JP2004532028A5 - - Google Patents
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- JP2004532028A5 JP2004532028A5 JP2002582274A JP2002582274A JP2004532028A5 JP 2004532028 A5 JP2004532028 A5 JP 2004532028A5 JP 2002582274 A JP2002582274 A JP 2002582274A JP 2002582274 A JP2002582274 A JP 2002582274A JP 2004532028 A5 JP2004532028 A5 JP 2004532028A5
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- Prior art keywords
- fusion protein
- agt
- label
- protein
- labeled
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
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- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
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- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
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- CPTBDICYNRMXFX-UHFFFAOYSA-N procarbazine Chemical compound CNNCC1=CC=C(C(=O)NC(C)C)C=C1 CPTBDICYNRMXFX-UHFFFAOYSA-N 0.000 description 1
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Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US28276601P | 2001-04-10 | 2001-04-10 | |
| PCT/GB2002/001636 WO2002083937A2 (en) | 2001-04-10 | 2002-04-05 | Methods using o6-alkylguanine-dna alkyltransferases |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2007328757A Division JP4226053B2 (ja) | 2001-04-10 | 2007-12-20 | Ｏ６−アルキルグアニン−ｄｎａアルキルトランスフェラーゼ（ａｇｔ）の使用方法 |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2004532028A JP2004532028A (ja) | 2004-10-21 |
| JP2004532028A5 true JP2004532028A5 (https=) | 2008-10-02 |
| JP4195815B2 JP4195815B2 (ja) | 2008-12-17 |
Family
ID=23083030
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2002582274A Expired - Lifetime JP4195815B2 (ja) | 2001-04-10 | 2002-04-05 | Ｏ６−アルキルグアニン−ｄｎａアルキルトランスフェラーゼ（ａｇｔ）の使用方法 |
| JP2007328757A Expired - Fee Related JP4226053B2 (ja) | 2001-04-10 | 2007-12-20 | Ｏ６−アルキルグアニン−ｄｎａアルキルトランスフェラーゼ（ａｇｔ）の使用方法 |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2007328757A Expired - Fee Related JP4226053B2 (ja) | 2001-04-10 | 2007-12-20 | Ｏ６−アルキルグアニン−ｄｎａアルキルトランスフェラーゼ（ａｇｔ）の使用方法 |
Country Status (14)
| Country | Link |
|---|---|
| US (2) | US7939284B2 (https=) |
| EP (4) | EP1696234B1 (https=) |
| JP (2) | JP4195815B2 (https=) |
| KR (1) | KR20040039194A (https=) |
| CN (2) | CN1975422B (https=) |
| AT (3) | ATE419378T1 (https=) |
| AU (1) | AU2002251257B2 (https=) |
| CA (1) | CA2443570A1 (https=) |
| DE (3) | DE60212642T2 (https=) |
| DK (1) | DK1410023T3 (https=) |
| IL (1) | IL157880A0 (https=) |
| NZ (3) | NZ537939A (https=) |
| WO (1) | WO2002083937A2 (https=) |
| ZA (1) | ZA200307442B (https=) |
Families Citing this family (54)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1717496A (zh) | 2002-10-03 | 2006-01-04 | 洛桑生态综合技术联合公司 | 用o6－烷基鸟嘌呤－dna烷基转移酶标记蛋白 |
| CN1720332A (zh) * | 2002-10-03 | 2006-01-11 | 洛桑生态综合技术联合公司 | O6－烷基鸟嘌呤－dna烷基转移酶的底物 |
| EP2341134B1 (en) | 2003-01-31 | 2014-08-27 | Promega Corporation | Covalent tethering of functional groups to proteins |
| US7429472B2 (en) | 2003-01-31 | 2008-09-30 | Promega Corporation | Method of immobilizing a protein or molecule via a mutant dehalogenase that is bound to an immobilized dehalogenase substrate and linked directly or indirectly to the protein or molecule |
| JP2007509608A (ja) * | 2003-05-23 | 2007-04-19 | ウペエフエル・エコル・ポリテクニック・フェデラル・ドゥ・ローザンヌ | アシル担体タンパク質に基づくタンパク質をラベルするための方法 |
| EP1730298B1 (en) * | 2004-03-02 | 2015-11-11 | EPFL Ecole Polytechnique Fédérale de Lausanne | Specific substrates for o6-alkylguanine-dna alkyltransferase |
