UA82177C2 - Полипептиды фактора коагуляции vii человека - Google Patents
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Abstract
Заявленное изобретение относится к новым вариантам фактора VII коагуляции человека, имеющим коагуляционную активность, а также полинуклеотидным конструктам, которые кодируют такие варианты векторов и клеток-хозяев, которые содержат и экспрессируют полинуклеотид, фармацевтическим композициям, применению.
Applications Claiming Priority (2)
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DKPA200101413 | 2001-09-27 | ||
PCT/DK2002/000635 WO2003027147A2 (en) | 2001-09-27 | 2002-09-26 | Human coagulation factor vii polypeptides |
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UA82177C2 true UA82177C2 (ru) | 2008-03-25 |
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UA2004031982A UA82177C2 (ru) | 2001-09-27 | 2002-09-26 | Полипептиды фактора коагуляции vii человека |
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EP (1) | EP1432794B1 (ru) |
JP (1) | JP4537059B2 (ru) |
KR (1) | KR20040039444A (ru) |
CN (1) | CN1602354A (ru) |
AT (1) | ATE532858T1 (ru) |
AU (1) | AU2002333211B2 (ru) |
BR (1) | BR0212818A (ru) |
CA (1) | CA2461003A1 (ru) |
CZ (1) | CZ2004427A3 (ru) |
ES (1) | ES2376694T3 (ru) |
HU (1) | HUP0500060A3 (ru) |
IL (1) | IL160897A0 (ru) |
MX (1) | MXPA04002833A (ru) |
NO (1) | NO20041700L (ru) |
PL (1) | PL368619A1 (ru) |
RU (1) | RU2325401C2 (ru) |
UA (1) | UA82177C2 (ru) |
WO (1) | WO2003027147A2 (ru) |
ZA (1) | ZA200402262B (ru) |
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US6747003B1 (en) | 1997-10-23 | 2004-06-08 | Regents Of The University Of Minnesota | Modified vitamin K-dependent polypeptides |
US7247708B2 (en) | 1997-10-23 | 2007-07-24 | Regents Of The University Of Minnesota | Modified vitamin K-dependent polypeptides |
US7812132B2 (en) | 2000-04-28 | 2010-10-12 | Regents Of The University Of Minnesota | Modified vitamin K-dependent polypeptides |
US7220837B1 (en) | 2000-04-28 | 2007-05-22 | Regents Of The University Of Minnesota | Modified vitamin K-dependent polypeptides |
US6905683B2 (en) | 2000-05-03 | 2005-06-14 | Novo Nordisk Healthcare A/G | Human coagulation factor VII variants |
US20030211094A1 (en) | 2001-06-26 | 2003-11-13 | Nelsestuen Gary L. | High molecular weight derivatives of vitamin k-dependent polypeptides |
KR100882482B1 (ko) | 2000-09-13 | 2009-02-06 | 노보 노르디스크 헬스 케어 악티엔게젤샤프트 | 사람 응고 인자 vii 변이체 |
AU2002218029A1 (en) | 2000-11-09 | 2002-05-21 | The Scripps Research Institute | Modified factor viia |
US7052868B2 (en) | 2001-09-27 | 2006-05-30 | Novo Nordisk Healthcare A/G | Human coagulation factor VII polypeptides |
US6960657B2 (en) | 2001-11-02 | 2005-11-01 | Novo Nordisk Healthcare A/G | Human coagulation factor VII polypeptides |
AU2003221469A1 (en) | 2002-04-30 | 2003-11-17 | Bayer Healthcare Llc | FACTOR VII OR VIIa POLYPEPTIDE VARIANTS |
WO2004000366A1 (en) | 2002-06-21 | 2003-12-31 | Novo Nordisk Health Care Ag | Pegylated factor vii glycoforms |
WO2004029090A1 (en) * | 2002-09-25 | 2004-04-08 | Novo Nordisk Health Care Ag | Human coagulation factor vii polypeptides |
US6911323B2 (en) | 2002-09-25 | 2005-06-28 | Novo Nordisk Healthcare A/G | Human coagulation factor VII polypeptides |
AU2004221761B2 (en) | 2003-03-20 | 2010-01-07 | Bayer Healthcare Llc | FVII or FVIIa variants |
WO2006127896A2 (en) | 2005-05-25 | 2006-11-30 | Neose Technologies, Inc. | Glycopegylated factor ix |
