A recombinant partial protein sequence (within amino acids 1-200) from the human protein was used as the immunogen for the Interleukin-1 Receptor Antagonist antibody.
Two forms of interleukin-1, designated IL-1a and IL-1beta, have been described. Although encoded by distinct genes and exhibiting roughly only 25% sequence identity, IL-1a and IL-1beta bind to the same receptor and seem to elicit similar biological responses. IL-1 production is generally thought to be associated with inflammation, but it has also been shown to be expressed during kidney development, thymocyte differentiation and cartilage degradation. IL-1 plays a critical role in the regulation of immune response and inflammation acting as an activator of T and B lymphocytes and natural killer (NK) cells. IL-1 receptor antagonist (IL-1ra) is a cytokine that inhibits IL-1a and IL-1beta binding to interleukin receptors. By neutralizing the activity of IL-1, IL-1ra contributes to the inhibition of the immune and inflammatory responses and has been targeted as a drug for the treatment of severely active rheumatoid arthritis. There are four isoforms of IL-1ra that are produced as a result of alternative splicing events.
