonsvektor, dyrket celle, fremgangsmate for fremstilling av peptidet, antistoff som binder til peptidet, anvendelse av preparat omfattende peptidet for fremstilling av medikament for behandling av sykdom, fremgangsmate for pavisning av peptidet i en biologisk prove samt polypeptidet for anvendelse innen medisin |
NO20111085A NO20111085L (no) | 1999-03-09 | 2011-07-29 | Isolert cytokin-zalphall-ligand-polypeptid, isolert Polynukleotid, ekspresjonsvektor, dyrket celle, fremgangsmate for fremstilling av peptidet, antistoff som binder til peptidet, anvendelse av preparat omfattende peptidet for fremstilling av medikament for behandling av sykdom, fremgangsmate for pavisning av peptidet i en biologisk prove samt polypeptidet for anvendelse innen medisin |
Family Applications After (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO20111085A NO20111085L (no) | 1999-03-09 | 2011-07-29 | Isolert cytokin-zalphall-ligand-polypeptid, isolert Polynukleotid, ekspresjonsvektor, dyrket celle, fremgangsmate for fremstilling av peptidet, antistoff som binder til peptidet, anvendelse av preparat omfattende peptidet for fremstilling av medikament for behandling av sykdom, fremgangsmate for pavisning av peptidet i en biologisk prove samt polypeptidet for anvendelse innen medisin |
Country Status (23)
Country | Link |
---|---|
EP (3) | EP2295577A3 (cs) |
JP (1) | JP4405686B2 (cs) |
KR (1) | KR100743640B1 (cs) |
CN (5) | CN102406937A (cs) |
AT (1) | ATE377076T1 (cs) |
AU (2) | AU777842B2 (cs) |
BR (1) | BR0008772B1 (cs) |
CA (1) | CA2366921C (cs) |
CZ (1) | CZ302921B6 (cs) |
DE (1) | DE60036930T2 (cs) |
DK (1) | DK1165791T3 (cs) |
ES (1) | ES2295019T3 (cs) |
HU (1) | HU229148B1 (cs) |
IL (5) | IL145288A0 (cs) |
MX (1) | MXPA01009074A (cs) |
NO (2) | NO331551B1 (cs) |
NZ (1) | NZ514708A (cs) |
PL (1) | PL207350B1 (cs) |
PT (1) | PT1165791E (cs) |
RU (1) | RU2346951C2 (cs) |
UA (1) | UA84387C2 (cs) |
WO (1) | WO2000053761A2 (cs) |
ZA (1) | ZA017370B (cs) |
Families Citing this family (36)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US7189400B2 (en) | 1998-03-17 | 2007-03-13 | Genetics Institute, Llc | Methods of treatment with antagonists of MU-1 |
US7198789B2 (en) | 1998-03-17 | 2007-04-03 | Genetics Institute, Llc | Methods and compositions for modulating interleukin-21 receptor activity |
US6057128A (en) | 1998-03-17 | 2000-05-02 | Genetics Institute, Inc. | MU-1, member of the cytokine receptor family |
CZ302921B6 (cs) * | 1999-03-09 | 2012-01-18 | Zymogenetics, Inc. | Izolovaný polypeptid, fúzní protein, polynukleotid, expresní vektor, hostitelská bunka, protilátka, zpusob prípravy proteinu, protilátky, množení hematopoetických bunek, redukce proliferace neoplastických T a B bunek, stimulace imunitní odpovedi u sa |
ES2629395T3 (es) * | 2001-10-04 | 2017-08-09 | Genetics Institute, Llc | Métodos y composiciones para modular la actividad de la interleucina-21 |
WO2003040313A2 (en) | 2001-11-05 | 2003-05-15 | Zymogenetics, Inc | Il-21 antagonists |
PT1531850E (pt) * | 2002-06-07 | 2012-05-07 | Zymogenetics Inc | Utilização de il-21 e anticorpo monoclonal para tratar cancros sólidos |
