Recombinant Rat IL-2 Protein

Interleukin-2 (IL-2) is a 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 (1‑3). Mature rat IL-2 shares 66% and 73% amino acid sequence identity with human and mouse IL-2, respectively. The receptor for IL-2 consists of three subunits that are present on the cell surface in varying preformed complexes (4 - 6). 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 (1, 2). It contributes to T cell homeostasis by promoting the Fas-induced death of naïve CD4⁺ T cells but not activated CD4⁺ memory lymphocytes (7). IL-2 plays a central role in the expansion and maintenance of regulatory T cells, although it inhibits the development of Th17 polarized cells (8‑10). Thus, IL-2 may be a key cytokine in the natural suppression of autoimmunity (11, 12).