|Detection of IFN‑ gamma R1/CD119 in Human Blood Monocytes by Flow Cytometry. Human peripheral blood monocytes were stained with Mouse Anti-Human IFN‑ gamma R1/CD119 Fluorescein‑conjugated Monoclonal Antibody (Catalog # FAB673F, filled histogram) or isotype control antibody (Catalog # IC002F, open histogram). View our protocol for Staining Membrane-associated Proteins.|
The high-affinity IFN-gamma receptor complex is made up of two type I transmembrane proteins, IFN-gamma R1 (IFN-gamma R alpha ) and IFN-gamma R2 (IFN-gamma R beta ). Both proteins are members of the type II cytokine receptor family and share approximately 52% amino acid sequence identity. IFN-gamma R1 is the ligand-binding subunit that is necessary and sufficient for IFN-gamma binding and receptor internalization. IFN-gamma R2 is required for IFN-gamma signaling but does not bind IFN-gamma by itself. Human IFN-gamma R1 cDNA encodes a 489 amino acid (aa) residue protein with a 17 aa signal peptide, a 228 aa extracellular domain, a 23 aa transmembrane domain, and a 221 aa intracellular domain. Human and mouse IFN-gamma R1 share 52% amino acid sequence identity and bind IFN-gamma in a species-specific manner. IFN-gamma R1 is constitutively expressed in most cell types. Soluble IFN-gamma R1 that binds IFN-gamma has been detected in biological fluids.
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