Recombinant Mouse IL-2, Tag Free

Interleukin 2 (IL-2) is an O-glycosylated four-stranded α-helical bundle cytokine with strong stimulatory activity against antigen-activated T cells. It is expressed by CD4+ and CD8+ T cells, γ-delta T cells, B cells, dendritic cells, and eosinophils. The amino acid sequence homology of mature mouse IL-2 with human and rat IL-2 is 56% and 73%, respectively. It shows heterogeneity specific to strains in the N-terminal region containing polyglutamine stretching. IL-2 in mice and humans exhibits cross-species activity. The IL-2 receptor is composed of three subunits, which are present on the cell surface in different prefabricated complex forms. IL-2Rα at 55 kDa binds specifically to IL-2 with low binding affinity. IL-2Rβ at 75 kDa is also a component of the IL-15 receptor, which binds IL-2 with moderate affinity. The 64 kDa common γ-chain γc/IL-2 R shared with the receptors of IL-4, -7, -9, -15, and -21 does not interact independently with IL-2. Upon binding to ligands, signal transduction is done by IL-2Rβ and γC. IL-2 is known for its autocrine and paracrine activity on T cells. It drives quiescent T cell proliferation and induces the synthesis of IL-2 and IL-2Rα. It promotes T cell homeostasis by promoting Fas-induced death of native CD4+ T cells, rather than activated CD4+ memory lymphocytes. IL-2 plays a central role in the expansion and maintenance of regulatory T cells, although it inhibits the development of Th17-polarized cells. Therefore, IL-2 may be a key cytokine that naturally suppresses autoimmunity.