US8791070B2 (en) | 2003-04-09 | 2014-07-29 | Novo Nordisk A/S | Glycopegylated factor IX |
EP1646398A2 (en) * | 2003-06-13 | 2006-04-19 | Novo Nordisk Health Care AG | Formulations comprising factor viia and a factor vii related polypeptide |
NZ573412A (en) | 2003-06-19 | 2010-09-30 | Maxygen Holdings Ltd | Factor VII or VIIa Gla domain variants |
JP4824559B2 (ja) | 2003-09-09 | 2011-11-30 | ノボ ノルディスク ヘルス ケア アクチェンゲゼルシャフト | 凝固因子viiポリペプチド |
EP1673453A2 (en) | 2003-10-07 | 2006-06-28 | Novo Nordisk Health Care AG | Hybrid molecules having factor vii/viia activity |
EP3594222B1 (en) | 2003-12-01 | 2022-08-03 | Novo Nordisk Health Care AG | Virus filtration of liquid factor vii compositions |
US20060040856A1 (en) | 2003-12-03 | 2006-02-23 | Neose Technologies, Inc. | Glycopegylated factor IX |
JP2007522805A (ja) * | 2004-02-03 | 2007-08-16 | ノボ ノルディスク ヘルス ケア アクチェンゲゼルシャフト | 新規化合物 |
US20060019893A1 (en) * | 2004-07-02 | 2006-01-26 | Genentech, Inc. | Factor VIIa variants |
KR101364001B1 (ko) * | 2004-12-23 | 2014-02-17 | 노보 노르디스크 헬스 케어 악티엔게젤샤프트 | 관심있는 비타민 k-의존성 단백질을 포함한 조성물 중의단백질 오염물질의 양의 감소 |
EP1893632B1 (en) | 2005-06-17 | 2015-08-12 | Novo Nordisk Health Care AG | Selective reduction and derivatization of engineered factor vii proteins comprising at least one non-native cysteine |
ES2397851T3 (es) | 2005-07-13 | 2013-03-11 | Novo Nordisk Health Care Ag | Células de inactivación proteínica de la célula huésped para la producción de proteínas terapéuticas |
ES2515915T3 (es) | 2005-09-01 | 2014-10-30 | Novo Nordisk Health Care Ag | Purificación de los polipéptidos del Factor VII mediante cromatografía de interacción hidrofóbica |
WO2007031559A2 (en) | 2005-09-14 | 2007-03-22 | Novo Nordisk Health Care Ag | Human coagulation factor vii polypeptides |
ES2353084T3 (es) * | 2006-04-07 | 2011-02-25 | Novo Nordisk Health Care Ag | Complejo covalente de factor vii y factor tisular. |
JP5570809B2 (ja) | 2006-09-01 | 2014-08-13 | ノボ ノルディスク ヘルス ケア アーゲー | 修飾タンパク質 |
EP1952822A1 (en) * | 2007-01-26 | 2008-08-06 | Novo Nordisk A/S | Factor VII polypeptides with increased affinity to platelets |
NZ579985A (en) | 2007-04-13 | 2012-02-24 | Catalyst Biosciences Inc | Modified factor vii polypetides and uses thereof |
US9493499B2 (en) | 2007-06-12 | 2016-11-15 | Novo Nordisk A/S | Process for the production of purified cytidinemonophosphate-sialic acid-polyalkylene oxide (CMP-SA-PEG) as modified nucleotide sugars via anion exchange chromatography |
EP2574676B1 (en) | 2007-12-27 | 2017-08-30 | Baxalta GmbH | Cell culture processes |
TWI538916B (zh) | 2008-04-11 | 2016-06-21 | 介控生化科技公司 | 經修飾的因子vii多肽和其用途 |
JP2013533871A (ja) | 2010-06-30 | 2013-08-29 | ノヴォ ノルディスク アー/エス | 組織因子経路インヒビターに特異的に結合することが可能な抗体 |
US20130337537A1 (en) | 2011-03-02 | 2013-12-19 | Novo Nordisk A/S | Coagulation factor-targeting to tlt-1 on activated platelets |
EP3527218A1 (en) | 2011-06-10 | 2019-08-21 | Bioverativ Therapeutics Inc. | Pro-coagulant compounds and methods of use thereof |
CN104717973A (zh) | 2012-10-10 | 2015-06-17 | 诺和诺德保健Ag(股份有限公司) | 因子vii多肽的液体药物组合物 |
CN109385443B (zh) * | 2017-08-07 | 2022-08-02 | 北京睿诚海汇健康科技有限公司 | 生菜作为宿主在表达凝血因子中的应用 |
EP3833381B1 (en) | 2019-08-15 | 2022-08-03 | Catalyst Biosciences, Inc. | Modified factor vii polypeptides for subcutaneous administration |
Family Cites Families (41)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4203570A (en) | 1978-08-23 | 1980-05-20 | The Western States Machine Company | Power-operated loading gate for centrifugal machines incorporating an auxiliary drive device |
