ES2596952T3 - Péptidos, dispositivos y procedimientos para la detección de anticuerpos de Ehrlichia - Google Patents
Péptidos, dispositivos y procedimientos para la detección de anticuerpos de Ehrlichia Download PDFInfo
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- ES2596952T3 ES2596952T3 ES10832262.9T ES10832262T ES2596952T3 ES 2596952 T3 ES2596952 T3 ES 2596952T3 ES 10832262 T ES10832262 T ES 10832262T ES 2596952 T3 ES2596952 T3 ES 2596952T3
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- G01N33/569—Immunoassay; Biospecific binding assay; Materials therefor for microorganisms, e.g. protozoa, bacteria, viruses
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- C07—ORGANIC CHEMISTRY
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- G—PHYSICS
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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
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
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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
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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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| 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 |
| CN104360058A (zh) * | 2014-08-18 | 2015-02-18 | 石河子大学 | 一种新型检测人布鲁氏菌病抗体的免疫层析试纸及制备方法 |
| JP6944438B2 (ja) | 2015-08-04 | 2021-10-06 | ゾエティス サービシズ リミテッド ライアビリティ カンパニー | 溶液ベースのプラズモン特異的結合パートナーアッセイにおけるシグナル増幅 |
| CN118275398A (zh) | 2017-01-30 | 2024-07-02 | 硕腾服务有限责任公司 | 基于溶液的等离子体振子特异性结合配偶体测定和金属纳米结构 |
| JP2018128408A (ja) * | 2017-02-10 | 2018-08-16 | 東ソー株式会社 | 抗体凝集体形成予測方法 |
| US20180287426A1 (en) * | 2017-03-30 | 2018-10-04 | Qualcomm Incorporated | Wireless power time division transmitter and coil array |
| US20190309422A1 (en) | 2018-04-06 | 2019-10-10 | Versum Materials Us, Llc | Spin-On Metallization |
| MX2023003961A (es) * | 2020-10-08 | 2023-06-02 | Controlpoint Inc | Metodos y aparatos para detectar infecciones respiratorias. |
| CN112521463B (zh) * | 2020-12-14 | 2023-08-04 | 杭州亿米诺生物科技有限公司 | 一种犬埃里希体MAP2-P30-gp19重组蛋白及其制备方法和应用 |
| EP4220166A1 (en) | 2022-02-01 | 2023-08-02 | Universitat Rovira I Virgili (URV) | In vitro method for detecting antibodies in a sample |
Family Cites Families (36)
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| US4366246A (en) | 1977-11-08 | 1982-12-28 | Genentech, Inc. | Method for microbial polypeptide expression |
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| US6207169B1 (en) | 1997-03-21 | 2001-03-27 | Corixa Corporation | Compounds and methods for the diagnosis and treatment of Ehrlichia infection |
| ATE438657T1 (de) | 1997-04-25 | 2009-08-15 | Antigenics Inc | Charakterisierung von granulozytischer ehrlichia und methoden für ihre verwendung. |
| CA2304256C (en) | 1997-09-19 | 2014-12-09 | Yasuko Rikihisa | Outer membrane protein of ehrlichia canis and ehrlichia chaffeensis |
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| US7087372B2 (en) * | 2001-01-18 | 2006-08-08 | Idexx Laboratories, Inc. | Compositions and methods for detection of Ehrlichia canis and Ehrlichia chaffeensis antibodies |
| EP1384075B1 (en) | 2001-03-28 | 2009-12-16 | 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 |
| CN100386430C (zh) * | 2002-11-04 | 2008-05-07 | 研究发展基金会 | 用于犬和人埃利希病的免疫诊断的p153和p156抗原及其用途 |
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| 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 |
| US20060046310A1 (en) | 2004-08-25 | 2006-03-02 | Zong-Li Xia | Amplification method for solid phase immunoassays |
| US7842474B2 (en) | 2005-04-04 | 2010-11-30 | Idexx Laboratories, Inc. | Ehrlichia canis DIVA (differentiate infected from vaccinated animals) |
| EP3527582B1 (en) | 2005-04-04 | 2022-08-17 | IDEXX Laboratories, Inc. | Ehrlichia canis diva (differentiate infected from vaccinated animals) |
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| 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 |
| US8784828B2 (en) | 2007-05-04 | 2014-07-22 | The Ohio State University Research Foundation | Ehrlichia ewingii proteins, nucleic acids, and methods of their use |
| JP2011501653A (ja) | 2007-09-21 | 2011-01-13 | アイデックス ラボラトリーズ インコーポレイテッド | エーリキア・シャフェンシス（ＥｈｒｌｉｃｈｉａＣｈａｆｆｅｅｎｓｉｓ）（ＶＬＰＴ）の検出のための方法および組成物 |
| WO2009039413A2 (en) | 2007-09-21 | 2009-03-26 | Idexx Laboratories, Inc. | Methods and compositions for detection of ehrlichia chaffeensis (p120) |
| EP2215477B1 (en) | 2007-10-31 | 2019-01-16 | IDEXX Laboratories Inc | Ehrlichia canis diva (differentiate infection from vaccinated animals) |
| WO2011063235A2 (en) | 2009-11-20 | 2011-05-26 | Abaxis, Inc. | Peptides, devices, and methods for the detection of ehrlichia antibodies |
| AU2013329025B2 (en) | 2012-10-11 | 2019-07-04 | Zoetis Services Llc | Peptides, devices, and methods for the detection of Ehrlichia antibodies |
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| EP2501718A2 (en) | 2012-09-26 |
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