NO327325B1 - Ekspresjonsvektor, vertcelle samt fremgangsmate for fremstilling av et peptidprodukt. - Google Patents
Ekspresjonsvektor, vertcelle samt fremgangsmate for fremstilling av et peptidprodukt. Download PDFInfo
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- NO327325B1 NO327325B1 NO19995014A NO995014A NO327325B1 NO 327325 B1 NO327325 B1 NO 327325B1 NO 19995014 A NO19995014 A NO 19995014A NO 995014 A NO995014 A NO 995014A NO 327325 B1 NO327325 B1 NO 327325B1
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- peptide
- peptide product
- host cell
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Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/22—Hormones
- A61K38/23—Calcitonins
-
- 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
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/461—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from fish
-
- 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
- C07K14/575—Hormones
- C07K14/585—Calcitonins
-
- 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
- C07K14/575—Hormones
- C07K14/635—Parathyroid hormone (parathormone); Parathyroid hormone-related peptides
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/70—Vectors or expression systems specially adapted for E. coli
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/70—Vectors or expression systems specially adapted for E. coli
- C12N15/71—Expression systems using regulatory sequences derived from the trp-operon
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/70—Vectors or expression systems specially adapted for E. coli
- C12N15/72—Expression systems using regulatory sequences derived from the lac-operon
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US4370097P | 1997-04-16 | 1997-04-16 | |
| PCT/US1998/007723 WO1998046722A1 (fr) | 1997-04-16 | 1998-04-15 | Expression directe de peptides dans un milieu de culture |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| NO995014D0 NO995014D0 (no) | 1999-10-14 |
| NO995014L NO995014L (no) | 1999-12-13 |
| NO327325B1 true NO327325B1 (no) | 2009-06-08 |
Family
ID=21928441
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO19995014A NO327325B1 (no) | 1997-04-16 | 1999-10-14 | Ekspresjonsvektor, vertcelle samt fremgangsmate for fremstilling av et peptidprodukt. |
Country Status (14)
| Country | Link |
|---|---|
| US (5) | US6103495A (fr) |
| EP (2) | EP1005526B1 (fr) |
| JP (2) | JP4907751B2 (fr) |
| AT (2) | ATE522598T1 (fr) |
| AU (1) | AU742270B2 (fr) |
| CA (1) | CA2285658C (fr) |
| DE (1) | DE69841939D1 (fr) |
| DK (2) | DK1005526T3 (fr) |
| ES (1) | ES2375330T3 (fr) |
| HU (1) | HUP0001272A3 (fr) |
| LT (1) | LT4701B (fr) |
| NO (1) | NO327325B1 (fr) |
| RU (1) | RU2218407C2 (fr) |
| WO (1) | WO1998046722A1 (fr) |
Families Citing this family (43)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DK1005526T3 (da) * | 1997-04-16 | 2011-02-07 | Unigene Lab Inc | Direkte ekspression af peptider i kulturmedium |
| KR100385298B1 (ko) * | 2000-09-05 | 2003-05-23 | 한국생명공학연구원 | 단백질 생산방법 |
| US7166575B2 (en) * | 2002-12-17 | 2007-01-23 | Nastech Pharmaceutical Company Inc. | Compositions and methods for enhanced mucosal delivery of peptide YY and methods for treating and preventing obesity |
