RU2501565C2 - Слитый белок дефектная хлорамфеникол ацетилтрансфераза (сат)-соматостатин и его применения - Google Patents
Слитый белок дефектная хлорамфеникол ацетилтрансфераза (сат)-соматостатин и его применения Download PDFInfo
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- RU2501565C2 RU2501565C2 RU2011100104/15A RU2011100104A RU2501565C2 RU 2501565 C2 RU2501565 C2 RU 2501565C2 RU 2011100104/15 A RU2011100104/15 A RU 2011100104/15A RU 2011100104 A RU2011100104 A RU 2011100104A RU 2501565 C2 RU2501565 C2 RU 2501565C2
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- somatostatin
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| CA2728735A1 (en) | 2008-06-25 | 2009-12-30 | Braasch Biotech Llc | Compositions and methods for enhanced somatostatin immunogenicity |
| RU2501565C2 (ru) | 2008-06-25 | 2013-12-20 | Брааш Биотех Ллк | Слитый белок дефектная хлорамфеникол ацетилтрансфераза (сат)-соматостатин и его применения |
| WO2014003538A1 (en) * | 2012-06-26 | 2014-01-03 | Biovalence Sdn. Bhd. | Rapid specific pathogen free animal |
| JP6595340B2 (ja) | 2012-11-08 | 2019-10-23 | ペアシュイ ファルマ ソシエテ アノニム | Ｃ４ｓプロテオグリカン特異的トランスポーター分子 |
| RU2526571C1 (ru) * | 2013-04-08 | 2014-08-27 | Сергей Михайлович Юдин | Инъекционный препарат для повышения спермопродукции человека и способ его применения |
| WO2016029013A2 (en) | 2014-08-21 | 2016-02-25 | Braasch Biotech Llc | Methods for improving immunological response in vaccinated animals |
| WO2021024020A1 (en) | 2019-08-06 | 2021-02-11 | Astellas Pharma Inc. | Combination therapy involving antibodies against claudin 18.2 and immune checkpoint inhibitors for treatment of cancer |
| JP7727389B2 (ja) * | 2020-02-11 | 2025-08-21 | ブラッシュ・バイオテック・エルエルシー | 乳房炎の処置及び／又は予防のための組成物 |
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| RU2034457C1 (ru) * | 1993-06-22 | 1995-05-10 | Товарищество с ограниченной ответственностью "Ветек" | Способ повышения продуктивности сельскохозяйственных животных и препарат для его осуществления |
| US6316004B1 (en) * | 1993-06-22 | 2001-11-13 | T. Tikhonenko | Chimeric somatostatin containing protein and encoding DNA, plasmids of expression, method for preparing chimeric protein, strain-producers, immunogenic composition, method for increasing the productivity of farm animals |
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| US4342832A (en) | 1979-07-05 | 1982-08-03 | Genentech, Inc. | Method of constructing a replicable cloning vehicle having quasi-synthetic genes |
| US4446235A (en) | 1982-03-22 | 1984-05-01 | Genentech, Inc. | Method for cloning human growth hormone varient genes |
| WO1989004326A1 (en) * | 1987-11-04 | 1989-05-18 | California Biotechnology Inc. | Alveolar surfactant proteins |
| US6025368A (en) | 1997-02-25 | 2000-02-15 | Celtrix Pharmaceuticals, Inc. | Method for treating the symptoms of chronic stress-related disorders using IGF |
| US20070048860A1 (en) | 1997-10-10 | 2007-03-01 | The Government Of The Usa, As Represented By The Secretary, Department Of Health And Human Services | Carcinoembryonic antigen (CEA) peptides |
| PL213561B1 (pl) * | 2004-01-09 | 2013-03-29 | Inst Biotechnologii I Antybiotykow | Sposób otrzymywania plazmidu, plazmid oraz zastosowania |
