











Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
447-ML
Formulation | Lyophilized from a 0.2 μm filtered solution in Tris and NaCl with BSA as a carrier protein. |
Reconstitution | Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
447-ML/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in Tris and NaCl. |
Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Recombinant Mouse IL-15 Protein Summary
Product Specifications
Asn49-Ser162, with an N-terminal Met
Analysis

Background: IL-15
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.