| TW200411053A (en) | 2002-12-30 | 2004-07-01 | Ind Tech Res Inst | Nucleic acid encoding recombinant salmon calcitionin, expression vector thereof, and method for producing recombinant salmon calcitonin therewith |
| US8088734B2 (en) * | 2003-01-21 | 2012-01-03 | Unigene Laboratories Inc. | Oral delivery of peptides |
| WO2005072277A2 (fr) * | 2004-01-21 | 2005-08-11 | Unigene Laboratories Inc. | Fragments amides de l'hormone parathyroide et leurs applications |
| US8227241B2 (en) * | 2004-03-12 | 2012-07-24 | Unigene Laboratories, Inc. | Bacterial host cell for the direct expression of peptides |
| US7648965B2 (en) * | 2004-05-14 | 2010-01-19 | Unigene Laboratories Inc. | Method for fostering bone formation and preservation |
| US7531518B2 (en) * | 2004-05-14 | 2009-05-12 | Unigene Laboratories Inc. | Method for fostering bone formation and preservation |
| US20060089723A1 (en) * | 2004-10-25 | 2006-04-27 | Murphy Kieran P | Method for bone augmentation |
| US7445911B2 (en) * | 2004-11-24 | 2008-11-04 | Unigene Laboratories Inc. | Enzymatic reactions in the presence of keto acids |
| PA8660701A1 (es) | 2005-02-04 | 2006-09-22 | Pfizer Prod Inc | Agonistas de pyy y sus usos |
| US20060293667A1 (en) * | 2005-05-19 | 2006-12-28 | Agnes Vignery | Bone implant device and methods of using same |
| WO2006130806A2 (fr) * | 2005-06-01 | 2006-12-07 | University Of Pittsburgh Of The Commonwealth System Of Higher Education | Dosage destine aux agonistes et antagonistes de canaux ioniques et aux regulateurs d'expression genetique |
| WO2006132925A2 (fr) | 2005-06-01 | 2006-12-14 | University Of Pittsburgh Of The Commonwealth System Of Higher Education | Procede de biosynthese de peptide amide et administration d'endomorphine-2 in vivo en vue du traitement de la douleur |
| ES2437068T3 (es) | 2005-06-24 | 2014-01-08 | Enteris Biopharma, Inc. | Líneas celulares para expresar enzima útil en la preparación de productos amidados |
| ATE524493T1 (de) | 2006-07-24 | 2011-09-15 | Biorexis Pharmaceutical Corp | Exendin-fusionsproteine |
| US8377863B2 (en) | 2007-05-29 | 2013-02-19 | Unigene Laboratories Inc. | Peptide pharmaceutical for oral delivery |
| RU2370280C2 (ru) * | 2007-10-08 | 2009-10-20 | Институт физико-химической биологии им. А.Н.Белозерского | СПОСОБ СУПЕРПРОДУКЦИИ В РАСТЕНИИ АНТИТЕЛ ПРОТИВ ОНКОГЕНА HER2/neu |
| US9399773B2 (en) | 2012-08-10 | 2016-07-26 | Shi-Lung Lin | Production and extraction of MicroRNA precursor as drug for cancer therapy |
| US9422559B2 (en) | 2010-06-02 | 2016-08-23 | Shi-Lung Lin | Production and utilization of a novel anti-cancer drug in therapy |
| EP2389388B1 (fr) | 2009-01-22 | 2017-03-08 | KeyBioscience AG | Traitement de l'obésité |
| CN103764669B (zh) | 2011-06-15 | 2017-08-15 | 雷索特制药公司 | 抗炎药物产品 |
| JP6185468B2 (ja) | 2011-08-12 | 2017-08-23 | メロ バイオテクノロジー インコーポレイテッドＭｅｌｌｏ Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，Ｉｎｃ． | 原核細胞内においてヘアピン様ｒｎａを発現させる方法及び組成物 |
| JP6170933B2 (ja) | 2011-11-02 | 2017-07-26 | キーバイオサイエンス・アクチエンゲゼルシャフト | ペプチドの使用 |
| SI3095484T1 (en) | 2011-11-02 | 2018-08-31 | Keybioscience Ag | Calcitonin mimetics for the treatment of diseases and disorders |
| US9102751B2 (en) * | 2012-05-18 | 2015-08-11 | Janssen Biotech, Inc. | Huwentoxin-IV variants and methods of use |
| US10414808B2 (en) | 2012-05-18 | 2019-09-17 | Janssen Biotech, Inc. | Huwentoxin-IV variants and methods of use |
