epitope corresponding to amino acids 21-214 mapping near the N-terminus of EpoR of human origin
Modification Notes
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 homodimers 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.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFIHCELISA
recommended for detection of erythropoietin (Epo) receptor of mouse, rat and human origin by WB, IP, IF, IHC(P) and ELISA:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 21-214 mapping near the N-terminus of EpoR of human origin
Tissue Specificity
epitope corresponding to amino acids 21-214 mapping near the N-terminus of EpoR of human origin