Cayman IFNGR1 Extracellular Ligand-binding Domain (human, recombinant)

The interferon-γ (IFN-γ) receptor is a heterodimeric receptor with roles in innate and adaptive immunity, as well as a wide range of infectious and inflammatory diseases.^, It is composed of two IFNGR1 chains that bind IFN-γ and two non-ligand binding IFNGR2 chains that facilitate signal transduction. IFNGR1 is a transmembrane protein that is composed of an extracellular IFN-γ binding domain and an intracellular domain that contains binding motifs for JAK1 and the transcription factor STAT1, and an isoleucine-leucine sequence at residues 270 and 271 that is required for receptor internalization. Upon INF-γ binding, IFNGR1 is phosphorylated by JAK1 to induce STAT1 recruitment to the receptor, which is then translocated to the nucleus to initiate gene transcription.^, Ifngr1^-/- mice exhibit increased susceptibility to bacterial, parasitic, and viral infections, such as Theilers murine encephalomyelitis, L. major, L. monocytogenes, and various mycobacteria.^, IFNGR1 SNPs have been associated with both increased and decreased susceptibility to pulmonary tuberculosis infection in humans. IFNGR1 SNPs have also been associated with increased susceptibility to H. pylori infection and increased risk of developing chronic gastritis and gastric carcinomas. Caymans IFNGR1 Extracellular Ligand-binding Domain (human, recombinant) can be used for Western blot and cell-based assays. This protein consists of 239 amino acids after removal of the signal peptide and has a calculated molecular weight of 27.3 kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass of Caymans IFNGR1 Extracellular Ligand-binding Domain (human, recombinant) is 40 kDa due to glycosylation.

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