The GIR-94 antibody recognizes the extracellular region of the alpha chain subunit (80-95 kDa glycoprotein) of the human interferon-γ receptor (IFN-γRα, aka, CD119). The functionally active-form of the human IFN-γ receptor consists of two (or more) subunits, with IFN-γRα responsible for IFN-γ binding and both the IFN-γR α and β chains required for the transduction of biologic responses. The IFN-γ receptor α chain (CD119) is expressed on the surface of most human cells (except mature erythrocytes) including monocytes, macrophages, T cells, B cells, NK cells, neutrophils, fibroblasts, epithelial cells, and endothelium. The ability of this antibody to bind to IFN-γ receptors of species other than human has not been determined. The immunogen used to generate this hybridoma was human IFN-γRα purified from human placenta. The GIR-94 is a non-neutralizing antibody. Human PBMC (Left panel) and red blood cells (Right panel) were isolated by Lymphoprep (Nycomed) density centrifugation. The cells were stained with GIR-94 (1 μg, Cat. No. 558935) followed by biotinylated goat anti- mouse IgG (0.25 μg, Cat. No. 553999) and streptavidin -PE (0.015 μg, Cat No. 554061) in a three-layer staining protocol to amplify immunofluorescent signals. Staining with the GIR-94 antibody (filled histograms) is compared to staining obtained using the secondary antibody alone (open histograms). Histograms in left panel are gated on the lymphocyte population defined by its light scattering characteristics.
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