|Detection of IL‑12 R beta 1 in Human PBMCs by Flow Cytometry. Human peripheral blood mononuclear cells (PBMCs) treated with 5 μg/mL PHA for 72 hours were stained with Mouse Anti-Human CD3 epsilon PE‑conjugated Monoclonal Antibody (Catalog # FAB100P) and either (A) Mouse Anti-Human IL‑12 R beta 1 APC‑conjugated Monoclonal Antibody (Catalog # FAB839A) or (B) Mouse IgG1 Allophycocyanin Isotype Control (Catalog # IC002A). View our protocol for Staining Membrane-associated Proteins.|
Interleukin12 (IL-12) is a key mediator of cellular-immunity and induces the differentiation of Th1 cells from precursor T helper cells. The biological activities of IL-12 are mediated through the high-affinity receptor complex composed of two subunits designated IL-12 R beta 1 and IL-12 R beta 2. Individually, IL-12 R beta 1 and IL-12 R beta 2 bind IL‑12 with low affinity. Co-expression of both subunits confers high-affinity binding and is required for IL-12 activity. Both IL-12 receptor subunits are type I transmembrane proteins that share similarities with the gp130/G-CSF R subgroup in the cytokine receptor superfamily. IL-12 R beta 1 cDNA encodes a 662 amino acid (aa) protein with a putative 23 aa signal peptide that is cleaved to generate the mature protein with a 522 aa extracellular domain, a 25 aa transmembrane domain and a 92 aa cytoplasmic region. Expression of IL-12 R beta 1 is detected in activated T cells, NK cells and B cells. The expression of IL‑12 R beta 2 is more restricted and appears to be limited to Th2 cells.