SIL-12 Receptor beta-1 Fc

The IL‐12 structurally related family of heterodimeric proteins plays an important role in activating, regulating, and modulating the immune response. This family of proteins transmits its activity through receptors, which, when stimulated by ligand binding, generally activate JAK proteins that subsequently phosphorylate STAT transcription factors. IL‐12R β‐1 is a single pass membrane protein expressed on T cells, B cells, and NK cells. By itself, IL‐12R β‐1 binds to IL‐12 with low affinity, but when paired with IL‐12R β‐2, forms a high affinity IL‐12 receptor. IL‐12R β‐1 can also pair with IL‐23R to form a high affinity receptor for IL‐23. Recombinant Human sIL‐12 Receptor β‐1 Fc has a calculated molecular weight of 84.3 kDa and contains 758 amino acid residues, which consists of the extracellular domain of IL‐12R β‐1 fused to the Fc portion of human IgG and contains a C‐terminal His‐tag. Due to glycosylation, it migrates at an approximate molecular weight of 116 kDa, under reducing conditions.