TWI788318B - 用於定序反應之聚合酶 - Google Patents
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- 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
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/52—Genes encoding for enzymes or proenzymes
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- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
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- C12P19/26—Preparation of nitrogen-containing carbohydrates
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- C12P19/30—Nucleotides
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- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
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| CA3046680A1 (en) | 2016-12-19 | 2018-06-28 | Quantum-Si Incorporated | Loading molecules into sample wells for analysis |
| WO2018204810A1 (en) | 2017-05-05 | 2018-11-08 | Quantum-Si Incorporated | Substrates having modified surface reactivity and antifouling properties in biological reactions |
| US10934533B1 (en) | 2018-10-10 | 2021-03-02 | New England Biolabs, Inc. | Variant DNA polymerases having improved properties and method for improved isothermal amplification of a target DNA |
| US10865441B2 (en) * | 2019-03-13 | 2020-12-15 | Abclonal Science, Inc. | Mutant Taq polymerase for faster amplification |
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| MX2022000055A (es) * | 2019-06-28 | 2022-05-30 | Quantum Si Inc | Enzimas de polimerización para reacciones de secuenciación. |
| AU2020364058A1 (en) | 2019-10-11 | 2022-05-26 | Quantum-Si Incorporated | Surface modification in the vapor phase |
| CN115362266A (zh) * | 2020-02-10 | 2022-11-18 | 铂赛基因组学公司 | Phi29突变体及其用途 |
| JP2023554368A (ja) | 2020-12-15 | 2023-12-27 | クアンタム－エスアイ インコーポレイテッド | 単一分子速度論による分子バーコード分析 |
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Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2011040971A2 (en) * | 2009-09-30 | 2011-04-07 | Pacific Biosciences Of California, Inc. | Generation of modified polymerases for improved accuracy in single molecule sequencing |
| US20130217007A1 (en) * | 2012-02-01 | 2013-08-22 | Pacific Biosciences Of California, Inc. | Recombinant Polymerases With Increased Phototolerance |
Family Cites Families (57)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE4435728A1 (de) | 1994-01-19 | 1995-07-20 | Boehringer Mannheim Gmbh | Biotinsilan-Verbindungen und diese Verbindungen enthaltende Bindematrix |
| US5654419A (en) | 1994-02-01 | 1997-08-05 | The Regents Of The University Of California | Fluorescent labels and their use in separations |
| US6248518B1 (en) | 1996-10-29 | 2001-06-19 | Board Of Regents Of University Of Nebraska | Method for detecting point mutations in DNA utilizing fluorescence energy transfer |
| DE19810879A1 (de) | 1998-03-13 | 1999-09-16 | Roche Diagnostics Gmbh | Polymerasenchimären |
| US6153442A (en) | 1998-05-20 | 2000-11-28 | Dade Behring Inc. | Reagents and methods for specific binding assays |
| US6787308B2 (en) | 1998-07-30 | 2004-09-07 | Solexa Ltd. | Arrayed biomolecules and their use in sequencing |
| US6232075B1 (en) | 1998-12-14 | 2001-05-15 | Li-Cor, Inc. | Heterogeneous assay for pyrophosphate detection |
| US6914128B1 (en) | 1999-03-25 | 2005-07-05 | Abbott Gmbh & Co. Kg | Human antibodies that bind human IL-12 and methods for producing |
