Product Information
Molecular Weight41580Da
Protein NameInterleukin-3 receptor subunit alpha
Human Gene Id3563
Human Swiss Prot NoP26951
Mouse Swiss Prot NoP26952
SpecificityIL-3Rα Polyclonal Antibody detects endogenous levels of IL-3Rα protein.
FormulationLiquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Concentration1 mg/ml
Storage Stability-20°C/1 year
Other NameIL3RA; IL3R; Interleukin-3 receptor subunit alpha; IL-3 receptor subunit alpha; IL-3R subunit alpha; IL-3R-alpha; IL-3RA; CD123
Observed Band(KD)42
Functiondomain:The box 1 motif is required for JAK interaction and/or activation.,domain:The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.,function:This is a receptor for interleukin-3.,miscellaneous:The gene encoding for this protein is located in the pseudoautosomal region 1 (PAR1) of X and Y chromosomes.,similarity:Belongs to the type I cytokine receptor family. Type 5 subfamily.,subunit:Heterodimer of an alpha and a beta subunit. The beta subunit is common to the IL3, IL5 and GM-CSF receptors.,
Subcellular Locationintracellular,plasma membrane,membrane,integral component of membrane,
ExpressionBrain,Lung,
Backgroundinterleukin 3 receptor subunit alpha(IL3RA) Homo sapiens The protein encoded by this gene is an interleukin 3 specific subunit of a heterodimeric cytokine receptor. The receptor is comprised of a ligand specific alpha subunit and a signal transducing beta subunit shared by the receptors for interleukin 3 (IL3), colony stimulating factor 2 (CSF2/GM-CSF), and interleukin 5 (IL5). The binding of this protein to IL3 depends on the beta subunit. The beta subunit is activated by the ligand binding, and is required for the biological activities of IL3. This gene and the gene encoding the colony stimulating factor 2 receptor alpha chain (CSF2RA) form a cytokine receptor gene cluster in a X-Y pseudoautosomal region on chromosomes X or Y. Alternatively spliced transcript variants encoding distinct isoforms have been found. [provided by RefSeq, Jun 2012],