EP1553982A4 (en) | 2002-07-15 | 2008-03-26 | Wyeth Corp | METHOD AND COMPOSITIONS FOR MODULATING THE DEVELOPMENT AND FUNCTION OF T-HELPER CELLS (T sb H / sb) |
BR0315134A (pt) * | 2002-10-11 | 2005-08-16 | Novo Nordisk As | Usos de il-21 e de um polipeptìdeo de il-21 |
EP1731163A2 (en) * | 2002-10-11 | 2006-12-13 | Novo Nordisk A/S | Treatment of allergic conditions by use of IL 21 |
DE60330044D1 (de) * | 2002-12-13 | 2009-12-24 | Zymogenetics Inc | Il-21-produktion in prokaryontischen wirten |
US7495085B2 (en) | 2003-03-14 | 2009-02-24 | Wyeth | Antibodies against human or mouse IL-21 receptor |
CA2529520A1 (en) * | 2003-06-19 | 2004-12-29 | Centocor, Inc. | Interleukin-21 analogs |
DE602004031341D1 (de) | 2003-07-21 | 2011-03-24 | Transgene Sa | Multifunktionelle cytokine |
ATE500267T1 (de) | 2003-07-21 | 2011-03-15 | Transgene Sa | Multifunktionelle cytokine |
JP2007506789A (ja) * | 2003-09-25 | 2007-03-22 | ザイモジェネティクス, インコーポレイテッド | Il−21を用いた自己免疫疾患の治療方法 |
US20060228331A1 (en) | 2003-10-10 | 2006-10-12 | Novo Nordisk A/S | IL-21 Derivatives and variants |
DE602004029173D1 (de) * | 2003-10-10 | 2010-10-28 | Novo Nordisk As | Il-21-derivate |
EP2633866A3 (en) | 2003-10-17 | 2013-12-18 | Novo Nordisk A/S | Combination therapy |
EP1708737A2 (en) * | 2004-01-15 | 2006-10-11 | Novo Nordisk A/S | Use of interleukin-21 for the treatment of autoimmune diseases and allograft rejection |
MXPA06008209A (es) | 2004-01-21 | 2006-08-31 | Novo Nordisk As | Conjugacion de peptidos mediada por transglutaminasa. |
GT200600148A (es) | 2005-04-14 | 2006-11-22 | Metodos para el tratamiento y la prevencion de fibrosis | |
EP2360181B1 (en) | 2005-04-18 | 2013-09-18 | Novo Nordisk A/S | IL-21 variants |
EP1963369B1 (en) | 2005-11-28 | 2013-05-15 | Zymogenetics, Inc. | Il-21 antagonists |
US8475784B2 (en) | 2006-10-26 | 2013-07-02 | Novo Nordisk A/S | IL-21 variants |
JP2010512769A (ja) | 2006-12-21 | 2010-04-30 | ノヴォ ノルディスク アクティーゼルスカブ | Il−21受容体との結合が変化したインターロイキン−21変異体 |
ES2572231T3 (es) | 2007-12-07 | 2016-05-30 | Zymogenetics Inc | Anticuerpos monoclonales anti-IL-21 humana |
PE20100141A1 (es) | 2008-05-23 | 2010-02-22 | Wyeth Corp | Proteina de union al receptor de interleuquina 21 |
AU2009248812A1 (en) | 2008-05-23 | 2009-11-26 | Wyeth Llc | Methods of treatment utilizing binding proteins of the interleukin-21 receptor |
WO2010039533A2 (en) | 2008-09-23 | 2010-04-08 | Wyeth | Methods for predicting production of activating signals by cross-linked binding proteins |
CN102021196B (zh) * | 2009-11-20 | 2013-06-26 | 上海杰隆生物工程股份有限公司 | 毕赤酵母生产重组人白细胞介素21的方法 |
KR20150036186A (ko) | 2012-06-27 | 2015-04-07 | 러트거즈,더스테이트유니버시티오브뉴저지 | 유세포 측정법을 이용한 rna 측정에 의한 t-세포 활성화에 대한 신속한 검정 |
WO2015110930A1 (en) | 2014-01-24 | 2015-07-30 | Pfizer Inc. | Modified interleukin 21 receptor proteins |
EP2982693A1 (en) * | 2014-08-07 | 2016-02-10 | Affimed Therapeutics AG | CD3 binding domain |
US12012441B2 (en) | 2020-10-26 | 2024-06-18 | Neptune Biosciences Llc | Engineered human IL-21 cytokines and methods for using the same |
CN112662694A (zh) * | 2020-12-25 | 2021-04-16 | 康九生物科技(长春)有限公司 | 一种麦芽糖结合蛋白、麦芽糖结合蛋白表达载体、重组工程菌及其应用 |
Family Cites Families (47)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
