Abnormal activation and cytokine spectra in lymph nodes of people chronically infected with HIV-1.
Authors: Biancotto A, Grivel JC, Iglehart SJ, Vanpouille C, Lisco A, Sieg SF, Debernardo R, Garate K, Rodriguez B, Margolis LB, Lederman MM
Blood, 2007;109(10):4272-9.
Species: Human
Sample Type: Cell Culture Supernates
Application: Luminex Development
Marked differences in human melanoma antigen-specific T cell responsiveness after vaccination using a functional microarray.
Authors: Chen DS, Soen Y, Stuge TB
PLoS Med., 2005;2(10):e265.
Species: Human
Sample Type: Whole Cells
Application: functional microarray
IL-21 sustains CD28 expression on IL-15-activated human naive CD8+ T cells.
Authors: Alves NL, Arosa FA, van Lier RA
J. Immunol., 2005;175(2):755-62.
Species: Human
Sample Type: Whole Cells
Application: Flow
Renal cells express a functional interleukin-15 receptor.
Authors: Tejman-Yarden N, Zlotnik M, Lewis E, Etzion O, Chaimovitz C, Douvdevani A
Nephrol. Dial. Transplant., 2005;20(3):516-23.
Species: Human
Sample Type: Tissue Homogenates
Application: DB

Interleukin 15 receptor alpha (IL-15 R alpha ) is a high affinity receptor that specifically binds IL-15 with high affinity and associates as a heterotrimer with the IL-2 receptors beta and gamma subunits to initiate signal transduction. IL-15 R alpha is expressed on a wide variety of T cells and B cells as well as non-lymphoid cells.
IL‑15 R alpha is a 58-60 kDa protein that shares structural similarities to the IL-2 R alpha protein. IL-15 R alpha and IL-2 R alpha genes also share similar intron-exon organization and are closely linked on human chromosome 10p14-p15. Human IL-15 R alpha shares 45% amino acid (aa) homology with the mouse form of the receptor. Eight isoforms of
IL‑15 R alpha mRNA have been identified resulting from alternative splicing events involving different exons. The exclusion of exon 2 results in an IL-15 R alpha isoform that does not bind IL-15. Human IL-15 R alpha DE3 cDNA encodes a 267 amino acid (aa) protein that contains a 30 aa signal sequence, a 175 aa extracellular region containing one N-linked glycosylation site, a 21 aa transmembrane domain, and a 41 aa cytoplasmic tail. Signaling of IL-15 can occur in one of three ways; through the heterotrimeric complex of IL-15 R alpha, IL-2 R beta, and IL-2 R gamma _c, through the heterodimeric complex of IL-2 receptors beta and gamma common, through a novel 60-65 kDa IL-15 RX subunit found on mast cells. The binding of IL-15 to IL-15 R alpha has been reported to antagonize the TNF-alpha -mediated apoptosis in fibroblasts by competing with TNF RI for TRAF2 binding.

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