| US10196662B2 (en) | 2012-08-10 | 2019-02-05 | Mello Biotechnology, Inc. | Composition for producing microRNA precursors as drugs for enhancing wound healing and production method of the microRNA precursors |
| DK2964193T3 (da) | 2013-03-05 | 2020-03-16 | Enteris Biopharma Inc | Lægemidler til oral indgivelse |
| WO2015051216A1 (fr) | 2013-10-03 | 2015-04-09 | Janssen Biotech, Inc. | Variants de protoxine ii et méthodes d'utilisation |
| JP6639389B2 (ja) | 2013-11-14 | 2020-02-05 | キーバイオサイエンス・アクチエンゲゼルシャフト | 疾患および障害を処置するためのカルシトニン模倣体 |
| CN103709236B (zh) * | 2013-12-23 | 2015-04-15 | 江南大学 | 一种可提高分泌效率的信号肽及其应用 |
| EP3244878B1 (fr) | 2015-01-12 | 2022-08-10 | Enteris BioPharma, Inc. | Formes galéniques orales solides |
| MA41642A (fr) | 2015-03-03 | 2018-01-09 | Janssen Biotech Inc | Variants de protoxine ii et méthodes d'utilisation |
| BR112017020896A2 (pt) | 2015-04-02 | 2018-07-10 | Janssen Biotech Inc | variantes de protoxina-ii e métodos de uso |
| WO2017095458A1 (fr) | 2015-12-02 | 2017-06-08 | Chih-Li Lin | Composition et méthode d'utilisation de précurseurs de mir-302 en tant que médicaments pour le traitement de la maladie d'alzheimer |
| JP2018535684A (ja) | 2015-12-02 | 2018-12-06 | リン、シー−ランLIN, Shi−Lung | ＣＤ３４陽性成体幹細胞の増殖を誘導する薬物としてのｍｉｃｒｏＲＮＡ前駆体の使用 |
| GB201704429D0 (en) | 2017-03-21 | 2017-05-03 | Keybioscience Ag | Calcitonin mimetics for treating diseases and disorders |
| GB201707955D0 (en) | 2017-05-18 | 2017-07-05 | Keybioscience Ag | Dual amylin and calcitonin receptor agonists for treating diseases and disorders |
| GB201813677D0 (en) | 2018-08-22 | 2018-10-03 | Keybioscience Ag | Calcitonin mimetics for treating diseases and disorders |
| GB201813678D0 (en) | 2018-08-22 | 2018-10-03 | Keybioscience Ag | Acylated calcitonin mimetics |
| GB202001024D0 (en) | 2020-01-24 | 2020-03-11 | Key Bioscience Ag | Oxyntomodulin mimetics |
Family Cites Families (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5332664A (en) * | 1981-07-15 | 1994-07-26 | Celltech Limited | Human calcitonin precursor polyprotein structural gene |
| US4595658A (en) * | 1982-09-13 | 1986-06-17 | The Rockefeller University | Method for facilitating externalization of proteins synthesized in bacteria |
| US4620948A (en) * | 1982-12-22 | 1986-11-04 | Genentech, Inc. | Purification and activity assurance of precipitated heterologous proteins |
| US4962055A (en) * | 1983-03-08 | 1990-10-09 | Rikagaku Kenkyusho | Plasmid, method for construction of the same, microorganisms carrying the plasmid and method for cultivation of the microorganism |
| US4757013A (en) * | 1983-07-25 | 1988-07-12 | The Research Foundation Of State University Of New York | Cloning vehicles for polypeptide expression in microbial hosts |
| US6319685B1 (en) | 1984-09-27 | 2001-11-20 | Unigene Laboratories, Inc. | Alpha-amidating enzyme compositions and processes for their production and use |
| US4708934A (en) | 1984-09-27 | 1987-11-24 | Unigene Laboratories, Inc. | α-amidation enzyme |
| US5747281A (en) * | 1984-09-28 | 1998-05-05 | Cornell Research Foundation, Inc. | System useful for the production of proteins from recombinant DNA in single celled organisms |
| EP0177343B1 (fr) | 1984-10-05 | 1992-07-22 | Genentech, Inc. | ADN, cultures de cellules et méthodes pour sécréter des protéines hétérologiques et récupérer des protéines périplasmiques |
