Mouse IL-2 Antibody

Interleukin-2 (IL-2) is an O-glycosylated four alpha-helix bundle cytokine that has potent stimulatory activity for antigen-activated T cells. It is expressed by CD4⁺ and CD8⁺ T cells, gamma delta T cells, B cells, dendritic cells, and eosinophils. Mature mouse IL-2 shares 56% and 73% aa sequence identity with human and rat IL-2, respectively. It shows strain-specific heterogeneity in an N-terminal region that contains a poly-glutamine stretch. Mouse and human IL-2 exhibit cross-species activity. The receptor for IL-2 consists of three subunits that are present on the cell surface in varying preformed complexes. The 55 kDa IL-2 R alpha is specific for IL-2 and binds with low affinity. The 75 kDa IL-2 R beta, which is also a component of the IL-15 receptor, binds IL-2 with intermediate affinity. The 64 kDa common gamma chain gammac/IL-2 R gamma, which is shared with the receptors for IL-4, -7, -9, -15, and -21, does not independently interact with IL-2. Upon ligand binding, signal transduction is performed by both IL-2 R beta and gammac. IL-2 is best known for its autocrine and paracrine activity on T cells. It drives resting T cells to proliferate and induces IL-2 and IL-2 R alpha synthesis. It contributes to T cell homeostasis by promoting the Fas-induced death of naïve CD4⁺ T cells but not 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. Thus, IL-2 may be a key cytokine in the natural suppression of autoimmunity.