描述：
Erythropoietin (Epo), a glycoprotein produced primarily by the kidney, is the principal factor
that regulates erythropoiesis by stimulating the proliferation and differentiation of erythroid
progenitor cells. The biological effects of Epo are mediated by the erythropoietin receptor
(Epo R). A member of the hematopoietic growth factor receptor superfamily which includes
IL-2, IL-3, IL-4, IL-5, IL-6, IL-7, GM-CSF, G-CSF, thrombopoietin, LIF, CNTF, growth hormone,
and prolactin, Epo R is expressed not only by erythroid cells but also by embryonic stem cells,
endothelial cells, and neural cells. Mouse Epo R cDNA encode a type I membrane-spanning
protein with 507 amino acid (aa) residues. Mouse Epo R has a 24 aa hydrophobic signal
peptide, a 225 aa extracellular domain, a 22 aa transmembrane domain, and a 236 aa
intracellular domain. At the protein sequence level, the human Epo R is approximately 82%
identical to the mouse protein. Mouse and human Epo R both contain 11 cysteine residues
and an Nlinked glycosylation site. Mouse Epo R, however, contains two disulfide bridges not
found with human Epo R. In common with other hematopoietic growth factor receptor
superfamily members, mouse Epo R has 4 positionally conserved cysteines in its extracellular
domain, a tryptophan-serine-X-tryptophan-serine (WSXWS) motif or its homolog located near
the transmembrane region, and lacks kinase motifs in its intracellular domain. Based on its
amino acid composition the molecular weight of Epo R would be 55 kDa but after post
translational modification including glycosylation and tyrosine and serinethreonine
phosphorylation the molecular weight can be as high as 78 kDa. As a result of alternative
splicing of the Epo R gene, cDNA clones encoding a truncated form of the Epo R as well as a
soluble form of Epo R has been found. The presence of a soluble form of the Epo R has also
been detected in human sera. Recombinant soluble Epo R binds Epo with high affinity and is
a potent Epo antagonist.
原厂资料：
Erythropoietin (Epo), a glycoprotein produced primarily by the kidney, is the principal factor
that regulates erythropoiesis by stimulating the proliferation and differentiation of erythroid
progenitor cells. The biological effects of Epo are mediated by the erythropoietin receptor
(Epo R). A member of the hematopoietic growth factor receptor superfamily which includes
IL-2, IL-3, IL-4, IL-5, IL-6, IL-7, GM-CSF, G-CSF, thrombopoietin, LIF, CNTF, growth hormone,
and prolactin, Epo R is expressed not only by erythroid cells but also by embryonic stem cells,
endothelial cells, and neural cells. Mouse Epo R cDNA encode a type I membrane-spanning
protein with 507 amino acid (aa) residues. Mouse Epo R has a 24 aa hydrophobic signal
peptide, a 225 aa extracellular domain, a 22 aa transmembrane domain, and a 236 aa
intracellular domain. At the protein sequence level, the human Epo R is approximately 82%
identical to the mouse protein. Mouse and human Epo R both contain 11 cysteine residues
and an Nlinked glycosylation site. Mouse Epo R, however, contains two disulfide bridges not
found with human Epo R. In common with other hematopoietic growth factor receptor
superfamily members, mouse Epo R has 4 positionally conserved cysteines in its extracellular
domain, a tryptophan-serine-X-tryptophan-serine (WSXWS) motif or its homolog located near
the transmembrane region, and lacks kinase motifs in its intracellular domain. Based on its
amino acid composition the molecular weight of Epo R would be 55 kDa but after post
translational modification including glycosylation and tyrosine and serinethreonine
phosphorylation the molecular weight can be as high as 78 kDa. As a result of alternative
splicing of the Epo R gene, cDNA clones encoding a truncated form of the Epo R as well as a
soluble form of Epo R has been found. The presence of a soluble form of the Epo R has also
been detected in human sera. Recombinant soluble Epo R binds Epo with high affinity and is
a potent Epo antagonist.
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