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Updated: Sep 2, 2026

An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions
Published on: March 14, 2016
Monoclonal anti-IL 1 is directed against a common site of human IL 1 alpha and IL 1 beta
Cytokines exhibiting interleukin 1 (IL 1) activity are known as important mediators of immunity and inflammation. Therefore, the ability of a monoclonal anti-IL 1 antibody to neutralize and bind IL 1 was investigated. Anti-IL 1 IgG blocked the IL 1-mediated thymocyte and fibroblast proliferation and also inhibited the biological activity of epidermal cell-derived thymocyte activating factor (ETAF), but did not affect interleukin 2 (IL 2) and interleukin 3 (IL 3) activity. Monoclonal anti-IL 1 blocked the activity and bound to both human IL 1 alpha and IL 1 beta. Additionally using anti-IL 1, it was possible to immunoprecipitate 31 kD, 17 kD and 4 kD biosynthetically radiolabeled biologically active species of IL 1. These data indicate that IL 1 alpha and IL 1 beta share a common site which is responsible for the biological activity. Moreover, this part of the IL 1 molecule also appears to be located within the low mw 4 kD break-down product. Since anti-IL 1 also was capable to detect surface bound IL 1 on LPS-stimulated mononuclear adherent cells, the antibody may help to elucidate the role of surface IL 1 during an immune response. In addition, anti-IL 1 IgG may be very helpful to investigate the in vivo role of IL 1 during the pathogenesis of inflammatory diseases.
Cytokines exhibiting interleukin 1 (IL 1) activity are known as important mediators of immunity and inflammation. Therefore, the ability of a monoclonal anti-IL 1 antibody to neutralize and bind IL 1 was investigated. Anti-IL 1 IgG blocked the IL 1-mediated thymocyte and fibroblast proliferation and also inhibited the biological activity of epidermal cell-derived thymocyte activating factor (ETAF), but did not affect interleukin 2 (IL 2) and interleukin 3 (IL 3) activity. Monoclonal anti-IL 1 blocked the activity and bound to both human IL 1 alpha and IL 1 beta. Additionally using anti-IL 1, it was possible to immunoprecipitate 31 kD, 17 kD and 4 kD biosynthetically radiolabeled biologically active species of IL 1. These data indicate that IL 1 alpha and IL 1 beta share a common site which is responsible for the biological activity. Moreover, this part of the IL 1 molecule also appears to be located within the low mw 4 kD break-down product. Since anti-IL 1 also was capable to detect surface bound IL 1 on LPS-stimulated mononuclear adherent cells, the antibody may help to elucidate the role of surface IL 1 during an immune response. In addition, anti-IL 1 IgG may be very helpful to investigate the in vivo role of IL 1 during the pathogenesis of inflammatory diseases.
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