JP2011504374A - 繊維状ポリペプチドおよび多糖を含む組成物 - Google Patents
繊維状ポリペプチドおよび多糖を含む組成物 Download PDFInfo
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- C07K14/43563—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from insects
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- C07K—PEPTIDES
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- C07K14/43586—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from insects from silkworms
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- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
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- C07K14/43504—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
- C07K14/43595—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from coelenteratae, e.g. medusae
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- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
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- C07K14/745—Blood coagulation or fibrinolysis factors
- C07K14/75—Fibrinogen
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- C07K17/00—Carrier-bound or immobilised peptides; Preparation thereof
- C07K17/02—Peptides being immobilised on, or in, an organic carrier
- C07K17/10—Peptides being immobilised on, or in, an organic carrier the carrier being a carbohydrate
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- C08B—POLYSACCHARIDES; DERIVATIVES THEREOF
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- C08B—POLYSACCHARIDES; DERIVATIVES THEREOF
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- C08B15/05—Derivatives containing elements other than carbon, hydrogen, oxygen, halogens or sulfur
- C08B15/06—Derivatives containing elements other than carbon, hydrogen, oxygen, halogens or sulfur containing nitrogen, e.g. carbamates
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- C—CHEMISTRY; METALLURGY
- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08L—COMPOSITIONS OF MACROMOLECULAR COMPOUNDS
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- 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
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/82—Vectors or expression systems specially adapted for eukaryotic hosts for plant cells, e.g. plant artificial chromosomes (PACs)
- C12N15/8241—Phenotypically and genetically modified plants via recombinant DNA technology
- C12N15/8242—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits
- C12N15/8257—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits for the production of primary gene products, e.g. pharmaceutical products, interferon
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- C07K2319/00—Fusion polypeptide
- C07K2319/20—Fusion polypeptide containing a tag with affinity for a non-protein ligand
Landscapes
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| PCT/IL2008/001542 WO2009069123A2 (en) | 2007-11-26 | 2008-11-26 | Compositions comprising fibrous polypeptides and polysaccharides |
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| WO2014103846A1 (ja) * | 2012-12-27 | 2014-07-03 | スパイバー株式会社 | 親水性組換えタンパク質の抽出方法 |
| JP2015518489A (ja) * | 2012-05-02 | 2015-07-02 | スパイバー テクノロジーズ アーベーSpiber Technologies Ab | 親和性リガンドとして免疫グロブリン断片を組み込んだクモ糸融合タンパク質の構造 |
| US9968682B2 (en) | 2013-04-25 | 2018-05-15 | Spiber Inc. | Polypeptide hydrogel and method for producing same |
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| WO2019194231A1 (ja) * | 2018-04-03 | 2019-10-10 | Spiber株式会社 | タンパク質組成物及びその製造方法 |