| US7998930B2 (en) | 2004-11-04 | 2011-08-16 | Hanall Biopharma Co., Ltd. | Modified growth hormones |
| EP1896002A4 (en) | 2005-06-27 | 2009-11-25 | Biovail Lab Int Srl | BUPROPIONAL SALT FORMULATIONS WITH MODIFIED RELEASE |
| CA2728735A1 (en) | 2008-06-25 | 2009-12-30 | Braasch Biotech Llc | Compositions and methods for enhanced somatostatin immunogenicity |
| RU2501565C2 (ru) | 2008-06-25 | 2013-12-20 | Брааш Биотех Ллк | Слитый белок дефектная хлорамфеникол ацетилтрансфераза (сат)-соматостатин и его применения |
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2034457C1 (ru) * | 1993-06-22 | 1995-05-10 | Товарищество с ограниченной ответственностью "Ветек" | Способ повышения продуктивности сельскохозяйственных животных и препарат для его осуществления |
| US6316004B1 (en) * | 1993-06-22 | 2001-11-13 | T. Tikhonenko | Chimeric somatostatin containing protein and encoding DNA, plasmids of expression, method for preparing chimeric protein, strain-producers, immunogenic composition, method for increasing the productivity of farm animals |
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| Title |
|---|
| SZCZEPANOWSKI et al. The 120 592 bp IncF plasmid pRSB107 isolated from a sewage-treatment plantencodes nine different antibiotic-resistance determinants, twoiron-acquisition systems and other putative virulence-associated functions. Microbiology (Mosc.) 151:1095-1111 (2005). NUCLEOTIDE SEQUENCE. SZCZEPANOWSKI et al. The 120 592 bp IncF plasmid pRSB107 isolated from a sewage-treatment plantencodes nine different antibiotic-resistance determinants, twoiron-acquisition systems and other putative virulence-associated functions. Microbiology (Mosc.) 151:1095-1111 (2005). NUCLEOTIDE SEQUENCE. Vallenet D. et al., Comparative analysis of Acinetobacters: three genomes for three lifestyles. PLoS ONE 3:E1805-E1805 (2008). NUCLEOTIDE SEQUENCE. LEWENDON A. and SHAW W.V. The PKa of the catalytic histidine residue of chloramphenicol acetyltransferase, Biochem. J. (1993) 290, pp.15-19. * |
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| NZ590011A (en) | 2012-09-28 |
| DK2303314T3 (da) | 2014-01-13 |
| US8367073B2 (en) | 2013-02-05 |
| US20120076806A1 (en) | 2012-03-29 |
| BRPI0822826A2 (pt) | 2015-07-07 |
| US20100136037A1 (en) | 2010-06-03 |
| JP2011525914A (ja) | 2011-09-29 |
| US7722881B2 (en) | 2010-05-25 |
| EP2303314A4 (en) | 2012-07-18 |
| MX2010014082A (es) | 2011-04-07 |
| EP2303314A1 (en) | 2011-04-06 |
| ES2445403T3 (es) | 2014-03-03 |
| WO2009157926A1 (en) | 2009-12-30 |
| AU2008358353B2 (en) | 2013-11-07 |
| CN102105163A (zh) | 2011-06-22 |
| KR20110039517A (ko) | 2011-04-19 |
| JP5506792B2 (ja) | 2014-05-28 |
| AU2008358353A1 (en) | 2009-12-30 |
| CA2728734A1 (en) | 2009-12-30 |
| US7943143B2 (en) | 2011-05-17 |
| IL209792A0 (en) | 2011-02-28 |
| KR101555731B1 (ko) | 2015-09-25 |
| EP2303314B1 (en) | 2013-12-11 |
| RU2011100104A (ru) | 2012-07-20 |
| US20090324629A1 (en) | 2009-12-31 |
| IL209792A (en) | 2012-12-31 |
| ZA201009125B (en) | 2012-06-27 |
| CN102105163B (zh) | 2014-12-10 |
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