Monoclonal mouse antibodies against camel immunoglobulins (65.11)
| Autor: | Pamela Holzlöhner, Erik Schliebs, Natalia Maier, Friederike Pfister, Jonas Füner, Burkhard Micheel, Katja Heilmann |
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| Rok vydání: | 2011 |
| Předmět: | |
| Zdroj: | The Journal of Immunology. 186:65.11-65.11 |
| ISSN: | 1550-6606 0022-1767 |
| DOI: | 10.4049/jimmunol.186.supp.65.11 |
| Popis: | Camelid antibodies are of special interest because some of them belong to immunoglobulin subclasses (IgG2 and IgG3) which are build up only by heavy chains. To use such antibodies for practical application we need specific identification tools. Immunoglobulins llama (Lama glama) were isolated by Protein G (IgG3 and IgG1) and Protein A (IgG2) sepharose. Fab Fragments were generated from llama IgG1 by papain digestion. Balb/c mice were immunized against the three different IgG subtypes and the Fab fragments and monoclonal antibodies were produce by hybridoma technology. We were hitherto able to obtain the following purified monoclonal antibodies (moAb): - moAb reacting to all subtypes with identical binding strength, - moAb that preferentially bind the conventional IgG1, - moAb that bind only IgG1. All generated monoclonal antibodies react against immunoglobulins from new world (llama and alpaca) and old world camelids (bactrian camel and dromedary) but show no cross reactivity with immunoglobulins from other species (rat, mouse, sheep, rabbit, goat, chicken and human). The monoclonal antibodies are suitable to detect camelid antibodies by enzyme immunoassay (ELISA) but not in western blots, indicating that the binding epitops are discontinuous. The production of monoclonal mouse antibodies binding to camelid heavy chain only antibodies is subject for future experiments. |
| Databáze: | OpenAIRE |
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