Mouse IL‑3R alpha/CD123 Biotinylated Antibody

Interleukin 3 (IL-3) is a pleiotropic cytokine produced primarily by activated T cells or mast cells. IL-3 stimulates the proliferation and differentiation of hemopoietic cells including the pluripotent hematopoietic stem cells as well as various lineage-committed cells. The biological effects of IL-3 on the various cell types are mediated by the binding of IL-3 to specific cell surface receptor complexes. The functional high-affinity IL-3 receptor is a heterodimer consisting of a ligand binding alpha subunit and the beta subunit. The alpha subunit alone binds IL-3 with low affinity. The beta subunit is required for the high-affinity binding of IL-3 to the heterodimeric receptor complex. The beta subunit has also been found to be a component of the high-affinity receptor complex for IL-5 and GM-CSF and is also referred to as the beta common ( betac) chain. In the mouse, there are two IL-3 R beta proteins. The first identified mouse IL-3 R beta was also called AIC2A and binds IL-3 with low affinity (1). The second mIL-3 R beta was referred to as AIC2B (2). AIC2B doesn’t bind IL-3 and is the homolog of the human IL-3 R beta. AIC2A was found to be the result of a gene duplication event. The mouse IL-3 R alpha, also called SUT-1, will form complexes with either mouse IL-3 R beta protein (3). Both the alpha and the beta subunits are members of the cytokine receptor superfamily.