Human IL-15R alpha Alexa Fluor® 488-conjugated Antibody Summary
Accession # EAW86418
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of IL‑15 R alpha in Human PBMCs by Flow Cytometry. Human peripheral blood mononuclear cells (PBMCs) either (A) untreated or (B) treated overnight with PHA were stained with Mouse Anti-Human IL-15 Ra Alexa Fluor® 488-conjugated Monoclonal Antibody (Catalog # FAB1471G) and Mouse Anti-Human CD4 APC-conjugated Monoclonal Antibody (Catalog # FAB3791A). Quadrant markers were set based on control antibody staining (Catalog # IC0041G). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
Background: IL-15R alpha
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 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 R beta and IL-2 R gamma c, or 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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