GHR shows a high degree of homology with the prolactin receptor and with th
e other receptors that belong to the hemopoietic receptor superfamily, This
paper describes a monoclonal antibody (MAb) (2B4B6) specific for both the
extracellular domain of human GHR and human growth hormone (GH) binding pro
tein. Mice were immunized against a seven-aminoacid peptide sequence screen
ed by FASTA (sequence similarity search served by Genome-Net) from the Euro
pean Bioinformatics Institute to exclude the existence of human membrane pr
oteins with significant sequence homology, MAbs were screened against the p
eptide sequence and 2B4B6 was selected for its capability to recognize the
full-length hGHBP. As evaluated by both enzyme-linked immunoadsorbent assay
(ELISA) and FAGS analysis, this MAb seems to recognize and bind to a hGHR
positive cell line, IM-9, as well as a murine cell line, BaF3 (8/6), transf
ected with a chimeric construct, hGHR/hG-CSFR and expressing hGHR on the ce
ll membrane, Studies investigating the biological effects of this MAb showe
d that anti-hGHR mediated inhibition of cell proliferation was not due to c
ompetition with GH binding but rather to prevention of receptor dimerizatio
n, Because of its specificity, this MAb may be usefully applied in situatio
ns in which GHR and receptors with a high degree of homology, such as PRLR
(prolactin receptor), are expressed simultaneously, as occurs in the immune
system.