Human IL-36 gamma/IL-1F9 Antibody

Interleukin-36 gamma (IL-36 gamma) [also named IL-1F9, IL-1 epsilon (epsilon), and IL-1H1] is a member of the IL-1 family, which includes IL-1 beta, IL-1 alpha, IL-1ra, IL-18 and IL-1F5 through F10 (1‑4). All family members show a 12 beta-strand, beta-trefoil configuration, and are believed to have arisen from a common ancestral gene that has undergone multiple duplications (4). IL-36 gamma is synthesized as a 19 kDa, 169 amino acid (aa) protein that contains no signal sequence, no prosegment and no potential N-linked glycosylation site (1, 2, 5). The molecule is secreted when transfected into 293T cells (5). Human to mouse, IL-36 gamma has 53% aa sequence identity. Within the family, IL-36 gamma shares 30%, 23%, 33%, 57%, 35%, 45%, and 32% aa sequence identity with IL-1 ra, IL-1 beta, IL-1F5, F6, F7, F8, and F10, respectively. Cells reported to express IL-36 gamma include Langerhans cells, keratinocytes/stratified squamous epithelium, plus chief cells and parietal cells of the stomach (4, 5). The receptor for IL-36 gamma is reported to be a combination of IL-1 Rrp2 and IL-1 RAcP (6). Recombinant IL-36 gamma, along with IL-36 beta/IL-1F8 and IL-36 alpha/IL-1F6, has been shown to activate the pathway involving NF-kappa B and MAPK in an IL-1 Rrp2 dependent manner.