Interleukins are immunomodulatory proteins that elicit a wide array of responses in cells and tissues. Interleukin 1 family member 10 (IL1F10, IL 38) is a member of the IL1 family (Lin et al. 2001, Bensen et al. 2001). IL1F10 is produced in Human apoptotic cells (Mora et al. 2016) and human epidermal keratinocytes (based on mRNA studies) (Boutet M A et al. 2016). Like several other IL1 family members, IL1F10 is synthesized as precursors that require N terminal processing to attain full receptor agonist or antagonist function. The N terminal truncation of IL1F10 precursor occurs during apoptosis and the predicted cleavage site is at amino acid 19 (Mora et al. 2016). The proteases from apoptosis are believed to be the responsible for the cleavage process. This truncated form of IL1F10 may undergo additional processing before becoming an active interleukin. This event is a black box because the precise cleavage site of IL1F10 and requirement of additional processing steps are uncertain.