IL-18/IL-1F4 Protein, Porcine

IL-18/IL-1F4 protein is a pro-inflammatory cytokine that is critical in epithelial barrier repair and coordinates immune responses involving Th1 cells and NK cells. IL-18 binds to IL18R1 and IL18RAP to form a ternary complex that activates NF-κ-B and triggers the synthesis of inflammatory mediators. IL-18/IL-1F4 Protein, Porcine is the recombinant Porcine-derived IL-18/IL-1F4 protein, expressed by E. coli , with tag free. The total length of IL-18/IL-1F4 Protein, Porcine is 157 a.a., with molecular weight of ~18.0 kDa.

IL-18, a pro-inflammatory cytokine, plays a crucial role in epithelial barrier repair and orchestrates polarized immune responses involving T-helper 1 (Th1) cells and natural killer (NK) cells. Upon binding to IL18R1 and IL18RAP, IL-18 forms a signaling ternary complex that activates NF-kappa-B, triggering the synthesis of inflammatory mediators. It synergizes with IL-12 to induce IFNG synthesis in Th1 cells and NK cells. Notably, IL-18 is involved in the transduction of inflammation downstream of pyroptosis, where its mature form is specifically released into the extracellular milieu by passing through the gasdermin-D (GSDMD) pore. At the plasma membrane, IL-18 forms a ternary complex with the ligand-binding receptor subunit IL18R1 and the signaling receptor subunit IL18RAP, initiating intracellular signaling. The interaction with the cargo receptor TMED10 facilitates IL-18's translocation from the cytoplasm into the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) and subsequent secretion.

Porcine

E. coli

Tag Free

O19073 (Y36-N192)

397057  [NCBI]

YFGKLEPKLSIIRNLNDQVLFINQGHQAVFEDMPDSDCSDNAPQTVFIIYMYKDSLTRGLAVTISVQCKKMSTLSCKNKTLSFKEMSPPDNIDDEGNDIIFFQRSVPGHDDKIQFESSLYKGYFLACKKENDLFKLILKEKDECGDKSIMFTVQNKN

Approximately 18.0 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.