Interleukin-2, equine recombinant (reIL-2)

Recombinant equine Interleukin-2 produced in E. coli is a single, non-glycosylated, polypeptide chain containing 129 amino acids (with a substitution of S for C - at position 141 compared with the wild type IL2) and having a molecular mass of 14.9 kDa. IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin-4 (IL4) and interleukin-7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli. The ED50 as determined by a cell proliferation assay using murine CTLL-2 cells is less than 1.0 µg/ml, corresponding to a specific activity of > 1000 IU/mg.