| US7056661B2 (en) | 1999-05-19 | 2006-06-06 | Cornell Research Foundation, Inc. | Method for sequencing nucleic acid molecules |
| US6869764B2 (en) | 2000-06-07 | 2005-03-22 | L--Cor, Inc. | Nucleic acid sequencing using charge-switch nucleotides |
| US6936702B2 (en) | 2000-06-07 | 2005-08-30 | Li-Cor, Inc. | Charge-switch nucleotides |
| CA2314398A1 (en) | 2000-08-10 | 2002-02-10 | Edward Shipwash | Microarrays and microsystems for amino acid analysis and protein sequencing |
| EP1490483B1 (en) | 2001-04-19 | 2015-06-03 | The Scripps Research Institute | In vivo incorporation of unnatural amino acids |
| US20100035254A1 (en) | 2003-04-08 | 2010-02-11 | Pacific Biosciences Of California, Inc. | Composition and method for nucleic acid sequencing |
| US7745116B2 (en) | 2003-04-08 | 2010-06-29 | Pacific Biosciences Of California, Inc. | Composition and method for nucleic acid sequencing |
| GB0324456D0 (en) | 2003-10-20 | 2003-11-19 | Isis Innovation | Parallel DNA sequencing methods |
| US8637650B2 (en) | 2003-11-05 | 2014-01-28 | Genovoxx Gmbh | Macromolecular nucleotide compounds and methods for using the same |
| US7462452B2 (en) | 2004-04-30 | 2008-12-09 | Pacific Biosciences Of California, Inc. | Field-switch sequencing |
| US7405281B2 (en) | 2005-09-29 | 2008-07-29 | Pacific Biosciences Of California, Inc. | Fluorescent nucleotide analogs and uses therefor |
| DE602006016984D1 (de) | 2005-12-12 | 2010-10-28 | Us Gov Health & Human Serv | Sonde zum sequenzieren von nukleinsäure und verwendungsverfahren |
| CA2633524A1 (en) * | 2005-12-22 | 2007-07-05 | Pacific Biosciences Of California, Inc. | Polymerases for nucleotide analogue incorporation |
| US8084734B2 (en) | 2006-05-26 | 2011-12-27 | The George Washington University | Laser desorption ionization and peptide sequencing on laser induced silicon microcolumn arrays |
| WO2009097368A2 (en) | 2008-01-28 | 2009-08-06 | Complete Genomics, Inc. | Methods and compositions for efficient base calling in sequencing reactions |
| US7968702B2 (en) | 2008-03-13 | 2011-06-28 | Pacific Biosciences Of California, Inc. | Labeled reactants and their uses |
| CN102084001B (zh) | 2008-03-28 | 2015-03-18 | 加利福尼亚太平洋生物科学股份有限公司 | 用于核酸测序的组合物和方法 |
| US9127259B2 (en) * | 2008-03-31 | 2015-09-08 | Pacific Biosciences Of California, Inc. | Enzymes resistant to photodamage |
| US8420366B2 (en) | 2008-03-31 | 2013-04-16 | Pacific Biosciences Of California, Inc. | Generation of modified polymerases for improved accuracy in single molecule sequencing |
| WO2009145818A1 (en) | 2008-03-31 | 2009-12-03 | Pacific Biosciences Of California, Inc | Single molecule loading methods and compositions |
| AU2009251883B2 (en) | 2008-03-31 | 2014-09-11 | Pacific Biosciences Of California, Inc. | Generation of modified polymerases for improved accuracy in single molecule sequencing |
| US8999676B2 (en) | 2008-03-31 | 2015-04-07 | Pacific Biosciences Of California, Inc. | Recombinant polymerases for improved single molecule sequencing |
| US9023633B2 (en) * | 2008-11-03 | 2015-05-05 | Kapa Biosystems | Chimeric DNA polymerases |
| WO2010059206A2 (en) | 2008-11-19 | 2010-05-27 | Pacific Biosciences Of California, Inc. | Modular nucleotide compositions and uses therefor |
| WO2010065322A1 (en) | 2008-12-01 | 2010-06-10 | Research Triangle Institute | Concurrent identification of multitudes of polypeptides |
| KR101063981B1 (ko) | 2009-01-12 | 2011-09-14 | 서강대학교산학협력단 | 자유 라디칼 개시제 및 이를 이용한 펩타이드 서열의 동정방법 |
