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 protein shares 70% amino acid sequence identity with
mouse and rat IL-15. Alternative splicing generates isoforms of Interleukin 15
with either a long or short signal peptide (LSP or SSP), and the SSP isoform is
retained intracellularly (3). The IL-15 protein 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 Interleukin 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 protein
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).
De Sabatino, A. et al. (2011) Cytokine Growth Factor Rev. 22:19.
Grabstein, K. et al. (1994) Science 264:965.
Tagaya, Y. et al. (1997) Proc. Natl. Acad. Sci. USA 94:14444.
Giri, J.G. et al. (1995) EMBO J. 14:3654.
Giri, J. et al. (1994) EMBO J. 13:2822.
Dubois, S. et al. (2002) Immunity 17:537.
Castillo, E.F. and K.S. Schluns (2012) Cytokine 59:479.
Budagian, V. et al. (2004) J. Biol. Chem. 279:40368.
Mortier, E. et al. (2004) J. Immunol. 173:1681.
Bergamaschi, C. et al. (2012) Blood 120:e1.
Budagian, V. et al. (2004) J. Biol. Chem. 279:42192.
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