Recombinant Human IL-15R alpha Fc Chimera (HEK293), CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human IL-15R alpha Fc Chimera (HEK293), CF Summary

Details of Functionality
Measured by its ability to block human IL-15-induced proliferation of CTLL‑2 mouse cytotoxic T cells. Ruchatz, H. et al. (1998) J. Immunol. 160:5654.

The ED50 for this effect is 2-10 ng/mL.

Source
Human embryonic kidney cell, HEK293-derived human IL-15 R alpha protein
Human IL-15 R alpha
(Met1-Thr205)
Accession # Q13261
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Ile31
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
IL15RA
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
45 kDa (monomer).
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.
SDS-PAGE
75-90 kDa, reducing conditions
Publications
Read Publications using
7194-IR in the following applications:

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 PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human IL-15R alpha Fc Chimera (HEK293), CF

  • CD215 antigen
  • CD215
  • IL15 R alpha
  • IL-15 R alpha
  • IL-15 receptor subunit alpha
  • IL-15R alpha
  • IL15RA
  • IL-15Ra
  • IL-15R-alpha
  • interleukin 15 receptor, alpha
  • interleukin-15 receptor subunit alpha
  • MGC104179

Background

Interleukin 15 Receptor alpha (IL‑15 R alpha ), also known as CD215, is a widely expressed 60 kDa transmembrane glycoprotein that plays an important role in the homeostasis and activation of NK cells and CD8+ memory T cells and participates in the development and function of many other hematopoietic cell types and non‑immune cell types (1 ‑ 3). Mature human IL‑15 R alpha consists of a 175 aa extracellular domain (ECD) containing one N‑linked glycosylation site, a 23 aa transmembrane segment, and a 39 aa cytoplasmic tail (4). Within the ECD, human IL‑15 R alpha shares approximately 60% aa sequence identity with mouse and rat IL‑15 R alpha . Alternate splicing of human IL‑15 R alpha generates additional isoforms with variable length deletions in the ECD and/or substitutions in the cytoplasmic domain (4, 5). IL‑15 R alpha binds to Interleukin‑15 with high affinity (6). IL‑15 additionally interacts 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 (7, 8). The use of shared receptor components contributes to the overlapping biological effects of IL‑15 and IL‑2. The dominant mechanism of IL‑15 action is known as transpresentation in which IL‑15/IL‑15 R alpha complexes are expressed on the surface of one cell and interact with complexes of IL‑2 R beta / gamma c on adjacent cells (9). This enables cells to respond to IL‑15 even if they do not express IL‑15 R alpha (10 ‑ 12). IL‑15/IL‑15 R alpha complexes can transmit reverse signaling that promotes cellular adhesion, tyrosine phosphorylation of intracellular proteins, and cytokine secretion by the IL‑15/IL‑15 R alpha expressing cells (13, 14). Shed soluble forms of IL‑15 R alpha retain the ability to bind tightly to IL‑15 and can inhibit IL‑15 bioactivity (6, 15, 16).

  1. Ma, A. et al. (2006) Annu. Rev. Immunol. 24:657.
  2. Di Sabatino, A. et al. (2011) Cytokine Growth Factor Rev. 22:19.
  3. Budagian, V. et al. (2006) Cytokine Growth Factor Rev. 17:259.
  4. Anderson, D.M. et al. (1995) J. Biol. Chem. 270:29862.
  5. Dubois, S. et al. (1999) J. Biol. Chem. 274:26978.
  6. Giri, J.G. et al. (1995) EMBO 14:3654.
  7. Grabstein, K. et al. (1994) Science 264:965.
  8. Giri, J. et al. (1994) EMBO J. 13:2822.
  9. Stonier, S.W. and K.S. Schluns (2010) Immunol. Lett. 127:85.
  10. Duitman, E.H. et al. (2008) Mol. Cell. Biol. 28:4851.
  11. Dubois, S. et al. (2002) Immunity 17:537.
  12. Burkett, P.R. et al. (2004) J. Exp. Med. 200:825.
  13. Budagian, V. et al. (2004) J. Biol. Chem. 279:42192.
  14. Neely, G.G. et al. (2004) J. Immunol. 172:4225.
  15. Budagian, V. et al. (2004) J. Biol. Chem. 279:40368.
  16. Mortier, E. et al. (2004) J. Immunol. 173:1681.

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Publications for IL-15R alpha (7194-IR)(3)

We have publications tested in 2 confirmed species: Human, Mouse.

We have publications tested in 4 applications: Bioassay, In Vivo, In vivo assay, Size Exclusion Chromatography.


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(1)
In Vivo
(1)
In vivo assay
(1)
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(1)
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(2)
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(2)
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Bioinformatics

Gene Symbol IL15RA
Uniprot