caa a22 4500 469090588 CHVBK 20180323133016.0 cr unu---uuuuu 170328e19920201xx s 000 0 eng 10.1007/BF00788749 doi (NATIONALLICENCE)springer-10.1007/BF00788749 Development and characterization of a panel of monoclonal antibodies against the catalytic domain of the human fes proto-oncogene product [Elektronische Daten] [Adrie van Bokhoven, Hans van Duijnhoven, Manfred Jücker, Anton Roebroek, Wim van de Ven] In developing monoclonal antibodies (Moabs) against the humanfes proto-oncogene product, recombinant DNA technology was used to target reactivity of the Moabs towards the catalytic domain of it. Therefore, sequences of humanfes exons 15-19 encoding amino acid residues 612 to 822 which harbor the catalytic domain except the presumed ATP-binding region, were fused in phase to the bacterialtrp E gene which encodes anthranilate synthase. After partial purification of it, the bacterially produced hybrid product of thistrp E-δfes fusion gene was used as immunogen. A series of twelve mouse Moabs was obtained which recognized the human p92fes protein and the viral oncogene product p85gag-fes encoded by the Snyder-Theilen strain of feline sarcoma virus. Reactivity appeared to be directed towards the catalytic domain of the humanfes proto-oncogene product. This was demonstrated by in vitro transcription and translation experiments using humanfes coding sequences from exons 16-19. Upon testing their functional activity in divers immunological techniques, the whole panel of Moabs appeared to be useful in immunoprecipitation, Western blot and immunohistochemical analysis. Immunocytochemical analysis indicated that p85gag-fes is predominantly a cytoplasmic protein. Kluwer Academic Publishers, 1992 fes proto-oncogen nationallicence tyrosine-specific protein kinase nationallicence monoclonal antibody nationallicence van Bokhoven Adrie Molecular Oncology Section; Department of Biochemistry, University of Nijmegen, Nijmegen, The Netherlands aut van Duijnhoven Hans Molecular Oncology Section; Department of Biochemistry, University of Nijmegen, Nijmegen, The Netherlands aut Jücker Manfred Medizinische Klinik, Universität Köln, Germany aut Roebroek Anton Laboratory for Molecular Oncology, Center for Human Genetics, University of Leuven, Herestraat 49, B-3000, Leuven, Belgium aut van de Ven Wim Molecular Oncology Section; Department of Biochemistry, University of Nijmegen, Nijmegen, The Netherlands aut Molecular Biology Reports Kluwer Academic Publishers 16/1(1992-02-01), 17-25 0301-4851 16:1<17 1992 16 11033 https://doi.org/10.1007/BF00788749 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00788749 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- van Bokhoven Adrie Molecular Oncology Section; Department of Biochemistry, University of Nijmegen, Nijmegen, The Netherlands aut NATIONALLICENCE 700 1- van Duijnhoven Hans Molecular Oncology Section; Department of Biochemistry, University of Nijmegen, Nijmegen, The Netherlands aut NATIONALLICENCE 700 1- Jücker Manfred Medizinische Klinik, Universität Köln, Germany aut NATIONALLICENCE 700 1- Roebroek Anton Laboratory for Molecular Oncology, Center for Human Genetics, University of Leuven, Herestraat 49, B-3000, Leuven, Belgium aut NATIONALLICENCE 700 1- van de Ven Wim Molecular Oncology Section; Department of Biochemistry, University of Nijmegen, Nijmegen, The Netherlands aut NATIONALLICENCE 773 0- Molecular Biology Reports Kluwer Academic Publishers 16/1(1992-02-01), 17-25 0301-4851 16:1<17 1992 16 11033 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer