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Human IL-18 Recombinant Protein
- Catalog Number:
- RP1360H
- Availability:
- In stock
- Application:
- Cell Culture, ELISA Standard, ELISpot Control, Western Blot Control
- 100% Homology:
- Homo sapiens (human), Pan paniscus (pygmy chimpanzee), Pan troglodytes (chimpanzee)
- Human IL-18 (Interleukin-18) (catalog RP1360H) is a yeast-derived cytokine supplied lyophilized without carrier protein in 10% trehalose; it has no affinity tags and is naturally endotoxin-free, and should be reconstituted in sterile PBS that contains at least 0.1% carrier protein. The protein is ~18.2 kDa, 157 amino acids long (full sequence provided), and >98% pure by SDS-PAGE, with 100% amino-acid homology to human, pygmy chimpanzee, and chimpanzee. Store at -20°C (stable up to twelve months from date of receipt; working aliquots with carrier protein stable ~3 months) and avoid repeated freeze/thaw cycles. Product origin is the USA. It is commonly used to study IL-18 signaling and immune responses (including induction of IFN-γ production, activation of NK cells and T cells, and regulation of inflammatory pathways); typical experimental uses include cell-culture stimulation and activation assays, cytokine signaling studies, ELISA and neutralization assays, flow-cytometry and Western blot controls, and antibody generation/validation. Kingfisher Biotech products are supplied for research applications and are not intended for medicinal, diagnostic, or therapeutic use.
| Amino Acid Sequence | YFGKLESKLS VIRNLNDQVL FIDQGNRPLF EDMTDSDCRD NAPRTIFIIS MYKDSQPRGM AVTISVKCEK ISTLSCENKI ISFKEMNPPD NIKDTKSDII FFQRSVPGHD NKMQFESSSY EGYFLACEKE RDLFKLILKK EDELGDRSIM FTVQNED (157) |
| Endotoxin | Naturally endotoxin-free |
| Storage Conditions | -20°C |
| Molecular Weight | 18.2 kDa |
| Purity | >98% as visualized by SDS-PAGE analysis. |
| Country Of Origin | USA |
- Human IL-18 (Interleukin-18) is a pro-inflammatory cytokine belonging to the IL-1 family that plays a central role in innate and adaptive immune responses. IL-18 is produced primarily by monocytes, macrophages, dendritic cells, epithelial cells, and other tissue-resident cells as an inactive precursor that requires cleavage by caspase-1 following inflammasome activation to become biologically active. Once released, IL-18 stimulates production of interferon-γ (IFN-γ) by T cells and natural killer (NK) cells, thereby promoting Th1-type immune responses and enhancing cell-mediated immunity against intracellular pathogens. IL-18 can also contribute to Th2 or Th17 responses depending on the cytokine milieu. In healthy individuals, circulating IL-18 levels are generally low but detectable; concentrations increase during infection, inflammatory stimulation, and immune activation. Elevated IL-18 has been implicated in autoimmune and inflammatory diseases such as rheumatoid arthritis, systemic lupus erythematosus, inflammatory bowel disease, psoriasis, and adult-onset Still's disease, as well as in sepsis, metabolic syndrome, and certain malignancies. In clinical and translational research, human IL-18 serves as a biomarker of inflammasome activation and immune dysregulation and is being investigated as both a therapeutic target and, in modified forms, as an immunostimulatory agent in cancer immunotherapy.
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