IE54046B1 (en) | 1981-08-25 | 1989-05-24 | Celltech Ltd | Expression vectors |
US4579821A (en) | 1981-11-23 | 1986-04-01 | University Patents, Inc. | Control of DNA sequence transcription |
US4656134A (en) | 1982-01-11 | 1987-04-07 | Board Of Trustees Of Leland Stanford Jr. University | Gene amplification in eukaryotic cells |
US4486533A (en) | 1982-09-02 | 1984-12-04 | St. Louis University | Filamentous fungi functional replicating extrachromosomal element |
US4599311A (en) | 1982-08-13 | 1986-07-08 | Kawasaki Glenn H | Glycolytic promotersfor regulated protein expression: protease inhibitor |
US4977092A (en) | 1985-06-26 | 1990-12-11 | Amgen | Expression of exogenous polypeptides and polypeptide products including hepatitis B surface antigen in yeast cells |
US4601978A (en) | 1982-11-24 | 1986-07-22 | The Regents Of The University Of California | Mammalian metallothionein promoter system |
US4713339A (en) | 1983-01-19 | 1987-12-15 | Genentech, Inc. | Polycistronic expression vector construction |
US5139936A (en) | 1983-02-28 | 1992-08-18 | Collaborative Research, Inc. | Use of the GAL1 yeast promoter |
US4661454A (en) | 1983-02-28 | 1987-04-28 | Collaborative Research, Inc. | GAL1 yeast promoter linked to non galactokinase gene |
US4650764A (en) | 1983-04-12 | 1987-03-17 | Wisconsin Alumni Research Foundation | Helper cell |
US4870008A (en) | 1983-08-12 | 1989-09-26 | Chiron Corporation | Secretory expression in eukaryotes |
US4931373A (en) | 1984-05-25 | 1990-06-05 | Zymogenetics, Inc. | Stable DNA constructs for expression of α-1 antitrypsin |
US4766073A (en) | 1985-02-25 | 1988-08-23 | Zymogenetics Inc. | Expression of biologically active PDGF analogs in eucaryotic cells |
ATE54167T1 (de) | 1984-12-06 | 1990-07-15 | Fina Research | Promotoren fuer die expression von fremden genen in hefe, plasmide, die diese promotoren enthalten, sowie deren verwendung zur herstellung von polypeptiden. |
US4683202A (en) | 1985-03-28 | 1987-07-28 | Cetus Corporation | Process for amplifying nucleic acid sequences |
GR860984B (en) | 1985-04-17 | 1986-08-18 | Zymogenetics Inc | Expression of factor vii and ix activities in mammalian cells |
US4882279A (en) | 1985-10-25 | 1989-11-21 | Phillips Petroleum Company | Site selective genomic modification of yeast of the genus pichia |
US4935349A (en) | 1986-01-17 | 1990-06-19 | Zymogenetics, Inc. | Expression of higher eucaryotic genes in aspergillus |
GB8611832D0 (en) | 1986-05-15 | 1986-06-25 | Holland I B | Polypeptide |
US4980289A (en) | 1987-04-27 | 1990-12-25 | Wisconsin Alumni Research Foundation | Promoter deficient retroviral vector |
US5063154A (en) | 1987-06-24 | 1991-11-05 | Whitehead Institute For Biomedical Research | Pheromone - inducible yeast promoter |
ES2092468T3 (es) | 1988-01-22 | 1996-12-01 | Zymogenetics Inc | Metodos para producir analogos de receptores secretados. |
US5567584A (en) | 1988-01-22 | 1996-10-22 | Zymogenetics, Inc. | Methods of using biologically active dimerized polypeptide fusions to detect PDGF |
US4956288A (en) | 1988-04-22 | 1990-09-11 | Biogen, Inc. | Method for producing cells containing stably integrated foreign DNA at a high copy number, the cells produced by this method, and the use of these cells to produce the polypeptides coded for by the foreign DNA |