US4873191A (en) | 1981-06-12 | 1989-10-10 | Ohio University | Genetic transformation of zygotes |
US4456591A (en) | 1981-06-25 | 1984-06-26 | Baxter Travenol Laboratories, Inc. | Therapeutic method for activating factor VII |
US4546082A (en) | 1982-06-17 | 1985-10-08 | Regents Of The Univ. Of California | E. coli/Saccharomyces cerevisiae plasmid cloning vector containing the alpha-factor gene for secretion and processing of hybrid proteins |
US4599311A (en) | 1982-08-13 | 1986-07-08 | Kawasaki Glenn H | Glycolytic promotersfor regulated protein expression: protease inhibitor |
US4501728A (en) | 1983-01-06 | 1985-02-26 | Technology Unlimited, Inc. | Masking of liposomes from RES recognition |
US4713339A (en) | 1983-01-19 | 1987-12-15 | Genentech, Inc. | Polycistronic expression vector construction |
JPS60501140A (ja) | 1983-04-22 | 1985-07-25 | アムジエン | 酵母による外因性ポリペプチドの分泌 |
NZ207926A (en) | 1983-04-25 | 1988-04-29 | Genentech Inc | Use of yeast #a#-factor to assist in expression of proteins heterologus to yeast |
US4745051A (en) | 1983-05-27 | 1988-05-17 | The Texas A&M University System | Method for producing a recombinant baculovirus expression vector |
US4870008A (en) | 1983-08-12 | 1989-09-26 | Chiron Corporation | Secretory expression in eukaryotes |
DK58285D0 (da) | 1984-05-30 | 1985-02-08 | Novo Industri As | Peptider samt fremstilling og anvendelse deraf |
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 |
US4975282A (en) | 1985-06-26 | 1990-12-04 | The Liposome Company, Inc. | Multilamellar liposomes having improved trapping efficiencies |
EP0625577A1 (en) | 1985-08-29 | 1994-11-23 | Genencor International, Inc. | Heterologous polypeptides expressed in filamentous fungi, processes for their preparation, and vectors for their preparation |
HU206897B (en) | 1985-10-25 | 1993-01-28 | Zymogenetics Inc | Process for utilizing bar-1 gen for selecting strange proteins |
DK122686D0 (da) | 1986-03-17 | 1986-03-17 | Novo Industri As | Fremstilling af proteiner |
GB8610600D0 (en) | 1986-04-30 | 1986-06-04 | Novo Industri As | Transformation of trichoderma |
GB8615942D0 (en) | 1986-06-30 | 1986-08-06 | Animal & Food Research Council | Peptide production |
NZ221259A (en) | 1986-07-31 | 1990-05-28 | Calgene Inc | Seed specific transcriptional regulation |
DK323587D0 (da) * | 1987-06-25 | 1987-06-25 | Novo Industri As | Protein |
US4837028A (en) | 1986-12-24 | 1989-06-06 | Liposome Technology, Inc. | Liposomes with enhanced circulation time |
GB8700458D0 (en) | 1987-01-09 | 1987-02-11 | Unvala Ltd | Communications systems |
EP0279582A3 (en) | 1987-02-17 | 1989-10-18 | Pharming B.V. | Dna sequences to target proteins to the mammary gland for efficient secretion |
US4873316A (en) | 1987-06-23 | 1989-10-10 | Biogen, Inc. | Isolation of exogenous recombinant proteins from the milk of transgenic mammals |
EP0383779B2 (en) | 1987-09-04 | 2000-05-31 | Novo Nordisk A/S | PROCESS FOR THE PRODUCTION OF PROTEIN PRODUCTS IN $i(ASPERGILLUS) AND PROMOTERS FOR USE IN $i(ASPERGILLUS) |
DK463887D0 (da) | 1987-09-07 | 1987-09-07 | Novo Industri As | Gaerleader |
GB8826446D0 (en) | 1988-11-11 | 1988-12-14 | Agricultural & Food Res | Peptide production |
AU4647889A (en) | 1988-11-18 | 1990-06-12 | Cetus Corporation | Insect signal peptide mediated secretion of recombinant proteins |
