|Detection ofIFN‑ gamma R1/CD119 in Mouse Splenocytes by FlowCytometry. CD11b+ mouse splenocyteswere stained with Hamster Anti-Mouse IFN‑ gamma R1/CD119PE‑conjugated Monoclonal Antibody (Catalog # FAB1026P, filledhistogram) or isotype control (open histogram). View our protocol for StainingMembrane-associated Proteins.|
The high-affinity IFN-gamma receptor complex is made up of two type I membrane 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% overall amino acid (aa) sequence identity. IFN-gamma R1 is the ligand-binding subunit that is both 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. Mouse IFN-gamma R1 cDNA encodes a 477 aa residue protein with a 22 aa signal peptide, a 231 aa extracellular domain, a 24 aa transmembrane segment, and a 200 aa intracellular domain. Human and mouse IFN-gamma R1 share 50% amino acid sequence similarity 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. The recombinant soluble IFN-gamma R1 produced at R&D Systems has been shown to bind IFN-gamma with high affinity and is a potent IFN-gamma antagonist.
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