Interleukin 15 (IL-15), encoded by the IL-15 gene, is a member of the family of four alpha-helical bundles of cytokines. The primary mechanism of action of IL-15 appears to be juxtacrine signaling determined by cell-cell contacts. This role also includes endocrine and reverse signaling. IL-15 was initially characterized as a soluble molecule, but it was later found that the major form of IL-15 protein is the membrane-bound form, which can be directly bound to the cell membrane or presented by the IL-15Rα receptor. The IL-15 receptor consists of three subunits: IL-15Rα, CD122, and CD132. CD122 and CD132 are shared with the IL-2 receptor, and there is actually an additional subunit (CD25). The shared subunits contain cytoplasmic motifs required for signal transduction that underlie many of the overlapping biological activities of IL-15 and IL-2. IL-15Rα is a subunit that specifically binds IL-15 with very high affinity and can bind IL-15 independently of other subunits. This property suggests that IL-15 is able to transmit signals between multiple cells.
This product is designed as a tool for the delivery and expression of IL-15-IL15Rα mRNA for research. The product leverages the lipid nanoparticle (LNP) technology platform for simple and efficient delivery of IL-15-IL15Rα mRNA to a variety of mammalian cells in vitro and in vivo. The LNPs used are formulated with SM-102, DSPC, cholesterol and DMG-PEG2000 at an optimal molar concentration for a high rate of encapsulation and efficient mRNA delivery. The IL-15-IL15Rα fusion protein is approximately 59 kD, consisting of full-length human IL-15 (162 amino acids) and IL15Rα (353 amino acids) with 15-residue peptide linker GGGGSGGGGSGGGGS between them. The GenPept accession numbers for IL-15 and IL15Rα are NP_000576 and NP_001243694 respectively.