IL-15 (mutant) (human):Fc (human) (rec.)

The extracellular domain of human IL-15 (aa 20-359) including mutations at Q148D and Q156D is fused at the C-terminus to the Fc portion of human IgG1. Lyophilized from 0.2µm-filtered solution in PBS. This mutant IL-15/Fc fusion protein specifically binds to the IL-15R, competitively inhibits IL-15-triggered cell proliferation, promotes transplant tolerance, does not activate the STAT-signaling pathway, and exerts a prolonged circulating half-life caused by the modified Fc domain. Interleukin-15 (IL-15) has a broad spectrum of biological activities. It is crucial for the development, proliferation, survival and differentiation of multiple cells from both innate and adaptive immune systems. IL-15 up-regulation has a central role in the development of several autoimmune or chronic inflammatory disorders. Targeting IL-15 or its receptor may have a valuable impact on the treatment of immune-mediated diseases. IL-15 participates in the development of important immune antitumor mechanisms. It activates CD8() T cells, natural killer (NK) cells, NK T cells, and can promote the formation of antitumor antibodies. IL-15 can also protect T effector cells from the action of T regulatory cells and reverse tolerance to tumor-associated antigens. In pre-clinical studies IL-15 has been found to demonstrate potentiated antitumor effects following pre-association with IL-15Ralpha, or when used in combination with chemotherapy, adoptive therapy, monoclonal antibodies, and tumor vaccines.