Measured in a cell proliferation assay using MO7e human megakaryocytic leukemic cells. The ED50 for this effect is 0.3-2.6 ng/mL. The specific activity of Recombinant Human IL-15 is approximately 4.5 x 105 U/μg, which is calibrated against recombinant human IL-15 WHO International Standard (NIBSC code: 95/554).
<0.10 EU per 1 μg of the protein by the LAL method.
13 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
>97%, by SDS-PAGE with silver staining.
Reconstitute at 100 μg/mL in sterile PBS.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human IL-15 Protein
Interleukin 15 (IL-15) is a widely expressed 14 kDa cytokine that is structurally and functionally related to IL-2 and plays an important role in many immunological diseases (1, 2). Mature human IL-15 shares 70% amino acid sequence identity with mouse and rat IL-15. Alternative splicing generates isoforms of IL-15 with either a long or short signal peptide (LSP or SSP), and the SSP isoform is retained intracellularly (3). IL-15 binds with high affinity to IL-15 R alpha (4). It binds with lower affinity to a complex of IL-2 R beta and the common gamma chain ( gamma c) which are also subunits of the IL-2 receptor complex (5). IL-15 associates with IL-15 R alpha in the endoplasmic reticulum, and this complex is expressed on the cell surface (6). The dominant mechanism of IL-15 action is known as transpresentation in which IL-15 and IL-15 R alpha are coordinately expressed on the surface of one cell and interact with complexes of IL-2 R beta / gamma c on adjacent cells (7). This enables cells to respond to IL-15 even if they do not express IL-15 R alpha (6). In human and mouse, soluble IL-15-binding forms of IL-15 R alpha can be generated by proteolytic shedding and bind up nearly all the IL-15 in circulation (8-10). Soluble IL-15 R alpha functions as an inhibitor that limits IL-15 action (4, 9). Ligation of membrane-associated IL-15/IL-15 R alpha complexes also induces reverse signaling that promotes activation of the IL-15/IL-15 R alpha expressing cells (11). IL-15 induces or enhances the differentiation, maintenance, or activation of multiple T cell subsets including NK, NKT, Th17, Treg, and CD8+ memory cells (12 - 16). An important component of these functions is the ability of IL-15 to induce dendritic cell differentiation and inflammatory activation (11, 14). IL-15 exhibits anti-tumor activity independent of its actions on NK cells or CD8+ T cells (17). It also inhibits the deposition of lipid in adipocytes, and its circulating levels are decreased in obesity (18).
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