| DE102009013653B4 (de) | 2009-03-18 | 2014-09-18 | Bruker Daltonik Gmbh | Protein-Sequenzierung mit MALDI-Massenspektrometrie |
| US20100261185A1 (en) | 2009-03-27 | 2010-10-14 | Life Technologies Corporation | Labeled enzyme compositions, methods and systems |
| WO2010117420A2 (en) | 2009-03-30 | 2010-10-14 | Pacific Biosciences Of California, Inc. | Fret-labeled compounds and uses therefor |
| EP3211095B1 (en) | 2009-04-03 | 2019-01-02 | Sequenom, Inc. | Nucleic acid preparation compositions and methods |
| ES2359058B1 (es) * | 2009-07-02 | 2012-03-27 | Consejo Superior De Investigaciones Cient�?Ficas (Csic) | Quimera de adn polimerasa del fago ph1 29. |
| US9566335B1 (en) | 2009-09-25 | 2017-02-14 | The Governing Council Of The University Of Toronto | Protein sequencing method and reagents |
| CA2798635A1 (en) | 2010-05-06 | 2011-11-10 | Ibis Biosciences, Inc. | Integrated sample preparation systems and stabilized enzyme mixtures |
| EP2689028B1 (en) | 2011-03-23 | 2017-08-30 | Pacific Biosciences Of California, Inc. | Isolation of polymerase-nucleic acid complexes and loading onto substrates |
| EP3222627B1 (en) | 2012-02-15 | 2019-08-07 | Pacific Biosciences of California, Inc. | Polymerase enzyme substrates with protein shield |
| US9399766B2 (en) * | 2012-10-01 | 2016-07-26 | Pacific Biosciences Of California, Inc. | Recombinant polymerases for incorporation of protein shield nucleotide analogs |
| US9435810B2 (en) | 2013-03-15 | 2016-09-06 | Washington University | Molecules and methods for iterative polypeptide analysis and processing |
| US9678080B2 (en) | 2013-06-14 | 2017-06-13 | Pacific Biosciences Of California, Inc. | Bis-biotinylation tags |
| US10544449B2 (en) | 2013-06-14 | 2020-01-28 | Pacific Biosciences Of California, Inc. | Bis-biotinylation tags |
| WO2015021079A1 (en) | 2013-08-05 | 2015-02-12 | Pacific Biosciences Of California, Inc. | Protected fluorescent reagent compounds |
| EP3543703A1 (en) | 2014-09-15 | 2019-09-25 | Board of Regents, The University of Texas System | Improved single molecule peptide sequencing |
| EP3258952A4 (en) | 2015-02-04 | 2018-12-05 | Pacific Biosciences Of California, Inc. | Multimeric protected fluorescent reagents |
| EP3371194B1 (en) | 2015-10-16 | 2020-12-30 | Andrew Emili | Protein sequencing method |
| CN108350491A (zh) | 2015-11-18 | 2018-07-31 | 加利福尼亚太平洋生物科学股份有限公司 | 将核酸加载到基材上 |
| US10676788B2 (en) | 2015-11-20 | 2020-06-09 | Pacific Biosciences Of California, Inc. | Modified nucleotide reagents |
| MX2019007248A (es) * | 2016-12-19 | 2019-08-16 | Quantum Si Inc | Enzimas de polimerizacion para reacciones de secuenciacion. |
| JP7418323B2 (ja) | 2017-08-24 | 2024-01-19 | ザ ユナイテッド ステイツ オブ アメリカ， アズ リプレゼンテッド バイ ザ セクレタリー， デパートメント オブ ヘルス アンド ヒューマン サービシーズ | 遠赤および近ｉｒ範囲におけるシアニンフルオロフォアの配座の束縛 |
| US10836798B2 (en) | 2018-11-08 | 2020-11-17 | Government Of The United States Of America, As Represented By The Secretary Of Commerce | Amino acid-specific binder and selectively identifying an amino acid |
| MX2022000055A (es) * | 2019-06-28 | 2022-05-30 | Quantum Si Inc | Enzimas de polimerización para reacciones de secuenciación. |
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| US20130217007A1 (en) * | 2012-02-01 | 2013-08-22 | Pacific Biosciences Of California, Inc. | Recombinant Polymerases With Increased Phototolerance |
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