| JP2023522994A (ja) * | 2020-04-23 | 2023-06-01 | シービックス マテリアル サイエンシーズ リミテッド | 修飾されたスパイダーシルク繊維およびその使用 |
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Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2000503206A (ja) * | 1996-01-16 | 2000-03-21 | ユニヴァーシティ・オブ・ブリティッシュ・コロンビア | 成長因子―多糖結合融合タンパクを使用して細胞増殖を調節する組成物および方法 |
| JP2004504803A (ja) * | 1999-11-08 | 2004-02-19 | シービーデイ テクノロジーズ リミテッド | 多糖含有材料の改変 |
| WO2004104042A1 (en) * | 2003-05-21 | 2004-12-02 | Commonwealth Scientific And Industrial Research Organisation | A bioelastomer |
| JP2007507495A (ja) * | 2003-05-14 | 2007-03-29 | ダウ・コーニング・コーポレイション | 反復配列タンパク質ポリマー活性剤結合体、方法および使用 |
| JP2007531506A (ja) * | 2003-05-21 | 2007-11-08 | コモンウェルス サイエンティフィック アンド インダストリアル リサーチ オーガナイゼイション | 合成バイオエラストマー |
| WO2008055931A1 (de) * | 2006-11-08 | 2008-05-15 | Basf Se | Verwendung von natürlichen, rekombinanten und synthetischen resilinen in der kosmetik |
Family Cites Families (63)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| NL154600B (nl) | 1971-02-10 | 1977-09-15 | Organon Nv | Werkwijze voor het aantonen en bepalen van specifiek bindende eiwitten en hun corresponderende bindbare stoffen. |
| NL154598B (nl) | 1970-11-10 | 1977-09-15 | Organon Nv | Werkwijze voor het aantonen en bepalen van laagmoleculire verbindingen en van eiwitten die deze verbindingen specifiek kunnen binden, alsmede testverpakking. |
| NL154599B (nl) | 1970-12-28 | 1977-09-15 | Organon Nv | Werkwijze voor het aantonen en bepalen van specifiek bindende eiwitten en hun corresponderende bindbare stoffen, alsmede testverpakking. |
| US3901654A (en) | 1971-06-21 | 1975-08-26 | Biological Developments | Receptor assays of biologically active compounds employing biologically specific receptors |
| US3853987A (en) | 1971-09-01 | 1974-12-10 | W Dreyer | Immunological reagent and radioimmuno assay |
| US3867517A (en) | 1971-12-21 | 1975-02-18 | Abbott Lab | Direct radioimmunoassay for antigens and their antibodies |
| NL171930C (nl) | 1972-05-11 | 1983-06-01 | Akzo Nv | Werkwijze voor het aantonen en bepalen van haptenen, alsmede testverpakkingen. |
| US3850578A (en) | 1973-03-12 | 1974-11-26 | H Mcconnell | Process for assaying for biologically active molecules |
| US3935074A (en) | 1973-12-17 | 1976-01-27 | Syva Company | Antibody steric hindrance immunoassay with two antibodies |
| US3996345A (en) | 1974-08-12 | 1976-12-07 | Syva Company | Fluorescence quenching with immunological pairs in immunoassays |
| US4034074A (en) | 1974-09-19 | 1977-07-05 | The Board Of Trustees Of Leland Stanford Junior University | Universal reagent 2-site immunoradiometric assay using labelled anti (IgG) |
| US3984533A (en) | 1975-11-13 | 1976-10-05 | General Electric Company | Electrophoretic method of detecting antigen-antibody reaction |
| US4098876A (en) | 1976-10-26 | 1978-07-04 | Corning Glass Works | Reverse sandwich immunoassay |
| US4879219A (en) | 1980-09-19 | 1989-11-07 | General Hospital Corporation | Immunoassay utilizing monoclonal high affinity IgM antibodies |
| CA1192510A (en) | 1981-05-27 | 1985-08-27 | Lawrence E. Pelcher | Rna plant virus vector or portion thereof, a method of construction thereof, and a method of producing a gene derived product therefrom |
| US4946929A (en) | 1983-03-22 | 1990-08-07 | Massachusetts Institute Of Technology | Bioerodible articles useful as implants and prostheses having predictable degradation rates |
