|IL‑15 R alpha in Human Prostate Cancer Tissue. IL‑15 R alpha was detected in immersion fixed paraffin-embedded sections of human prostate cancer tissue using 15 µg/mL Goat Anti-Human IL‑15 R alpha Antigen Affinity-purified Polyclonal Antibody (Catalog # AF247) overnight at 4 °C. Tissue was stained with the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.|
IL‑15 R alpha Inhibition of IL‑15-dependent Cell Proliferation and Neutralization by Human IL‑15 R alpha Antibody. Recombinant Human IL‑15 R alpha Fc Chimera (Catalog #|
147‑IR) inhibits Recombinant Human IL‑15 (Catalog #
247‑IL) induced proliferation in the CTLL‑2 mouse cytotoxic T cell line in a dose-dependent manner (orange line). Inhibition of Recombinant Human IL‑15 (2 ng/mL) activity elicited by Recombinant Human IL‑15 R alpha Fc Chimera (30 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Human IL‑15 R alpha Antigen Affinity-purified Polyclonal Antibody (Catalog # AF247). The ND50 is typically
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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