Human IL‑36 alpha /IL‑1F6 Alexa Fluor™ Plus 488‑conjugated Antibody

Human interleukin 1 family member #6 [IL-1F6; also IL-36 alpha and FIL-1 epsilon (epsilon)] is a member of the IL-1 family of proteins (1‑3, 6). IL-1 family members include IL-1 beta, IL-1 alpha, IL‑1ra, IL-18 and IL-1F5 through F10 (4). All family members show a 12 beta -strand, beta -trefoil configuration, and all family members are believed to have arisen from a common ancestral gene that has undergone multiple duplications (4). IL-36 alpha is synthesized as a 158 amino acid (aa) protein that contains no signal sequence, no prosegment and no potential N-linked glycosylation site(s) (1‑3). It appears to be actively secreted (1). When found in cell lysate, it presents as an 18 kDa monomer (2). Human to mouse, full length IL-36 alpha has 54% aa identity. Within the family, IL-36 alpha is 30% aa identical to IL-1ra, and 27%, 31%, 36%, 46%, 57% and 28% aa identical to IL-1 beta, IL-36Ra, IL-1F7, IL-36 beta, IL-36 gamma, and IL-1F10, respectively. Cells reported to express IL-36 alpha include monocytes, B cells and T cells (1, 4). Notably, IL-36 alpha is the only novel IL-1 family member found to be expressed on T-cells. The receptor for IL-36 alpha is reported to be a combination of IL-1 Rrp2 and IL-1 RAcP (5). Recombinant IL-36 alpha, along with IL-36 beta and IL-36 gamma, has been shown to act as an agonist by activating the pathway involving NF-kappa B and MAPK in an IL-1 Rrp2 dependent manner. This suggests that IL-36 alpha may signal in a similar fashion to IL-1 and IL-18 in having a binding receptor which upon ligation, recruits a second receptor as a signaling component, forming an active heterodimeric receptor complex.