GB8910962D0 (en) | 1989-05-12 | 1989-06-28 | Natural Environment Res | Novel baculovirus expression vectors and use thereof in the expression of foreign proteins in insects or insect cells |
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 |
US5155037A (en) | 1989-08-04 | 1992-10-13 | The Texas A&M University System | Insect signal sequences useful to improve the efficiency of processing and secretion of foreign genes in insect systems |
US5023328A (en) | 1989-08-04 | 1991-06-11 | The Texas A&M University System | Lepidopteran AKH signal sequence |
DE69131292T2 (de) | 1990-01-29 | 1999-09-30 | Zymogenetics, Inc. | Antikoagulierende proteine |
DK300090D0 (da) | 1990-12-19 | 1990-12-19 | Novo Nordisk As | Fremgangsmaade til fremstilling af leadersekvenser |
AU1228592A (en) | 1991-01-11 | 1992-08-17 | American Red Cross | Expression of active human protein c in mammary tissue of transgenic animals |
JP4451514B2 (ja) * | 1999-08-24 | 2010-04-14 | 財団法人化学及血清療法研究所 | 血液凝固第vii因子改変体 |
DE60138364D1 (de) * | 2000-02-11 | 2009-05-28 | Bayer Healthcare Llc | Gerinnungsfaktor vii oder viia konjugate |
WO2001083725A1 (en) * | 2000-05-03 | 2001-11-08 | Novo Nordisk A/S | Human coagulation factor vii variants |
ATE386538T1 (de) * | 2001-02-05 | 2008-03-15 | Novo Nordisk Healthcare Ag | Kombinierte verwendung von faktor vii polypeptiden und faktor viii polypeptiden |
-
2002
- 2002-09-26 AU AU2002333211A patent/AU2002333211B2/en not_active Ceased
- 2002-09-26 UA UA2004031982A patent/UA82177C2/ru unknown
- 2002-09-26 AT AT02799394T patent/ATE532858T1/de active
- 2002-09-26 WO PCT/DK2002/000635 patent/WO2003027147A2/en active Application Filing
- 2002-09-26 ES ES02799394T patent/ES2376694T3/es not_active Expired - Lifetime
- 2002-09-26 HU HU0500060A patent/HUP0500060A3/hu unknown
- 2002-09-26 KR KR10-2004-7004600A patent/KR20040039444A/ko not_active Application Discontinuation
- 2002-09-26 CN CNA028206096A patent/CN1602354A/zh active Pending
- 2002-09-26 RU RU2004112768/13A patent/RU2325401C2/ru not_active IP Right Cessation
- 2002-09-26 IL IL16089702A patent/IL160897A0/xx unknown
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- 2002-09-26 MX MXPA04002833A patent/MXPA04002833A/es active IP Right Grant
- 2002-09-26 CA CA002461003A patent/CA2461003A1/en not_active Abandoned
- 2002-09-26 JP JP2003530733A patent/JP4537059B2/ja not_active Expired - Fee Related
- 2002-09-26 CZ CZ2004427A patent/CZ2004427A3/cs unknown
- 2002-09-26 PL PL02368619A patent/PL368619A1/xx unknown
- 2002-09-26 EP EP02799394A patent/EP1432794B1/en not_active Expired - Lifetime
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2004
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IL160897A0 (en) | 2004-08-31 |
CZ2004427A3 (cs) | 2004-08-18 |
WO2003027147A2 (en) | 2003-04-03 |
CA2461003A1 (en) | 2003-04-03 |
JP2005509413A (ja) | 2005-04-14 |
HUP0500060A3 (en) | 2010-01-28 |
RU2004112768A (ru) | 2006-01-10 |
EP1432794A2 (en) | 2004-06-30 |
ATE532858T1 (de) | 2011-11-15 |
JP4537059B2 (ja) | 2010-09-01 |
EP1432794B1 (en) | 2011-11-09 |
PL368619A1 (en) | 2005-04-04 |
NO20041700L (no) | 2004-04-26 |
KR20040039444A (ko) | 2004-05-10 |
CN1602354A (zh) | 2005-03-30 |
ES2376694T3 (es) | 2012-03-16 |
BR0212818A (pt) | 2004-10-05 |
AU2002333211B2 (en) | 2008-05-08 |
ZA200402262B (en) | 2004-06-02 |
WO2003027147A3 (en) | 2003-11-27 |
HUP0500060A2 (hu) | 2005-04-28 |
MXPA04002833A (es) | 2004-07-15 |
RU2325401C2 (ru) | 2008-05-27 |
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