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 alpha subunit (IL-3Ralpha) and a signal transducing beta subunit (IL-3Rbeta) common to the IL-3/IL-5/GM-CSF receptors. The alpha subunits are low-affinity ligand-binding proteins while the beta subunits do not themselves bind ligand, but are required for high affinity binding by the alpha subunits. The mouse IL-3 receptor has two distinct beta 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 beta subunits are 91% homologous at the amino acid level but only 56% homologous to the human beta subunit. The carboxy-terminus of the beta 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.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 96% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000
Application Notes:
CD123 (Q192) polyclonal antibody detects endogenous levels of CD123 protein.
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