Interferons (IFN) are a family of cytokines with potent antiviral, antiproliferative and immunomodulatory properties, classified based on their binding specificity to cell surface receptors (1). Human IFNA2 was originally cloned in the early ‘80s and now more than a dozen closely related IFN alpha subtypes have been identified in both the human and mouse genome, each sharing about 80% amino acid (aa) sequence homology (2-4). Structurally, type I IFNs belong to the class of five helical-bundle cytokines, with the IFNA subtypes containing 2 conserved disulfide bonds (5). The extracellular domain (ECD) of mature human IFNA8, also known as IFN?alpha B2, shares 60% aa sequence identity with mouse homolog. The type I IFNs bind to the interferon alpha receptor (IFNAR), which consists of two subunits: IFNAR1 (alpha-subunit) and IFNAR2 (beta -subunit) (6, 7). Individual IFNA subtypes are known to display unique efficacies to viral protection, and IFNA8 is the most potent IFNA, judging by both antiviral and antiproliferative activities (8). The reason for this higher potency is unstructured tail region of IFNA8 that gains structure during complex formation and might explain the differences in activity between IFNAs (8). IFNA8 has been shown to exhibit antiproliferative and cytotoxic effects on renal cancer cell (RCC) lines and chronic myelogenous leukemia (CML)-derived cell lines (9, 10).