Detects mouse IL-15 R alpha in direct ELISAs and Western blots. In direct ELISAs, approximately 5% cross-reactivity with recombinant human (rh) IL‑15 R alpha is observed and less than 1% cross-reactivity with rhIL-2 R alpha, recombinant mouse (rm) IL-2 R beta, and rmIL-2 R gamma is observed.
Polyclonal Goat IgG
Mouse myeloma cell line NS0-derived recombinant mouse IL-15 R alpha Gly33-Lys205 Accession # Q60819
Supplied in a saline solution containing BSA and Sodium Azide.
10 µL/106 cells
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 EL‑4 Mouse Cell Line by Flow Cytometry. EL‑4 mouse lymphoblast cell line was stained with Goat Anti-Mouse IL‑15 R alpha PE‑conjugated Antigen Affinity-purified Polyclonal Antibody (Catalog # FAB551P, filled histogram) or isotype control antibody (Catalog # IC108P, open histogram). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
Background: IL-15 R 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. 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.
Anderson, D.M. et al. (1995) J. Biol. Chem. 270:29862.
Bulfone-Paus, S. et al. (1999) FASEB 13:1575.
Waldemann, T.A. and Y. Tagaya (1999) Ann. Rev. Immunol. 17:19.
Dubois, S. et al. (1999) J. Biol. Chem. 274:26978.
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