Recombinant Human IL-15 R alpha Fc Chimera Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human IL-15 R alpha Fc Chimera Protein, CF Summary

Additional Information
New IL-15 Ra Available! ~2x better activity; HEK293 expressed; Lower endotoxin spec; No His-tag!
New Product 7194-IR
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 0.005‑0.015 µg/mL.
Source
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human IL-15 R alpha protein
Human IL-15 R alpha
(Ile31-Thr172)
Accession # EAW86418
IEGRDMD Human IgG1
(Pro100-Lys330)
6-His tag
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
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
42.6 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
51-64 kDa, reducing conditions
Publications
Read Publications using
147-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 sterile PBS.

Notes

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

Alternate Names for Recombinant Human IL-15 R alpha Fc Chimera Protein, CF

  • CD215 antigen
  • CD215
  • IL-15 R alpha
  • IL-15 receptor subunit alpha
  • IL15R 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), 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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Applications: Bioactivity

Publications for IL-15 R alpha (147-IR)(4)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 1 application: Bioassay.


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Bioassay
(4)
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(4)
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Bioinformatics

Gene Symbol IL15RA
Entrez
Uniprot