IL-2 (human):Fc (human) (rec.) (non-lytic) MultiPack

The extracellular domain of human IL-2 (aa 21-153) is fused at the C-terminus to the Fc portion of a mutant human IgG1. Lyophilized from 0.2µm-filtered solution in PBS. Shows the biological function of the IL-2 moiety and exerts a prolonged circulating half-life caused by the modified Fc domain. Interleukin-2 (IL-2) is a 133 amino acid glycoprotein with one intramolecular disulfide bond and variable glycosylation. It is secreted by activated T cells and induces proliferation and maturation of activated T cells, natural killer cells, and lymphokine activated killer cells. IL-2 also stimulates proliferation of antibody-producing B cells, activates neutrophils, and induces mononuclear cells to secrete IFN-gamma and TNF-alpha and -beta. Moreover, studies have shown that IL-2 is required for activation-induced apoptosis, an important hemeostatic mechanism in the immune system, which is involved in the maintenance of peripheral tolerance to self-antigens.