The human IL-3, IL-5 and GM-CSF receptors are each composed of both unique a subunits and a common ∫ subunit. The a subunits are low affinity ligand binding proteins while the ∫ subunits do not themselves bind ligand, but are required for high affinity binding by the a subunits (1–5). In contrast, 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 (6). The murine ∫-subunits are 91% homologous at the amino acid level but only 56% homologous to the human ∫ subunit (6). Although neither the murine nor the human ∫ subunit contains tyrosine kinase domains, both activate tyrosine phosphorylation mediated signaling pathways (7,8).
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of IL-3/IL-5/GM-CSFR&beta chain of human origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope mapping at the C-terminus of IL-3/IL-5/GM-CSFR&beta of human origin
Tissue Specificity
epitope mapping at the C-terminus of IL-3/IL-5/GM-CSFRβ of human origin