| DE3632037A1 (de) * | 1986-09-20 | 1988-04-07 | Hoechst Ag | Gentechnisches verfahren zur herstellung von salm-calcitonin sowie mittel zur durchfuehrung dieses verfahrens |
| US5089406A (en) * | 1987-01-07 | 1992-02-18 | Allied-Signal Inc. | Method of producing a gene cassette coding for polypeptides with repeating amino acid sequences |
| US4946790A (en) * | 1987-02-06 | 1990-08-07 | Mitsui Toatsu Chemicals, Inc. | Recombinant plasmid for the expression of L-phenylalanine ammonia-lyase and transformed strain carrying same |
| US5789234A (en) | 1987-08-14 | 1998-08-04 | Unigene Laboratories, Inc. | Expression systems for amidating enzyme |
| US5223407A (en) * | 1988-08-31 | 1993-06-29 | Allelix Inc. | Excretion of heterologous proteins from e. coli |
| JP2551399B2 (ja) * | 1989-08-15 | 1996-11-06 | 株式会社資生堂 | Ｃ末端アミド化に関与する酵素並びにその製造方法及びその使用 |
| US5240831A (en) * | 1991-01-10 | 1993-08-31 | Board Of Regents, The University Of Texas | Methods and compositions for the expression of biologically active eukaryotic cytochrome p45os in bacteria |
| US5547862A (en) * | 1993-07-29 | 1996-08-20 | Ambion Inc. | Vectors containing multiple promoters in the same orientation |
| US5589364A (en) * | 1994-07-29 | 1996-12-31 | Magainin Pharmaceuticals Inc. | Recombinant production of biologically active peptides and proteins |
| DK1005526T3 (da) * | 1997-04-16 | 2011-02-07 | Unigene Lab Inc | Direkte ekspression af peptider i kulturmedium |
-
1998
- 1998-04-15 DK DK98918334.8T patent/DK1005526T3/da active
- 1998-04-15 AU AU71279/98A patent/AU742270B2/en not_active Ceased
- 1998-04-15 WO PCT/US1998/007723 patent/WO1998046722A1/fr active IP Right Grant
- 1998-04-15 CA CA2285658A patent/CA2285658C/fr not_active Expired - Fee Related
- 1998-04-15 US US09/060,765 patent/US6103495A/en not_active Expired - Lifetime
- 1998-04-15 DK DK09006784.4T patent/DK2088188T3/da active
- 1998-04-15 EP EP98918334A patent/EP1005526B1/fr not_active Expired - Lifetime
- 1998-04-15 JP JP54430898A patent/JP4907751B2/ja not_active Expired - Lifetime
- 1998-04-15 RU RU99124196/13A patent/RU2218407C2/ru active
- 1998-04-15 EP EP09006784A patent/EP2088188B1/fr not_active Expired - Lifetime
- 1998-04-15 AT AT09006784T patent/ATE522598T1/de not_active IP Right Cessation
- 1998-04-15 ES ES09006784T patent/ES2375330T3/es not_active Expired - Lifetime
- 1998-04-15 AT AT98918334T patent/ATE484572T1/de not_active IP Right Cessation
- 1998-04-15 HU HU0001272A patent/HUP0001272A3/hu unknown
- 1998-04-15 DE DE69841939T patent/DE69841939D1/de not_active Expired - Lifetime
-
1999
- 1999-10-14 NO NO19995014A patent/NO327325B1/no not_active IP Right Cessation
- 1999-11-10 LT LT99-133A patent/LT4701B/lt not_active IP Right Cessation
-
2000
- 2000-02-08 US US09/500,009 patent/US6210925B1/en not_active Expired - Lifetime
-
2001
- 2001-02-09 US US09/780,878 patent/US6627438B2/en not_active Expired - Lifetime
- 2001-02-09 US US09/780,643 patent/US6737250B2/en not_active Expired - Lifetime
-
2004
- 2004-04-05 US US10/818,966 patent/US7968311B2/en not_active Expired - Fee Related
-
2011
- 2011-11-09 JP JP2011245398A patent/JP5634971B2/ja not_active Expired - Lifetime
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