|Detection of Human IFN‑ alpha / beta R2 by Western Blot. Western blot shows lysates of THP‑1 human acute monocytic leukemia cell line, untreated (-) or treated with PMA. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Human IFN‑ alpha / beta R2 C-Terminus Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7014) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for IFN‑ alpha / beta R2 C-terminus at approximately 58 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.|
IFN-alpha / beta R2 (Interferon alpha/beta receptor 2/IFNAR2; also IFN alpha binding protein) is a 90-102 kDa member of the class II cytokine receptor family of molecules. It is expressed on hematopoietic cells, including T cells, NK cells, B cells and monocytes. It serves as a ligand binding subunit for type I IFN, and generates a functional IFN receptor by complexing with 125 kDa IFNAR1. Multiple type I IFNs signal through this heterodimeric receptor with distinct outcomes. This may be attributable to unique structural conformations created by the Type I IFN:IFNAR1 interaction, or the use of a truncated isoform of IFNAR2. Mature human IFNAR2 is a 489 amino acid (aa) type I transmembrane glycoprotein (aa 27-515). It contains a 217 aa extracellular region (aa 27-243) that contains an Ig-like domain (aa 39-118), a fibronectin type III domain, and a 251 aa cytoplasmic tail. There are two isoform variants. The first is 50-55 kDa in size and contains a 51 aa substitution for aa 281-515. The second is a 40 kDa soluble form that shows a two aa substitution for aa 238-515. IFNAR2 also undergoes proteolysis. Cleavage of the 92 kDa isoform generates a 58 kDa membrane-embedded stub that can be further cleaved into 27-35 kDa fragments that undergo nuclear translocation. Over aa 351-514. human IFNAR2 shares 48% aa identity with mouse IFNAR2.
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