Human IFN-gamma  R1/CD119 PE-conjugated Antibody

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.