IFNGR1 Extracellular Ligand-binding Domain (human, recombinant)

IFNγR1|Immune Interferon Receptor 1|Interferon Gamma Receptor Alpha-chain

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.{53695,23537} 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.{23537} 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.{23537,53696} Ifngr1-/- mice exhibit increased susceptibility to bacterial, parasitic, and viral infections, such as Theiler's murine encephalomyelitis, L. major, L. monocytogenes, and various mycobacteria.{23537,53697} IFNGR1 SNPs have been associated with both increased and decreased susceptibility to pulmonary tuberculosis infection in humans.{53695} IFNGR1 SNPs have also been associated with increased susceptibility to H. pylori infection and increased risk of developing chronic gastritis and gastric carcinomas.{53698} Cayman's 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 Cayman's IFNGR1 Extracellular Ligand-binding Domain (human, recombinant) is 40 kDa due to glycosylation.

-80

-80

Lyophilized from sterile PBS, pH 7.4

365

≥97% estimated by SDS-PAGE