| JPS6054684A (ja) | 1983-09-05 | 1985-03-29 | Teijin Ltd | 新規dνa及びハイブリツドdνa |
| US5011771A (en) | 1984-04-12 | 1991-04-30 | The General Hospital Corporation | Multiepitopic immunometric assay |
| US4666828A (en) | 1984-08-15 | 1987-05-19 | The General Hospital Corporation | Test for Huntington's disease |
| US4638045A (en) | 1985-02-19 | 1987-01-20 | Massachusetts Institute Of Technology | Non-peptide polyamino acid bioerodible polymers |
| CA1288073C (en) | 1985-03-07 | 1991-08-27 | Paul G. Ahlquist | Rna transformation vector |
| US4683202A (en) | 1985-03-28 | 1987-07-28 | Cetus Corporation | Process for amplifying nucleic acid sequences |
| US4801531A (en) | 1985-04-17 | 1989-01-31 | Biotechnology Research Partners, Ltd. | Apo AI/CIII genomic polymorphisms predictive of atherosclerosis |
| US4806621A (en) | 1986-01-21 | 1989-02-21 | Massachusetts Institute Of Technology | Biocompatible, bioerodible, hydrophobic, implantable polyimino carbonate article |
| GB8608850D0 (en) | 1986-04-11 | 1986-05-14 | Diatech Ltd | Packaging system |
| JPS6314693A (ja) | 1986-07-04 | 1988-01-21 | Sumitomo Chem Co Ltd | 植物ウイルスrnaベクタ− |
| CA1340581C (en) | 1986-11-20 | 1999-06-08 | Joseph P. Vacanti | Chimeric neomorphogenesis of organs by controlled cellular implantation using artificial matrices |
| US5804178A (en) | 1986-11-20 | 1998-09-08 | Massachusetts Institute Of Technology | Implantation of cell-matrix structure adjacent mesentery, omentum or peritoneum tissue |
| US5041138A (en) | 1986-11-20 | 1991-08-20 | Massachusetts Institute Of Technology | Neomorphogenesis of cartilage in vivo from cell culture |
| US5736372A (en) | 1986-11-20 | 1998-04-07 | Massachusetts Institute Of Technology | Biodegradable synthetic polymeric fibrous matrix containing chondrocyte for in vivo production of a cartilaginous structure |
| ES2060646T3 (es) | 1987-02-09 | 1994-12-01 | Lubrizol Genetics Inc | Virus rna hibrido. |
| US5019379A (en) | 1987-07-31 | 1991-05-28 | Massachusetts Institute Of Technology | Unsaturated polyanhydrides |
| US5137819A (en) * | 1988-07-08 | 1992-08-11 | University Of British Columbia | Cellulose binding fusion proteins for immobilization and purification of polypeptides |
| US5272057A (en) | 1988-10-14 | 1993-12-21 | Georgetown University | Method of detecting a predisposition to cancer by the use of restriction fragment length polymorphism of the gene for human poly (ADP-ribose) polymerase |
| US5010167A (en) | 1989-03-31 | 1991-04-23 | Massachusetts Institute Of Technology | Poly(amide-and imide-co-anhydride) for biological application |
| US5302523A (en) | 1989-06-21 | 1994-04-12 | Zeneca Limited | Transformation of plant cells |
| US5464764A (en) | 1989-08-22 | 1995-11-07 | University Of Utah Research Foundation | Positive-negative selection methods and vectors |
| US5192659A (en) | 1989-08-25 | 1993-03-09 | Genetype Ag | Intron sequence analysis method for detection of adjacent and remote locus alleles as haplotypes |
| EP0418695A1 (de) | 1989-09-13 | 1991-03-27 | Ciba-Geigy Ag | Regulatorische DNA-Sequenz |
| IL97020A (en) | 1990-01-30 | 2000-12-06 | Mogen Int | Recombinant polynucleotides comprising a chitinase gene and a glucanase gene |
