Production and characterization of monoclonal antibodies against α-globin chain-containing human hemoglobins for detecting α-thalassemia disease
© 2016 Taylor & Francis. Monoclonal antibodies against α-globin containing human Hbs, named AMS-Alpha1 and AMS-Alpha 2, were produced by the hybridoma technique using spleen cells enriched by the newly developed B lymphocyte enrichment protocol. These two monoclonal antibodies were of IgM clas...
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th-cmuir.6653943832-551292018-09-05T03:07:53Z Production and characterization of monoclonal antibodies against α-globin chain-containing human hemoglobins for detecting α-thalassemia disease Kanet Pakdeepak Supansa Pata Sawitree Chiampanichayakul Watchara Kasinrerk Thanusak Tatu Biochemistry, Genetics and Molecular Biology Health Professions Immunology and Microbiology Medicine © 2016 Taylor & Francis. Monoclonal antibodies against α-globin containing human Hbs, named AMS-Alpha1 and AMS-Alpha 2, were produced by the hybridoma technique using spleen cells enriched by the newly developed B lymphocyte enrichment protocol. These two monoclonal antibodies were of IgM class, reacting to only intact form of human Hbs A, A2, E, and F, which contain α-globin chain. By the indirect ELISA, the AMS-Alpha1 and AMS-Alpha 2 quantified less amount of α-globin chain containing hemoglobins in HbH disease than the SEA-α thalassemia 1 carriers and normal individuals. It was thus anticipated that these monoclonal antibodies can be used for detecting Hb Bart’s hydrops fetalis in which no α-globin chain is produced. 2018-09-05T02:52:06Z 2018-09-05T02:52:06Z 2016-11-01 Journal 15324230 15321819 2-s2.0-84987958839 10.1080/15321819.2016.1174135 https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84987958839&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/55129 |
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Biochemistry, Genetics and Molecular Biology Health Professions Immunology and Microbiology Medicine Kanet Pakdeepak Supansa Pata Sawitree Chiampanichayakul Watchara Kasinrerk Thanusak Tatu Production and characterization of monoclonal antibodies against α-globin chain-containing human hemoglobins for detecting α-thalassemia disease |
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© 2016 Taylor & Francis. Monoclonal antibodies against α-globin containing human Hbs, named AMS-Alpha1 and AMS-Alpha 2, were produced by the hybridoma technique using spleen cells enriched by the newly developed B lymphocyte enrichment protocol. These two monoclonal antibodies were of IgM class, reacting to only intact form of human Hbs A, A2, E, and F, which contain α-globin chain. By the indirect ELISA, the AMS-Alpha1 and AMS-Alpha 2 quantified less amount of α-globin chain containing hemoglobins in HbH disease than the SEA-α thalassemia 1 carriers and normal individuals. It was thus anticipated that these monoclonal antibodies can be used for detecting Hb Bart’s hydrops fetalis in which no α-globin chain is produced. |
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Kanet Pakdeepak Supansa Pata Sawitree Chiampanichayakul Watchara Kasinrerk Thanusak Tatu |
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Kanet Pakdeepak Supansa Pata Sawitree Chiampanichayakul Watchara Kasinrerk Thanusak Tatu |
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Kanet Pakdeepak |
title |
Production and characterization of monoclonal antibodies against α-globin chain-containing human hemoglobins for detecting α-thalassemia disease |
title_short |
Production and characterization of monoclonal antibodies against α-globin chain-containing human hemoglobins for detecting α-thalassemia disease |
title_full |
Production and characterization of monoclonal antibodies against α-globin chain-containing human hemoglobins for detecting α-thalassemia disease |
title_fullStr |
Production and characterization of monoclonal antibodies against α-globin chain-containing human hemoglobins for detecting α-thalassemia disease |
title_full_unstemmed |
Production and characterization of monoclonal antibodies against α-globin chain-containing human hemoglobins for detecting α-thalassemia disease |
title_sort |
production and characterization of monoclonal antibodies against α-globin chain-containing human hemoglobins for detecting α-thalassemia disease |
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2018 |
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https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84987958839&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/55129 |
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