| EP1720981A2 (en) | 2004-03-02 | 2006-11-15 | EPFL Ecole Polytechnique Fédérale de Lausanne | Mutants of o6-alkylguanine-dna alkyltransferase |
| US7425436B2 (en) | 2004-07-30 | 2008-09-16 | Promega Corporation | Covalent tethering of functional groups to proteins and substrates therefor |
| US7825096B2 (en) | 2004-09-08 | 2010-11-02 | The United States Of America As Represented By The Department Of Health And Human Services | O6-alkylguanine-DNA alkyltransferase inactivators and beta-glucuronidase cleavable prodrugs |
| US7273714B2 (en) * | 2005-03-11 | 2007-09-25 | Vion Pharmaceuticals, Inc. | Alkylguanyltransferase assays |
| US8178314B2 (en) | 2005-04-27 | 2012-05-15 | Covalys Biosciences Ag | Pyrimidines reacting with O6-alkylguanine-DNA alkyltransferase fusion protein and method for detecting protein |
| FR2890174B1 (fr) | 2005-08-30 | 2009-04-24 | Cis Bio Internat Sa | Procede pour la mise en evidence d'un processus biologique par mesure d'un fret |
| FR2890446B1 (fr) | 2005-09-05 | 2008-04-18 | Cis Bio Internat Sa | Methode de detection d'interaction intracellulaire entre bio-molecules |
| MX2009000044A (es) | 2006-06-30 | 2009-01-23 | Ambit Bios Corp | Etiqueta de acido nucleico detectable. |
| EP2087107A2 (en) | 2006-10-30 | 2009-08-12 | Promega Corporation | Mutant hydrolase proteins with enhanced kinetics and functional expression |
| US7897737B2 (en) | 2006-12-05 | 2011-03-01 | Lasergen, Inc. | 3′-OH unblocked, nucleotides and nucleosides, base modified with photocleavable, terminating groups and methods for their use in DNA sequencing |
| KR101504640B1 (ko) * | 2006-12-05 | 2015-03-20 | 레이저젠, 인코퍼레이티드 | 광절단가능 표지된 뉴클레오티드와 뉴클레오시드, 표지된 뉴클레오티드와 뉴클레오시드, 그리고 ｄｎａ 염기서열분석에서 이들의 이용 방법 |
| EP1978093A1 (en) * | 2007-04-04 | 2008-10-08 | Ecole Polytechnique Fédérale de Lausanne (EPFL) | Method of crosslinking two objects of interest |
| GB0711560D0 (en) * | 2007-06-14 | 2007-07-25 | Innova Biosciences Ltd | Improvements in or relating to production of conjugates |
| ATE522810T1 (de) * | 2007-10-29 | 2011-09-15 | New England Biolabs Inc | Verfahren und zusammensetzungen zum nachweis und zur anreicherung kleiner ziel-rnas |
| EP2093564A1 (en) | 2008-02-25 | 2009-08-26 | Technische Universität Dresden Medizinische Fakultät Carl Gustav Carus | Method for distinguishing secretory granules of different ages |
| NZ590265A (en) | 2008-06-11 | 2012-11-30 | Lasergen Inc | Nucleotides and nucleosides and methods for their use in dna sequencing |
| FR2936245B1 (fr) * | 2008-09-23 | 2012-07-06 | Cis Bio Int | Nouveaux substrats d'o6-alkylguanine-adn alkyltransferase et ses mutants. |
| DE112011100297B4 (de) | 2010-01-20 | 2017-08-24 | New England Biolabs, Inc. | Zusammensetzungen, Verfahren und damit in Zusammenhang stehende Anwendungen zum Spalten modifizierter DNA |
| JP6043288B2 (ja) | 2010-09-15 | 2016-12-14 | エンダセア， インコーポレイテッド | 時間分解蛍光ベースのアッセイによるリポ多糖の測定のための使用方法およびキット |
| WO2013040257A1 (en) | 2011-09-13 | 2013-03-21 | Lasergen, Inc. | 5-methoxy. 3'-oh unblocked, fast photocleavable terminating nucleotides and methods for nucleic acid sequencing |
| BR112014013745B1 (pt) * | 2011-12-09 | 2022-06-14 | Institut Pasteur | Método de teste in vitro, kit de detecção e seu uso, método in vitro de diagnóstico, método de fabricação de kit, e teste de imunosseleção multiplex |
| US9267117B2 (en) | 2012-03-15 | 2016-02-23 | New England Biolabs, Inc. | Mapping cytosine modifications |
