Human IL-15Rα sushi

Human IL-15Rα sushi

IL-15Rα sushi stands for recombinant human interleukin 15 receptor alpha, soluble sushi domain. It is composed of the extracellular sushi domain of IL-15Rα plus a natural hinge domain, and it is a high affinity agonist of IL-15 in culture, maintaining the natural biological effect of soluble IL-15Rα. Human IL-15Rα sushi is a recombinant protein optimized for use in cell culture, differentiation studies, and functional assays.

Applications

Human IL-15Rα sushi can be used for a variety of applications, including:
  • In vitro activation and expansion of memory and naive CD8+ T cells, NK cells, and NKT cells in combination with IL-15
  • Study of IL-15/IL-2 receptor signaling
  • Investigation of new potential adjuvants for vaccine studies

Background information

IL-15Rα is a subunit of the IL-15 receptor together with IL-2Rβ (CD122) and IL-2Rγ (CD132), two subunits shared with IL-2 receptor. A soluble form of IL-15Rα, including the extracellular sushi domain, is naturally released by antigen-presenting cells
in vivo
. Soluble IL-15Rα binds with high affinity IL-15 and acts as IL-15 antagonist through the prevention of IL-15 binding on its α/β/γ receptor. However, on lymphocytes that express only the heterodimeric IL-2Rβ/γ receptor, IL-15Rα presents IL-15
in trans
to the IL-2Rβ/γ receptor, and enhances the effects of IL-15, increasing lymphocyte proliferation and survival. Recombinant Human IL-15Rα sushi is composed of the extracellular sushi domain of IL-15Rα plus a natural hinge domain, and it is a high affinity agonist of IL-15 in culture, maintaining the natural biological effect of soluble IL-15Rα.

Quality description

Research-grade
cytokines are suitable for a wide variety of cell culture applications. They are sterile-filtered prior to lyophilization. Generally, endotoxin levels are <0.1 ng/μg (<1 EU/μg), and purities are >95%. The biological activity is tested in appropriate bioassays.
Premium-grade
cytokines offer the convenience of high and well-defined biological activities and allow exact unit dosing for demanding applications. The biological activity is determined after lyophilization and reconstitution, and normalized to WHO/NIBSC standards whenever available. In general, endotoxin levels are <0.01 ng/μg (<0.1 EU/μg), and purities are >97%. Lot-specific certificates of analysis are available on request (macstec@miltenyibiotec.de).

Biological activity

  • Proliferation of CTLL-2 cells
  • premium grade: ≥ 5×
    10
    5
    U/mg
  • research grade: ≥ 3×
    10
    5
    U/mg
  • Selected references

    1. Soman, G. et al. (2009) MTS dye based colorimetric CTLL-2 cell proliferation assay for product release and stability monitoring of interleukin-15: assay qualification, standardization and statistical analysis. J. Immunol. Methods 348: 83-94
    2. Mortier, E. et al. (2006) Soluble interleukin-15 receptor α (IL-15Rα)-sushi as a selective and potent agonist of IL-15 action through IL-15Rβ/γ: hyperagonist IL-15×IL-15Rα fusion proteins. J. Biol. Chem. 281: 1612-1619
    3. Bouchaud, G. et al. (2008) The exon-3-encoded domain of IL-15Rα contributes to IL-15 high-affinity binding and is crucial for the IL-15 antagonist effect of soluble IL-15Rα. J. Mol. Biol. 382(1): 1-12
    4. Wu, J. (2013) IL-15 agonists: The cancer cure cytokine. J. Mol. Genet. Med. 7(4): 85
Product options: 5
130-104-919

Human IL-15Rα sushi, research grade

E. coli
10 µg
-
130-104-920

Human IL-15Rα sushi, research grade

E. coli
25 µg
-
130-104-912

Human IL-15Rα sushi, premium grade

E. coli
10 µg
-
130-104-916

Human IL-15Rα sushi, premium grade

E. coli
25 µg
-
130-104-914

Human IL-15Rα sushi, premium grade

E. coli
100 µg
-