EPO Receptor polyclonal antibody

Erythropoiesis is regulated through the interaction of erythropoietin (Epo) with its receptor, EpoR, a member of the cytokine superfamily of receptors. The human EpoR is a 507 amino acid transmembrane protein that forms homo_x0002_dimers following erythropoietin activation and is related to the interleukin 2 (IL-2) receptor b-chain subunit (IL-2Rb) . EpoR and IL-2Rb share 45% amino acid identity within the box 1 and box 2 domains of their cytoplasmic regions while their remaining cytoplasmic sequences are highly divergent. These conserved domains are both required and sufficient for mitogenesis and for coupling ligand binding to the induction of tyrosine phosphorylation. The membrane proximal region is also required for the association of JAK2 with EpoR. The existence of multiple cross-linked complexes and differential ligand affinities suggests that EpoR may exist as a multireceptor complex.