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Production and characterization of four monoclonal antibodies specific for human interferon-alpha-1 and -alpha-2
F Noll1, W Handschack, E Eichmann
1Central Institute of Molecular Biology, Academy of Sciences of GDR, Berlin-Buch.
Four monoclonal antibodies against HuIFN-alpha-1 and -alpha-2 were produced by the lymphocyte hybridoma technique. The screening for monoclonal anti-IFN antibodies was performed by two different procedures permitting the detection of neutralizing and non-neutralizing antibodies. The first antibody screening in the supernatants of hybridoma clones was carried out by an immunodot ELISA using a novel chromogen, 2-bromo-1-naphthol, for the immunoperoxidase reaction. The second screening was performed with a solid-phase bioassay. The monoclonal antibodies IIG11 and IVH2 react specifically with HuIFN-alpha-1 independently of its origin, natural or recombinant. The mAb IIG11 recognizes also an epitope on a 27 kDa interferon, probably HuIFN-alpha-8. The mAb IIG7 binds to HuIFN-alpha-2 only, whereas the mAb IIB2 binds to HuIFN-alpha-2 and also to the 27 kDa interferon and to a 25 kDa interferon, not yet further characterized. These antibodies can be used successfully for immunopurification as well as for quantification of the corresponding interferons.
Four monoclonal antibodies against HuIFN-alpha-1 and -alpha-2 were produced by the lymphocyte hybridoma technique. The screening for monoclonal anti-IFN antibodies was performed by two different procedures permitting the detection of neutralizing and non-neutralizing antibodies. The first antibody screening in the supernatants of hybridoma clones was carried out by an immunodot ELISA using a novel chromogen, 2-bromo-1-naphthol, for the immunoperoxidase reaction. The second screening was performed with a solid-phase bioassay. The monoclonal antibodies IIG11 and IVH2 react specifically with HuIFN-alpha-1 independently of its origin, natural or recombinant. The mAb IIG11 recognizes also an epitope on a 27 kDa interferon, probably HuIFN-alpha-8. The mAb IIG7 binds to HuIFN-alpha-2 only, whereas the mAb IIB2 binds to HuIFN-alpha-2 and also to the 27 kDa interferon and to a 25 kDa interferon, not yet further characterized. These antibodies can be used successfully for immunopurification as well as for quantification of the corresponding interferons.