| US9708658B2 (en) | 2013-03-19 | 2017-07-18 | New England Biolabs, Inc. | Enrichment of target sequences |
| JP5781589B2 (ja) * | 2013-12-20 | 2015-09-24 | レーザーゲン インコーポレイテッド | 光開裂性標識ヌクレオチドとヌクレオシドおよび標識ヌクレオチドとヌクレオシドならびにｄｎａ配列決定におけるそれらの使用法 |
| WO2016003795A1 (en) | 2014-07-02 | 2016-01-07 | New England Biolabs, Inc. | Universal n-glycan binding reagent |
| WO2016093838A1 (en) | 2014-12-11 | 2016-06-16 | New England Biolabs, Inc. | Enrichment of target sequences |
| CN104844710B (zh) * | 2015-04-13 | 2018-02-02 | 西北大学 | 定向固定化pega复合型树酯的制备方法及应用 |
| US12098215B2 (en) | 2016-06-06 | 2024-09-24 | Northwestern University | Fusion protein construct |
| CN113444046B (zh) | 2016-07-20 | 2023-10-27 | 纳莹(上海)生物科技有限公司 | 一种荧光探针及其制备方法和用途 |
| 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 |
| CN111253417B (zh) * | 2019-09-04 | 2022-03-25 | 大连民族大学 | 一种嘌呤衍生物的合成及应用 |
| EP4069731A4 (en) | 2019-12-03 | 2024-05-29 | Alamar Biosciences, Inc. | Nucleic acid linked immune-sandwich assay (nulisa) |
| WO2021163561A1 (en) | 2020-02-13 | 2021-08-19 | New England Biolabs, Inc. | Variant family d dna polymerases |
| WO2021163559A1 (en) | 2020-02-13 | 2021-08-19 | New England Biolabs, Inc. | Variant family d dna polymerases |
| WO2021183921A1 (en) | 2020-03-12 | 2021-09-16 | New England Biolabs, Inc. | A rapid diagnostic test for lamp |
| CN112010983A (zh) * | 2020-08-11 | 2020-12-01 | 西北大学 | 止咳平喘中药活性成分靶向筛选方法及试剂盒 |
| EP4110945A2 (en) | 2020-08-21 | 2023-01-04 | New England Biolabs, Inc. | A rapid diagnostic test for lamp |
| WO2022250676A1 (en) | 2021-05-27 | 2022-12-01 | New England Biolabs, Inc. | Dnase i variants, compositions, methods, and kits |
| US11993792B2 (en) | 2021-05-27 | 2024-05-28 | New England Biolabs, Inc. | DNase I variants, compositions, methods, and kits |
| WO2023097226A2 (en) | 2021-11-24 | 2023-06-01 | New England Biolabs, Inc. | Double-stranded dna deaminases |
| WO2023197015A1 (en) | 2022-04-08 | 2023-10-12 | New England Biolabs, Inc. | Compositions and analysis of dephosphorylated oligoribonucleotides |
| EP4658673A1 (en) | 2023-02-01 | 2025-12-10 | New England Biolabs, Inc. | Duplex-specific dnases |
| AU2024355570A1 (en) | 2023-10-05 | 2026-04-16 | New England Biolabs, Inc. | Methyl cytosine-selective deaminases and uses thereof |
| WO2025129193A1 (en) | 2023-12-15 | 2025-06-19 | New England Biolabs, Inc. | Glycosyltransferases and related methods |
| WO2025137453A1 (en) | 2023-12-20 | 2025-06-26 | New England Biolabs, Inc. | Compositions, methods, kits, and instruments for analyzing rna structure |
| GB202400129D0 (en) | 2024-01-04 | 2024-02-21 | Cambridge Entpr Ltd | Nucleic acid barcodes |
| WO2025224010A1 (en) | 2024-04-24 | 2025-10-30 | Max-Planck-Gesellschaft zur Förderung der Wissenschaften e. V. | Improved o6-alkylguanine-dna alkyltransferase substrates |
| WO2025227034A1 (en) | 2024-04-26 | 2025-10-30 | New England Biolabs, Inc. | Salt active nuclease compositions and methods |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB9224888D0 (en) * | 1992-11-27 | 1993-01-13 | Univ Singapore | Monoclonal antibody |
| HU217779B (hu) * | 1993-06-08 | 2000-04-28 | Cancer Research Campaign Technology Limited | O6-Helyettesített guaninszármazékok, ezeket tartalmazó gyógyászati készítmények, valamint eljárás e vegyületek előállítására |
| DE19903895A1 (de) * | 1999-02-01 | 2000-08-03 | Kai Johnsson | Selektive Immobilisierung und Nachweis der O·6·-Alkylguanin-DNA-Alkyltransferase in der aktiven Form |
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