IL-36γ-2

IL1F9; IL-1F9; IL1H1; IL-1H1

IL-36 gamma [previously called 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, IL-36 Ra (IL-1F5), IL-36 alpha (IL-1F6), IL-36 beta (IL-1F8), IL-37 (IL-1F7) and IL-1F10. All family members show a 12 beta-strand, beta-trefoil configuration, and are believed to have arisen from a common ancestral gene. Mouse IL-36 gamma is an 18-22 kDa, 164 amino acid (aa) intracellular and secreted protein that contains no signal sequence, no prosegment and no potential N-linked glycosylation sites. Mouse IL-36 gamma (aa 13-164) shares 58%, 84%, 64% and 60% aa sequence identity with human, rat, equine and bovine IL-36 gamma, respectively, and 23-57% aa sequence identity with other family members. A 193 aa mouse isoform with a 29 aa N-terminal extension has been reported. Highest levels of IL-36 gamma are produced by Langerhans cells, keratinocytes, and stomach Chief cells and parietal cells; these cells contribute to first-line defense against pathogens in the skin, lungs and digestive tract. Its expression is induced by LPS treatment of monocytes, and by IL-alpha / beta, IL-17 or TNF-alpha treatment of keratinocytes and bronchial epithelia. Skin IL-36 gamma expression is increased in contact hypersensitivity and psoriasis. It is elevated in inflammatory disorders of the lung (such as asthma) and viral infections. Lung IL-36 gamma and other IL-36 proteins contribute to neutrophil influx. The receptor for IL-36 gamma is a combination of IL-1 Rrp2, mainly found in epithelia and keratinocytes, and the widely expressed IL-1 RAcP. IL-36 alpha, beta and gamma all activate NF-kappa B and MAPK pathways in an IL-1 Rrp2 dependent manner, and IL-36 gamma induces production of inflammatory cytokines and chemokines such as CXCL8/IL-8. Full-length recombinant IL-36 proteins appear less active than their endogenous counterparts, but trimming of the N-termini enhances their activity.

Approximately 17.3 kDa.

Sterile Filtered White lyophilized (freeze-dried) powder.

> 97% by SDS-PAGE and HPLC analyses.