US5037743A (en) | 1988-08-05 | 1991-08-06 | Zymogenetics, Inc. | BAR1 secretion signal |
US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
US5162228A (en) | 1988-12-28 | 1992-11-10 | Takeda Chemical Industries, Ltd. | Gylceraldehyde-3-phosphate dehydrogenase gene and promoter |
US5124263A (en) | 1989-01-12 | 1992-06-23 | Wisconsin Alumni Research Foundation | Recombination resistant retroviral helper cell and products produced thereby |
US5399346A (en) | 1989-06-14 | 1995-03-21 | The United States Of America As Represented By The Department Of Health And Human Services | Gene therapy |
US5162222A (en) | 1989-07-07 | 1992-11-10 | Guarino Linda A | Use of baculovirus early promoters for expression of foreign genes in stably transformed insect cells or recombinant baculoviruses |
IL99552A0 (en) | 1990-09-28 | 1992-08-18 | Ixsys Inc | Compositions containing procaryotic cells,a kit for the preparation of vectors useful for the coexpression of two or more dna sequences and methods for the use thereof |
US5298418A (en) | 1991-09-16 | 1994-03-29 | Boyce Thompson Institute For Plant Research, Inc. | Cell line isolated from larval midgut tissue of Trichoplusia ni |
US5641670A (en) | 1991-11-05 | 1997-06-24 | Transkaryotic Therapies, Inc. | Protein production and protein delivery |
WO1994006463A1 (en) | 1992-09-14 | 1994-03-31 | Pfizer Inc | Immortalized cells and uses therefor |
WO1995007358A1 (en) | 1993-07-30 | 1995-03-16 | University Of Medicine & Dentistry Of New Jersey | Efficient gene transfer into primary lymphocytes |
RU2220979C2 (ru) * | 1993-08-12 | 2004-01-10 | Иммьюнекс Корпорейшн | ПОЛИПЕПТИД ЛИГАНДА flt3 (ВАРИАНТЫ), ПОЛИНУКЛЕОТИД(ВАРИАНТЫ), ЭКСПРЕССИРУЮЩИЙ ВЕКТОР(ВАРИАНТЫ), ЛИНИЯ КЛЕТОК СНО (ВАРИАНТЫ), СПОСОБ ПРОДУЦИРОВАНИЯ ПОЛИПЕПТИДА ЛИГАНДА flt3 (ВАРИАНТЫ), ФАРМАЦЕВТИЧЕСКАЯ КОМПОЗИЦИЯ (ВАРИАНТЫ) |
US6117679A (en) | 1994-02-17 | 2000-09-12 | Maxygen, Inc. | Methods for generating polynucleotides having desired characteristics by iterative selection and recombination |
US5795966A (en) * | 1995-02-22 | 1998-08-18 | Immunex Corp | Antagonists of interleukin-15 |
EP0889966A1 (en) | 1995-11-09 | 1999-01-13 | ZymoGenetics, Inc. | Compositions and methods for producing heterologous polypeptides in pichia methanolica |
WO1998002536A2 (en) | 1996-07-17 | 1998-01-22 | Zymogenetics, Inc. | Preparation of pichia methanolica auxotrophic mutants |
IL128073A0 (en) | 1996-07-17 | 1999-11-30 | Zymogenetics Inc | Transformation of pichia methanolica |
PT1500329E (pt) | 1996-12-03 | 2012-06-18 | Amgen Fremont Inc | Anticorpos humanos que se ligam especificamente ao tnf alfa humano |
IL122818A0 (en) * | 1997-07-10 | 1998-08-16 | Yeda Res & Dev | Chimeric interleukin-6 soluble receptor/ligand protein analogs thereof and uses thereof |
US6057128A (en) * | 1998-03-17 | 2000-05-02 | Genetics Institute, Inc. | MU-1, member of the cytokine receptor family |
CZ302921B6 (cs) * | 1999-03-09 | 2012-01-18 | Zymogenetics, Inc. | Izolovaný polypeptid, fúzní protein, polynukleotid, expresní vektor, hostitelská bunka, protilátka, zpusob prípravy proteinu, protilátky, množení hematopoetických bunek, redukce proliferace neoplastických T a B bunek, stimulace imunitní odpovedi u sa |
