A recombinant partial protein sequence (within amino acids 1-152) from the human protein was used as the immunogen for the IL15 antibody.
Interleukin-15 (IL-15), also designated IL-T, is a cloned cytokine which shares several biological activities but no sequence homology with IL-2. Human, mouse and simian IL-15 cDNA clones have been isolated and characterized. All 3 species encode a 162 amino acid residue precursor protein containing a 48 amino acid leader that is cleaved to generate the mature form of IL-15. IL-15 stimulates the proliferation of T cells and NK cells, while enhancing B cell expansion and antibody production. Unlike IL-2, IL-15 is not produced by lymphocytes, but appears to be produced by macrophages, epithelial lines, muscle and placenta. IL-15 has also been shown to be a chemoattractant for human blood T lymphocytes and to be able to induce lymphokine-activated killer (LAK) activity in NK cells as well as to be able to induce the generation of cytolytic effector cells. Studies have shown that IL-15 is the only other cytokine that shares the beta signaling subunit of the IL-2R. Evidence also suggests that like IL-2, IL-4 and IL-7, IL-15 utilizes the common IL-2Rgamma subunit.
