Gibco™ Human IL-15 Recombinant Protein

Description

Carrier-Free Reconstitution: We recommend reconstituting the lyophilized protein in sterile double distilled water containing at least 0.1% human serum albumin or bovine serum albumin to prepare a stock solution of ≥1 mg/mL of the protein. The reconstituted protein should be apportioned into working aliquots and stored at ≤-20°C. Storage: The lyophilized protein is stable for a few weeks at room temperature, but is best stored at -20°C. Reconstituted human IL-15 should be stored at ≤-20°C (not in a frost-free freezer). Keep freeze-thaw cycles to a minimum.

IL-15 (Interleukin 15 ) is a cytokine that regulates T and natural killer cell activation and proliferation. IL-15 and IL-2 share many biological activities as both have been found to bind common hematopoietin receptor subunits, and may compete for the same receptor, and thus negatively regulate each other's activity. The number of CD8+ memory cells is shown to be controlled by a balance between IL-15 and IL-2. IL-15 induces the activation of JAK kinases, as well as the phosphorylation and activation of transcription activators STAT3, STAT5, and STAT6. In mouse, studies suggest that IL-15 may increase the expression of apoptosis inhibitor Bcl-xL, possibly through the transcription activation activity of STAT6, and thus prevent apoptosis. IL-15 plays an important role in the growth and differentiation of T and B lymphocytes, natural killer cells, macrophages, and monocytes as well as activation of a number of important intracellular signaling molecules. As such, IL-15 could be essential for the immune responses, allograft rejection, and the pathogenesis of autoimmune diseases. Further, IL-15 is a widely expressed pro-inflammatory cytokine and has been shown to play a role in several inflammatory disorders, including rheumatoid arthritis, psoriasis and pulmonary inflammatory diseases. Emerging data suggest that IL-15 may serve as a good therapeutic target, as there appears to be a beneficial effect of IL-15 neutralization in models of psoriasis and diabetes.