mouse monoclonal IgG1; IL-3Rα Antibody (S-12) is an IgG1 κ mouse monoclonal IL-3R alpha antibody (also designated IL3RA antibody, Interleukin 3 Receptor Subunit Alpha antibody, IL-3 Receptor Subunit Alpha antibody, IL-3R Subunit Alpha antibody, CD123 Antigen antibody, IL-3R-Alpha antibody, IL-3RA or IL3R antibody) that detects the IL-3R alpha protein of human origin by WB, IP and IF. IL-3Rα Antibody (S-12) is available as both the non-conjugated anti-IL-3R alpha antibody form, as well as multiple conjugated forms of anti-IL-3R alpha antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor® conjugates. Interleukin-3, or IL-3, is a pleiotropic cytokine that is primarily secreted by activated T lymphocytes and stimulates the proliferation and differentiation of hematopoietic cells. IL-3 exerts its biological effects through a receptor which consists of a ligand-specific α subunit (IL-3Rα) and a signal transducing β subunit (IL-3Rβ) common to the IL-3/IL-5/GM-CSF receptors. The α subunits are low-affinity ligand-binding proteins while the β subunits do not themselves bind ligand, but are required for high affinity binding by the α subunits. The mouse IL-3 receptor has two distinct β subunits, one that functions only in IL-3-mediated cell signaling and a second that is shared with IL-5 and GM-CSF. The murine β subunits are 91% homologous at the amino acid level but only 56% homologous to the human β subunit. The carboxy-terminus of the β subunit has been shown to be necessary for activation of the MAP kinase signaling pathway. Although the IL-3 receptor has no intrinsic kinase activity, stimulation with IL-3 leads to tyrosine phosphorylation of the JAK/Tyk 2 family member, JAK2, which in turn activates and causes nuclear translocation of Stat5a and Stat5b.