ES2668863T3 - Péptidos, dispositivos y métodos para la detección de anticuerpos de Ehrlichia - Google Patents
Péptidos, dispositivos y métodos para la detección de anticuerpos de Ehrlichia Download PDFInfo
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- ES2668863T3 ES2668863T3 ES13844762.8T ES13844762T ES2668863T3 ES 2668863 T3 ES2668863 T3 ES 2668863T3 ES 13844762 T ES13844762 T ES 13844762T ES 2668863 T3 ES2668863 T3 ES 2668863T3
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- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6854—Immunoglobulins
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- G—PHYSICS
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- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/195—Assays involving biological materials from specific organisms or of a specific nature from bacteria
- G01N2333/29—Assays involving biological materials from specific organisms or of a specific nature from bacteria from Richettsiales (o)
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- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
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| ES2668863T3 (es) | 2012-10-11 | 2018-05-22 | Abaxis, Inc. | Péptidos, dispositivos y métodos para la detección de anticuerpos de Ehrlichia |
| US9194870B2 (en) | 2014-01-21 | 2015-11-24 | Abaxis, Inc. | Peptides, devices, and methods for the detection of Anaplasma antibodies |
| US9442112B2 (en) * | 2014-04-04 | 2016-09-13 | Abaxis, Inc. | Compositions and methods for identifying Ehrlichia species |
| TWI691716B (zh) * | 2014-08-13 | 2020-04-21 | 美商艾巴希斯公司 | 電漿特異性結合搭配物檢定中之信號放大 |
| EP4465021A3 (en) | 2015-08-04 | 2025-02-26 | Zoetis Services LLC | Signal amplification in solution-based plasmonic specific-binding partner assays |
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| KR102486615B1 (ko) | 2017-01-30 | 2023-01-11 | 조에티스 서비시즈 엘엘씨 | 용액-기반 플라스몬 특이적-결합 파트너 검정 및 금속성 나노구조체 |
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Family Cites Families (44)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4366246A (en) | 1977-11-08 | 1982-12-28 | Genentech, Inc. | Method for microbial polypeptide expression |
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| CA2340855A1 (en) | 1998-07-28 | 2000-02-10 | Aquila Biopharmaceuticals, Inc. | Granulocytic ehrlichia genes and uses thereof |
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| US6893640B2 (en) | 1998-09-18 | 2005-05-17 | The Ohio State University Research Foundation | Outer membrane protein of Ehrlichia canis and Ehrlichia chaffeensis |
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| US7888491B2 (en) | 1998-09-18 | 2011-02-15 | The Ohio State University Research Foundation | Outer membrane protein of Ehrlichia canis and Ehrlichia chaffeensis |
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| US7183060B2 (en) | 2005-02-22 | 2007-02-27 | Idexx Laboratories, Inc. | Peptides for detection of antibody to Ehrlichia ewingii |
| US7407770B2 (en) | 2001-01-18 | 2008-08-05 | Idexx Corporation | Compositions and methods for detection of Ehrlichia canis and Ehrlichia chaffeensis antibodies |
| US7087372B2 (en) | 2001-01-18 | 2006-08-08 | Idexx Laboratories, Inc. | Compositions and methods for detection of Ehrlichia canis and Ehrlichia chaffeensis antibodies |
| US20030194756A1 (en) | 2002-04-12 | 2003-10-16 | O'connor Thomas Patrick | Peptides for detection of antibody to Ehrlichia equi |
| CA2442074C (en) | 2001-03-28 | 2014-07-22 | Heska Corporation | Methods of detecting early renal disease in animals |
| US20030129161A1 (en) | 2001-09-17 | 2003-07-10 | Hsien-Jue Chu | Interleukin-12 as a veterinary vaccine adjuvant |
| EP1581638B1 (en) | 2002-11-04 | 2007-09-05 | Research Development Foundation | P153 and p156 antigens for the immunodiagnosis of canine and human ehrlichioses and uses thereof |
| WO2004084841A2 (en) | 2003-03-27 | 2004-10-07 | Heska Corporation | Novel anti-feline albumin antibodies and methods of detecting early renal disease |
| US7304139B2 (en) | 2003-10-28 | 2007-12-04 | University Of Florida Research Foundation, Inc. | Polynucleotides and polypeptides of Anaplasma phagocytophilum and methods of using the same |
| US20050202046A1 (en) | 2004-03-11 | 2005-09-15 | Wyeth | Canine vaccine for protection against ehrlichiosis |
| US20060046310A1 (en) | 2004-08-25 | 2006-03-02 | Zong-Li Xia | Amplification method for solid phase immunoassays |
| US7842473B2 (en) | 2005-04-04 | 2010-11-30 | Idexx Laboratories, Inc. | Ehrlichia canis DIVA (differentiate infected from vaccinated animals) |
| US7842474B2 (en) | 2005-04-04 | 2010-11-30 | Idexx Laboratories, Inc. | Ehrlichia canis DIVA (differentiate infected from vaccinated animals) |
| MX2007016189A (es) | 2005-06-16 | 2008-03-10 | Res Dev Foundation | Ortologos de proteinas inmunoreactivas de ehrlichia canis y e. chaffeensis. |
| US20090176208A1 (en) | 2006-01-04 | 2009-07-09 | Simon Brodie | Methods for detecting, identifying and reporting the presence of animal pathological agents |
| US7776618B2 (en) | 2007-03-01 | 2010-08-17 | Church & Dwight Co., Inc. | Diagnostic detection device |
| US7507789B2 (en) | 2007-04-09 | 2009-03-24 | Idexx Laboratories, Inc. | Detection of Anaplasma platys |
| WO2008137881A2 (en) * | 2007-05-04 | 2008-11-13 | The Ohio State University Research Foundation | Ehrlichia ewingii proteins, nucleic acids, and methods of their use |
| US7964366B2 (en) | 2007-09-21 | 2011-06-21 | Idexx Laboratories, Inc. | Methods and compositions for detection of Ehrlichia chaffeensis (VLPT) |
| CA2700474C (en) | 2007-09-21 | 2016-10-04 | Idexx Laboratories, Inc. | Methods and compositions for detection of ehrlichia chaffeensis (p120) |
| EP3527221B1 (en) | 2007-10-31 | 2022-02-23 | Idexx Laboratories, Inc. | Ehrlichia canis diva (differentiate infected from vaccinated animals) |
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| CN103060468B (zh) | 2013-01-30 | 2014-02-12 | 扬州大学 | 一种埃里希氏菌的荧光定量pcr检测和分型的引物、探针及试剂盒 |
| US9442112B2 (en) | 2014-04-04 | 2016-09-13 | Abaxis, Inc. | Compositions and methods for identifying Ehrlichia species |
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