Human IL-12 R beta1 Biotinylated Antibody

Interleukin 12 (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 beta1 and IL-12 R beta2. Individually, IL-12 R beta1 and IL-12 R beta2 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 membrane proteins that share similarities with the gp130/G-CSF R subgroup in the cytokine receptor superfamily. IL-12 R beta1 cDNA encodes a 662 amino acid (aa) residue protein with a putative 23 aa residue signal peptide that is cleaved to generate the mature protein with a 522 aa residue extracellular domain, a 25 aa residue transmembrane domain and a 92 aa residue cytoplasmic region. Expression of IL-12 R beta1 has been detected in activated T cells, NK cells and B cells. The expression of IL‑12 R beta2 is more restricted and appears to be limited to Th2 cells.