Human IL-36 alpha/IL-1F6 Biotinylated Antibody

Human interleukin 1 family member #6 [IL-1F6; also FIL-1 epsilon (epsilon)] is a member of the IL-1 family of proteins (1‑3). 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-1F6 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-1F6 has 54% aa identity. Within the family, IL-1F6 is 30% aa identical to IL-1ra, and 27%, 31%, 36%, 46%, 57% and 28% aa identical to IL-1 beta, IL-1F5, F7, F8, F9 and F10, respectively. Cells reported to express IL-1F6 include monocytes, B cells and T cells (1, 4). Notably, IL-1F6 is the only novel IL-1 family member found to be expressed on T-cells. The receptor for IL-1F6 is reported to be a combination of IL-1 Rrp2 and IL-1 RAcP (5). Recombinant
IL‑1F6, along with IL-1F8 and IL-1F9, 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-1F6 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.