Human IL-1 was successfully used to produce an anti-IL-1 mAb. Anti-IL-1 (IgG2a) blocked IL-1-mediated thymocyte and fibroblast proliferation, but did not interfere with the biological effects of other lymphokines, such as IL-2 or IL-3. The antibody immunoprecipitated biosynthetically radiolabeled 33, 17, and 4 kD IL-1. An immunoadsorbent column yielded 20% of initial activity, and upon HPLC size-exclusion chromatography, affinity-purified IL-1 had a molecular mass of approximately 4 kD. These results provide first evidence of a monoclonal anti-IL-1 that reacts with different species of IL-1 and apparently binds to an epitope close to the active site of IL-1. Thus, anti-IL-1 IgG may be very helpful for further investigations of the molecular as well as biological characteristics of IL-1 and related mediators.
Characterization of a monoclonal antibody directed against the biologically active site of human interleukin 1.
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A Köck, M Danner, B M Stadler, T A Luger; Characterization of a monoclonal antibody directed against the biologically active site of human interleukin 1.. J Exp Med 1 February 1986; 163 (2): 463–468. doi: https://doi.org/10.1084/jem.163.2.463
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