Recombinant Human IL-15RA&IL-15 Complex (C-Fc)

Description

EnkiLife provides the Recombinant Human IL-15RA&IL-15 Complex (C-Fc) protein,aslo know as IL-15 Receptor alpha & IL-15 Fusion Protein,IL15RA&IL15,IL15RA&IL15 Complex, Interleukin-15,IL-15,IL15, which features high purity, high activity, and high stability. It can be applied in scientific research, biopharmaceuticals, and other fields.Purity:Greater than 95% as determined by reducing SDS-PAGE;Endotoxin Level:<1 EU/µg as determined by LAL test.;Construction:Recombinant Human Interleukin-15 Receptor Alpha & Interleukin-15 Fusion Protein Complex is produced by our Mammalian expression system and the target gene encoding Ile31-Asp96&Asn49-Ser162 (Asn120Asp) is expressed with a human IgG1 Fc tag at the C-terminus.Accession:Q13261&P40933. Expression Host:Human Cells.Species:Human.Predicted Molecular Mass:34.4&12.8 KDa. Background:IL15RA is a high-affinity receptor for interleukin-15. Il15ra associates as a heterotrimer with the IL-2 receptor beta and gamma subunits to initiate signal transduction. It can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells. Il15ra is expressed in special cells including a wide variety of Tand B cells and non-lymphoid cells.IL-15 is a cytokine that regulates T cell and natural killer cell activation and proliferation. IL-15 binds to the alpha subunit of the IL-15RA with high affinity. IL-15 also binds to the beta and gamma chains of the IL-2 receptor, but not the alpha subunit of the IL2 receptor. IL-15 is structurally and functionally related to IL-2. Both cytokines share some subunits of receptors, allowing them to compete for and negatively regulate each others activity. The number of CD8+ memory T cells is controlled by a balance between IL-15 and IL-2. Despite their many overlapping functional properties, IL-2 and IL-15 are, in fact, quite distinct players in the immune system. IL-15 is constitutively expressed by a wide variety of cell types and tissues, including monocytes, macrophages and DCs. The enhanced activity of the IL-15N72D:IL-15RαSu/Fc complex is likely the result of the increased binding activity of IL-15N72D to IL-15Rβγ c , optimized cytokine trans-presentation by the IL-15RαSu domain, the dimeric nature of the cytokine domain and its increased in vivo half-life compared to IL-15. These findings indicate that this IL-15 superagonist complex could serve as a superior immunostimulatory therapeutic agent.