Recombinant Mouse IL-15 Protein Summary
Details of Functionality |
Measured in a cell proliferation assay using CTLL‑2 mouse cytotoxic T cells. The ED50 for this effect is 2-15 ng/mL. |
Source |
E. coli-derived mouse IL-15 protein Asn49-Ser162, with an N-terminal Met |
Accession # |
|
N-terminal Sequence |
Met |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Il15 |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note |
<1.0 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
13.4 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. |
Publications |
Read Publications using 447-ML in the following applications:
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Packaging, Storage & Formulations
Storage |
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.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in Tris and NaCl with BSA as a carrier protein. |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse IL-15 Protein
Background
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 mouse IL-15 shares 70% and 96% amino acid sequence identity with human and rat IL-15, respectively. IL-15 binds with high affinity to IL‑15 R alpha (3). 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 (4). IL-15 associates with IL-15 R alpha in the endoplasmic reticulum, and this complex is expressed on the cell surface (5). 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 (6). This enables cells to respond to IL-15 even if they do not express IL-15 R alpha (5). 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 (7-9). Soluble IL-15 R alpha functions as an inhibitor that limits IL-15 action (3, 8). 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 (10). IL-15 induces or enhances the differentiation, maintenance, or activation of multiple T cell subsets including NK, NKT, Th17, Treg, and CD8
+ memory cells (11-15). An important component of these functions is the ability of IL-15 to induce dendritic cell differentiation and inflammatory activation (10, 13). IL-15 exhibits anti-tumor activity independent of its actions on NK cells or CD8
+ T cells (16). It also inhibits the deposition of lipid in adipocytes, and its circulating levels are decreased in obesity (17).
- De Sabatino, A. et al. (2011) Cytokine Growth Factor Rev. 22:19.
- Grabstein, K. et al. (1994) Science 264:965.
- 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.
- Mortier, E. et al. (2003) J. Exp. Med. 205:1213.
- Gordy, L.E. et al. (2011) J. Immunol. 187:6335.
- Harris, K.M. (2011) J. Leukoc. Biol. 90:727.
- Xia, J. et al. (2010) Clin. Immunol. 134:130.
- Schluns, K.S. et al. (2002) J. Immunol. 168:4827.
- Davies, E. et al. (2010) J. Leukoc. Biol. 88:529.
- Barra, N.G. et al. (2010) Obesity 18:1601.
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