mouse monoclonal IgG1; GM-CSFRα Antibody (S-50) is an IgG1 κ mouse monoclonal GM-CSFR alpha antibody (also designated CSF2R antibody, Colony Stimulating Factor 2 Receptor Subunit Alpha antibody, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha antibody, Alpha-GM-CSF Receptor antibody, GM-CSF-R-Alpha antibody, CD116 Antigen antibody, GMCSFR-Alpha antibody, GMR-Alpha antibody, AlphaGMR antibody, CDw116 antibody, or GMCSFR antibody) that detects the GM-CSFR alpha protein of mouse, rat and human origin by WB, IP, IF and FCM. GM-CSFRα Antibody (S-50) is available as both the non-conjugated anti-GM-CSFR alpha antibody form, as well as multiple conjugated forms of anti-GM-CSFR alpha antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor® conjugates. The human IL-3, IL-5 and GM-CSF receptors are each composed of both unique α subunits and a common β subunit. 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 (1–5). In contrast, 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. Although neither the murine nor the human β subunit contains tyrosine kinase domains, both activate tyrosine phosphorylation mediated signaling pathways.