{"id":{"repo_id":"aachen","oai_identifier":"oai:publications.rwth-aachen.de:50183"},"canonical_url":"https://search.dev.ndltd.org/etd/aachen/oai:publications.rwth-aachen.de:50183","repository":{"repo_id":"aachen","name":"RWTH Aachen University","base_url":"https://publications.rwth-aachen.de/oai2d"},"display":{"title":"Herstellung monoklonaler Antikörper gegen YB-1 und Charakterisierung ihrer Bindungseigenschaften","abstract":"Y-box protein-1 (YB-1) belongs to the cold shock protein family. Members of this family are highly conserved in evolution and fulfill numerous functions in gene regulation and mRNA translation. Here, we have successfully generated six distinct anti-YB-1 monoclonal antibodies by immunizing mice with recombinant protein. Two of the six monoclonal antibodies specifically recognize a linear epitope localized between amino acids 146 and 172. Binding experiments with several GFP-YB-1 deletion fragments in ELISA and immunoblots revealed that the other four monoclonal antibodies bind to conformational epitopes. The monoclonal antibodies are suitable to detect YB-1 protein by methodologies, such as ELISA, immunblotting and immunohistochemistry. In the course of anti-Thy1.1-induced mesangioproliferative glomerulonephritis high levels of YB-1 in the extracellular compartment (urine) were associated with severe tubolinterstitial damage. Immunohistochemistry was performed with breast tissue from healthy control patients and breast cancer patients. Here, absent staining for YB-1 in healthy tissue compared to nuclear as well as cytoplasmic staining pattern in breast cancer tissue was apparent.","abstract_html":"Y-box protein-1 (YB-1) belongs to the cold shock protein family. Members of this family are highly conserved in evolution and fulfill numerous functions in gene regulation and mRNA translation. Here, we have successfully generated six distinct anti-YB-1 monoclonal antibodies by immunizing mice with recombinant protein. Two of the six monoclonal antibodies specifically recognize a linear epitope localized between amino acids 146 and 172. Binding experiments with several GFP-YB-1 deletion fragments in ELISA and immunoblots revealed that the other four monoclonal antibodies bind to conformational epitopes. The monoclonal antibodies are suitable to detect YB-1 protein by methodologies, such as ELISA, immunblotting and immunohistochemistry. In the course of anti-Thy1.1-induced mesangioproliferative glomerulonephritis high levels of YB-1 in the extracellular compartment (urine) were associated with severe tubolinterstitial damage. Immunohistochemistry was performed with breast tissue from healthy control patients and breast cancer patients. 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Members of this family are highly conserved in evolution and fulfill numerous functions in gene regulation and mRNA translation. Here, we have successfully generated six distinct anti-YB-1 monoclonal antibodies by immunizing mice with recombinant protein. Two of the six monoclonal antibodies specifically recognize a linear epitope localized between amino acids 146 and 172. Binding experiments with several GFP-YB-1 deletion fragments in ELISA and immunoblots revealed that the other four monoclonal antibodies bind to conformational epitopes. The monoclonal antibodies are suitable to detect YB-1 protein by methodologies, such as ELISA, immunblotting and immunohistochemistry. In the course of anti-Thy1.1-induced mesangioproliferative glomerulonephritis high levels of YB-1 in the extracellular compartment (urine) were associated with severe tubolinterstitial damage. Immunohistochemistry was performed with breast tissue from healthy control patients and breast cancer patients. 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