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