US9418201B1 (en) | 2015-11-19 | 2016-08-16 | International Business Machines Corporation | Integration of functional analysis and common path pessimism removal in static timing analysis |
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2000
- 2000-03-09 CZ CZ20013184A patent/CZ302921B6/cs not_active IP Right Cessation
- 2000-03-09 IL IL14528800A patent/IL145288A0/xx unknown
- 2000-03-09 BR BRPI0008772-6A patent/BR0008772B1/pt not_active IP Right Cessation
- 2000-03-09 KR KR1020017011499A patent/KR100743640B1/ko not_active Expired - Fee Related
- 2000-03-09 EP EP20100185147 patent/EP2295577A3/en not_active Withdrawn
- 2000-03-09 DE DE60036930T patent/DE60036930T2/de not_active Expired - Lifetime
- 2000-03-09 CN CN2011103037822A patent/CN102406937A/zh active Pending
- 2000-03-09 UA UA2001106769A patent/UA84387C2/ru unknown
- 2000-03-09 NZ NZ514708A patent/NZ514708A/en not_active IP Right Cessation
- 2000-03-09 ES ES00916164T patent/ES2295019T3/es not_active Expired - Lifetime
- 2000-03-09 EP EP00916164A patent/EP1165791B1/en not_active Expired - Lifetime
- 2000-03-09 AT AT00916164T patent/ATE377076T1/de active
- 2000-03-09 DK DK00916164T patent/DK1165791T3/da active
- 2000-03-09 CN CNB008068747A patent/CN100500846C/zh not_active Expired - Fee Related
- 2000-03-09 JP JP2000603382A patent/JP4405686B2/ja not_active Expired - Fee Related
- 2000-03-09 CN CN2006101031515A patent/CN1927883B/zh not_active Expired - Fee Related
- 2000-03-09 CA CA2366921A patent/CA2366921C/en not_active Expired - Fee Related
- 2000-03-09 HU HU0200418A patent/HU229148B1/hu not_active IP Right Cessation
- 2000-03-09 MX MXPA01009074A patent/MXPA01009074A/es active IP Right Grant
- 2000-03-09 PT PT00916164T patent/PT1165791E/pt unknown
- 2000-03-09 AU AU37312/00A patent/AU777842B2/en not_active Ceased
- 2000-03-09 RU RU2004126135/13A patent/RU2346951C2/ru not_active IP Right Cessation
- 2000-03-09 PL PL351160A patent/PL207350B1/pl unknown
- 2000-03-09 CN CNA2005101141968A patent/CN1827639A/zh active Pending
- 2000-03-09 CN CN2009101354816A patent/CN101575377B/zh not_active Expired - Fee Related
- 2000-03-09 EP EP07017344A patent/EP1881070B1/en not_active Expired - Lifetime
- 2000-03-09 WO PCT/US2000/006067 patent/WO2000053761A2/en active Application Filing
-
2001
- 2001-09-05 IL IL145288A patent/IL145288A/en not_active IP Right Cessation
- 2001-09-06 ZA ZA2001/07370A patent/ZA017370B/en unknown
- 2001-09-07 NO NO20014364A patent/NO331551B1/no not_active IP Right Cessation
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2005
- 2005-01-20 AU AU2005200240A patent/AU2005200240A1/en not_active Abandoned
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2008
- 2008-12-04 IL IL195713A patent/IL195713A/en not_active IP Right Cessation
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2010
- 2010-08-04 IL IL207403A patent/IL207403A/en not_active IP Right Cessation
- 2010-08-05 IL IL207424A patent/IL207424A/en not_active IP Right Cessation
-
2011
- 2011-07-29 NO NO20111085A patent/NO20111085L/no unknown
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