| UA48104C2 (uk) | 1991-10-04 | 2002-08-15 | Новартіс Аг | Фрагмент днк, який містить послідовність,що кодує інсектицидний протеїн, оптимізовану для кукурудзи,фрагмент днк, який забезпечує направлену бажану для серцевини стебла експресію зв'язаного з нею структурного гена в рослині, фрагмент днк, який забезпечує специфічну для пилку експресію зв`язаного з нею структурного гена в рослині, рекомбінантна молекула днк, спосіб одержання оптимізованої для кукурудзи кодуючої послідовності інсектицидного протеїну, спосіб захисту рослин кукурудзи щонайменше від однієї комахи-шкідника |
| US5512474A (en) | 1992-05-29 | 1996-04-30 | Bsi Corporation | Cell culture support containing a cell adhesion factor and a positively-charged molecule |
| US5281521A (en) | 1992-07-20 | 1994-01-25 | The Trustees Of The University Of Pennsylvania | Modified avidin-biotin technique |
| US5399665A (en) | 1992-11-05 | 1995-03-21 | Massachusetts Institute Of Technology | Biodegradable polymers for cell transplantation |
| US5512600A (en) | 1993-01-15 | 1996-04-30 | Massachusetts Institute Of Technology | Preparation of bonded fiber structures for cell implantation |
| US5514378A (en) | 1993-02-01 | 1996-05-07 | Massachusetts Institute Of Technology | Biocompatible polymer membranes and methods of preparation of three dimensional membrane structures |
| US5527610A (en) | 1994-05-20 | 1996-06-18 | The Uab Research Foundation | Elastomeric polypeptide matrices for preventing adhesion of biological materials |
| US5716404A (en) | 1994-12-16 | 1998-02-10 | Massachusetts Institute Of Technology | Breast tissue engineering |
| US6123727A (en) | 1995-05-01 | 2000-09-26 | Massachusetts Institute Of Technology | Tissue engineered tendons and ligaments |
| US6095148A (en) | 1995-11-03 | 2000-08-01 | Children's Medical Center Corporation | Neuronal stimulation using electrically conducting polymers |
| US5902599A (en) | 1996-02-20 | 1999-05-11 | Massachusetts Institute Of Technology | Biodegradable polymer networks for use in orthopedic and dental applications |
| US6425222B1 (en) | 1996-03-08 | 2002-07-30 | Burns Norris & Stewart Limited Partnership | Method and kit for repairing a construction component |
| US5837752A (en) | 1997-07-17 | 1998-11-17 | Massachusetts Institute Of Technology | Semi-interpenetrating polymer networks |
| IL133134A0 (en) * | 1999-11-25 | 2001-03-19 | American Israeli Paper Mills | Improved paper products |
| ATE324417T1 (de) | 1999-12-17 | 2006-05-15 | Biopolymer Products Of Sweden | Polyphenolisches protein enthaltende bioadhäsive zusammensetzung |
| US7192445B2 (en) | 2000-12-06 | 2007-03-20 | Astra Tech Ab | Medical prosthetic devices and implants having improved biocompatibility |
| CN1390937A (zh) | 2002-04-25 | 2003-01-15 | 上海交通大学 | 按植物偏爱密码子设计合成的蜘蛛丝蛋白基因及其应用 |
| US6982298B2 (en) | 2003-01-10 | 2006-01-03 | The Cleveland Clinic Foundation | Hydroxyphenyl cross-linked macromolecular network and applications thereof |
| WO2006035442A2 (en) | 2004-09-29 | 2006-04-06 | Collplant Ltd. | Collagen producing plants and methods of generating and using same |
| GB0516846D0 (en) | 2005-08-17 | 2005-09-21 | Knight David P | Meniscal repair device |
| AU2008331099B2 (en) | 2007-11-26 | 2013-10-24 | Collplant Ltd. | Compositions comprising fibrous polypeptides and polysaccharides |
| WO2010055290A1 (en) | 2008-11-11 | 2010-05-20 | Oxford Biomedica (Uk) Limited | Method |
| WO2013030840A2 (en) | 2011-09-01 | 2013-03-07 | Yissum Research Development Company Of The Hebrew University Of Jerusalem Ltd. | Adhesive biopolymers and uses thereof |
-
2008
- 2008-11-26 AU AU2008331099A patent/AU2008331099B2/en not_active Ceased
