epitope corresponding to amino acids 17-210 mapping within an N-terminal extracellular domain of IL-3Rα of mouse origin
Modification Notes
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 å subunit (IL-3Rå) and a signal transducing ∫ subunit (IL-3R∫) common to the IL-3/IL-5/GM-CSF receptors. The å subunits are low-affinity ligand-binding proteins while the ∫ subunits do not themselves bind ligand, but are required for high affinity binding by the å subunits. The mouse IL-3 receptor has two distinct ∫ 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 ∫ subunits are 91% homologous at the amino acid level but only 56% homologous to the human ∫ subunit. The carboxy-terminus of the ∫ 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.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of IL-3Rα of mouse and rat origin by WB, IP, IF and ELISA:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 17-210 mapping within an N-terminal extracellular domain of IL-3R&alpha of mouse origin
Tissue Specificity
epitope corresponding to amino acids 17-210 mapping within an N-terminal extracellular domain of IL-3Rα of mouse origin