il 18 Human

Interleukin 18 (IL-18), also known as interferon-gamma-inducing factor (IGIF), is a proinflammatory cytokine that plays a crucial role in the immune response. IL-18 is produced by various cell types, including macrophages and dendritic cells, in response to infection or injury. Upon secretion, IL-18 binds to its receptor, IL-18R, which is expressed on various immune cells, including T cells and natural killer (NK) cells. This interaction triggers a signaling cascade that leads to the activation and differentiation of these cells. One of the primary functions of IL-18 is to induce the production of interferon-gamma (IFN-γ) from T cells and NK cells. IFN-γ is a potent proinflammatory cytokine that enhances the cytotoxic activity of NK cells and promotes the differentiation of T helper 1 (Th1) cells, both of which are essential for combating intracellular pathogens. IL-18, in conjunction with IL-12, plays a critical role in shaping the immune response towards a Th1 phenotype, which is characterized by the production of IFN-γ and other Th1-associated cytokines. This Th1-polarizing effect is essential for controlling infections caused by intracellular pathogens, such as viruses and certain bacteria. Moreover, IL-18 has been implicated in the pathogenesis of various inflammatory and autoimmune diseases. Elevated levels of IL-18 have been observed in patients with rheumatoid arthritis, Crohn's disease, and multiple sclerosis, suggesting that dysregulated IL-18 signaling may contribute to the chronic inflammation associated with these conditions. IL-18 binding protein (IL-18BP) is a naturally occurring inhibitor of IL-18 that plays a crucial role in regulating IL-18 activity. IL-18BP binds to IL-18 with high affinity, preventing its interaction with IL-18R and subsequent signaling. This inhibitory mechanism helps to control the inflammatory response and prevent excessive IL-18-mediated tissue damage. The balance between IL-18 and IL-18BP is crucial for maintaining immune homeostasis, and dysregulation of this balance has been implicated in various inflammatory and autoimmune disorders.

Interleukin-18 Human Recombinant is a highly purified protein produced in E. coli. It is a single, non-glycosylated polypeptide chain consisting of 157 amino acids, resulting in a molecular weight of 18.2 kDa. This recombinant IL-18 protein is carefully purified using proprietary chromatographic techniques to ensure its high purity and biological activity. As a laboratory reagent, it is a valuable tool for studying the biological activity and signaling pathways of IL-18 in various immunological and cellular processes.

Sterile Filtered White lyophilized (freeze-dried) powder

Lyophilized from a 0.2µm filtered solution in phosphate-buffered saline (PBS) at a pH of 7.0.

Reconstitute the lyophilized Interleukin 18 in sterile PBS at a concentration of 0.1mg/ml. This solution can then be further diluted to desired concentrations in other aqueous solutions.

Lyophilized Interleukin 18 is stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store it desiccated below -18°C. Upon reconstitution, the IL18 solution should be stored at 4°C for up to 7 days. For extended storage, it is advisable to store the reconstituted solution below -18°C. To enhance stability during long-term storage, consider adding a carrier protein such as 0.1% HSA or BSA. It is important to avoid repeated freeze-thaw cycles to maintain protein integrity and activity.

Greater than 95.0% as determined by SDS-PAGE.

IGIF, IL-1g, IL-18, IL1F4, MGC12320, IFN-gamma-inducing factor, Interleukin-1 gamma, IL-1 gamma, Iboctadekin.

Escherichia Coli.

YFGKLESKLS VIRNLNDQVL FIDQGNRPLF EDMTDSDCRD NAPRTIFIIS MYKDSQPRGM AVTISVKCEK ISTLSCENKI ISFKEMNPPD NIKDTKSDII FFQRSVPGHD NKMQFESSSY EGYFLACEKE RDLFKLILKK EDELGDRSIM FTVQNED