mouse monoclonal IgG2b; IL-2Rβ Antibody (C-2) is an IgG2b κ mouse monoclonal IL-2R beta antibody (also designated IL-2Rβ antibody) that detects the IL-2R beta protein of human origin by WB, IP, IF, IHC(P) and ELISA. IL-2Rβ Antibody (C-2) is available as both the non-conjugated anti-IL-2R beta antibody form, as well as multiple conjugated forms of anti-IL-2R beta antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor® conjugates. The IL-2 receptor is a multicomponent complex consisting of three subunits, α, β and γ, each of which is required for high affinity binding of IL-2. The a chain functions primarily in binding IL-2, whereas the β and γ chains contribute to IL-2 binding and are essential to IL-2-induced activation of signaling pathways leading to T cell growth. Both IL-4R and IL-7R were initially described as single chain high affinity ligand binding cytokine receptors. However, it is now well established that the IL-2R γ chain functions as a second subunit of the high affinity IL-4R and IL-7R receptors. Consequently, the originally described subunits of these latter receptors are now referred to as IL-4Rα and IL-7Rα respectively, while the common subunit is referred to as γc. Although the common γ chain enhances ligand binding in these three cytokine receptors, it has no capacity to bind these ligands on its own. There is evidence that the gc chain is also a subunit of IL-13R.