A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific alpha chain and a beta chain shared with the receptor for GM-CSF.

@article{Tavernier1991AHH,
  title={A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific alpha chain and a beta chain shared with the receptor for GM-CSF.},
  author={Jan Tavernier and Rene Devos and Sigrid Cornelis and T Tuypens and Jos{\'e} van der Heyden and Walter Fiers and Geert Plaetinck},
  journal={Cell},
  year={1991},
  volume={66 6},
  pages={1175-84}
}
cDNA clones encoding two receptor proteins involved in the binding of human interleukin 5 (hIL5) have been isolated. A first class codes for an IL5-specific chain (hIL5R alpha). The major transcript of this receptor gene, as analyzed in both HL-60 eosinophilic cells and eosinophilic myelocytes grown from cord blood, encodes a secreted form of this receptor. This soluble hIL5R alpha has antagonistic properties. A second component of the hIL5R is found to be identical to the beta chain of the… CONTINUE READING

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