Catalog#/Size：AC52388/100 µg.

Source：Escherichia coli.

Molecular Weight：Approximately 15.5 kDa, a single non-glycosylated polypeptide chain containing 134 amino acid.

Description：Accession # P60658.1, Ala21-Thr153（C125A）, with an N-terminal Ser.

SDS-PAGE：15.5kDa, reducing conditions

Purity：> 95 %, as determined by SDS-PAGE, under reducing non-reducing conditions, visualized by coomassie staining.

Endotoxin：Less than 0.01 EU/µg of rHuIL-2 as determined by kinetic Limulus Amoebocyte Lysate (LAL) assay.

Biological Activity：Recombinant human IL-2 bioactivity is measured in a cell proliferation assay using CTLL-2 mouse cytotoxic T cells, the EC50 for this effect is 5.214 to 6.755 ng/mL.

Quality statement:No animal- or human-derived materials were used for the manufacture of this product, unless otherwise stated in the respective Certificate of Origin.

IL-2, also named T-cell growth factor, was first discovered in 1976 and was characterized as a soluble factor with the unique ability to promote clonal expansion of many hematopoietic lines including regulatory T cells (Tregs) in vitro. Human IL-2 has 133 amino acids and in mature form it is a glycosylated globular protein of 15.5 k Da four-bundle,  α  -helical protein member of the common cytokine receptor  γ  -chain family of cytokines. IL-2 is predominantly produced by activated CD4₊ T cells and, to a lesser extent by activated CD8₊ T cells, activated dendritic cells, natural killer (NK) cells, NKT cells, as well as B cells.

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