|IL‑2 in Canine PBMCs. IL‑2 was detected in immersion fixed canine peripheral blood mononuclear cells (PBMCs) untreated or treated with calcium ionomycin and PMA using Goat Anti-Canine IL‑2 Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF1815) at 15 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Streptavidin (red; Catalog # NL999) and counterstained with DAPI (blue). Specific staining was localized to cell secretion. View our protocol for Fluorescent ICC Staining of Non-adherent Cells.|
Interleukin 2 was initially identified as a T cell growth factor that is produced by T cells following activation by mitogens or antigens. Since then, it has been shown that IL-2 can also stimulate the growth and differentiation of B cells, natural killer (NK) cells, lymphocyte activated killer (LAK) cells, monocytes/macrophages, and oligodendrocytes. The biological activity of IL-2 is mediated by the binding to cell surface receptor complexes composed of three subunits designated as alpha, beta, and gamma subunits. IL-2 binds the alpha subunit with low affinity. The functional high affinity IL-2 receptor is a heterotrimeric complex of the alpha, beta, and gamma subunits. IL-2 binds with intermediate affinity to the complex containing the beta and gamma subunits, which is also capable of transducing IL-2 signals. In T cells, the beta and gamma subunits are shared with the IL-15 receptor complex. The gamma subunit of the IL-2 receptor complex has also been shown to be a subunit of the receptor complexes of IL-4, IL-7, and IL-9. At the amino acid sequence level, canine IL-2 shares 90%, 86%, 85%, 76%, and 75% sequence similarities to feline, human, equine, mouse, and bovine IL-2, respectively.
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