Abstract
The human interleukin-2 (IL-2) receptor was purified by affinity chromatography using the anti-Tac monoclonal antibody, and its N-terminal amino acid sequence was determined. Complementary DNA clones were isolated and sequenced to reveal the primary structure of the IL-2 receptor precursor, which has 272 amino acid residues. The receptor is separated into two domains by a putative 19-residue transmembrane region. Two mRNAs (1.4 and 3.5 kilobases) hybridizing to the cDNA clone were found in human T cells bearing the IL-2 receptor. The cDNA directed synthesis of the IL-2 receptor in COS cells.
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Nikaido, T., Shimizu, A., Ishida, N. et al. Molecular cloning of cDNA encoding human interleukin-2 receptor. Nature 311, 631–635 (1984). https://doi.org/10.1038/311631a0
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DOI: https://doi.org/10.1038/311631a0
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