- 2008-11-26 WO PCT/IL2008/001542 patent/WO2009069123A2/en not_active Ceased
- 2008-11-26 US US12/744,703 patent/US8431158B2/en active Active
- 2008-11-26 EP EP08853290.8A patent/EP2220112B1/en active Active
- 2008-11-26 EP EP20120196826 patent/EP2599790A1/en not_active Withdrawn
- 2008-11-26 JP JP2010535508A patent/JP2011504374A/ja active Pending
-
2013
- 2013-04-25 US US13/870,032 patent/US8906651B2/en active Active
-
2014
- 2014-03-13 US US14/207,864 patent/US9145463B2/en active Active
- 2014-12-08 US US14/562,849 patent/US9273152B2/en active Active
-
2015
- 2015-03-20 JP JP2015057103A patent/JP2015144610A/ja active Pending
-
2016
- 2016-02-01 US US15/011,738 patent/US9815874B2/en not_active Expired - Fee Related
Patent Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2000503206A (ja) * | 1996-01-16 | 2000-03-21 | ユニヴァーシティ・オブ・ブリティッシュ・コロンビア | 成長因子―多糖結合融合タンパクを使用して細胞増殖を調節する組成物および方法 |
| JP2004504803A (ja) * | 1999-11-08 | 2004-02-19 | シービーデイ テクノロジーズ リミテッド | 多糖含有材料の改変 |
| JP2007507495A (ja) * | 2003-05-14 | 2007-03-29 | ダウ・コーニング・コーポレイション | 反復配列タンパク質ポリマー活性剤結合体、方法および使用 |
| WO2004104042A1 (en) * | 2003-05-21 | 2004-12-02 | Commonwealth Scientific And Industrial Research Organisation | A bioelastomer |
| JP2007531506A (ja) * | 2003-05-21 | 2007-11-08 | コモンウェルス サイエンティフィック アンド インダストリアル リサーチ オーガナイゼイション | 合成バイオエラストマー |
| WO2008055931A1 (de) * | 2006-11-08 | 2008-05-15 | Basf Se | Verwendung von natürlichen, rekombinanten und synthetischen resilinen in der kosmetik |
Non-Patent Citations (7)
| Title |
|---|
| JPN6013035428; 田宮信雄ら訳: ヴォート生化学(上) 第2版, 1996, 第129-137頁 * |
| JPN6013035430; KUMAR, M. et al.: Biomacromolecules Vol.7, 2006, pp.2543-2551 * |
| JPN6013035431; LEVY, I. et al.: Biomaterials Vol.25, 2004, pp.1841-1849 * |
| JPN6014019387; ELVIN, C.M. et al.: Nature Vol.437, 2005, pp.999-1002 * |
| JPN6014019388; 新村出 編: 広辞苑 , 1999, 第2317頁 * |
| JPN6014019390; TOMME, P. et al.: J. Chromatgr. B. Vol.715, 1998, pp.283-296 * |
| JPN6014049185; NOISHIKI, Y. et al.: J. Appl. Polym. Sci. Vol.86, 2002, pp.3425-3429 * |
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| WO2014103847A1 (ja) * | 2012-12-27 | 2014-07-03 | スパイバー株式会社 | 親水性組換えタンパク質の粗精製方法 |
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| JPWO2014103847A1 (ja) * | 2012-12-27 | 2017-01-12 | Spiber株式会社 | 親水性組換えタンパク質の粗精製方法 |
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| WO2019194231A1 (ja) * | 2018-04-03 | 2019-10-10 | Spiber株式会社 | タンパク質組成物及びその製造方法 |
| JP2023522994A (ja) * | 2020-04-23 | 2023-06-01 | シービックス マテリアル サイエンシーズ リミテッド | 修飾されたスパイダーシルク繊維およびその使用 |
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| Publication number | Publication date |
|---|---|
| EP2220112B1 (en) | 2015-08-26 |
| WO2009069123A2 (en) | 2009-06-04 |
| EP2220112A2 (en) | 2010-08-25 |
| AU2008331099B2 (en) | 2013-10-24 |
| US9815874B2 (en) | 2017-11-14 |
| WO2009069123A3 (en) | 2010-01-07 |
| AU2008331099A1 (en) | 2009-06-04 |
| US20130225793A1 (en) | 2013-08-29 |
| US20100317588A1 (en) | 2010-12-16 |
| US20150094452A1 (en) | 2015-04-02 |
| US9273152B2 (en) | 2016-03-01 |
| JP2015144610A (ja) | 2015-08-13 |
| US20140256641A1 (en) | 2014-09-11 |
| EP2599790A1 (en) | 2013-06-05 |
| US8431158B2 (en) | 2013-04-30 |
| US8906651B2 (en) | 2014-12-09 |
| US9145463B2 (en) | 2015-09-29 |
| US20160145311A1 (en) | 2016-05-26 |
| WO2009069123A8 (en) | 2010-07-08 |
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