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Human EPOR / Erythropoietin Receptor Protein (Fc Tag)

EPO-R

Catalog Number P10707-H02H
Organism Species Human
Host Human Cells
Synonyms EPO-R
Molecular Weight The recombinant human EPOR/Fc is a disulfide-linked homodimeric protein after removal of the signal peptide. The reduced monomer consists of 460 amino acids and has a predicted molecular mass of 51.0 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhEPOR/Fc monomer is approximately 55-60 kDa due to glycosylation.
predicted N Ala 25
SDS-PAGE
Purity > 90 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the extracellular domain (Met-Pro 250) of human erythropoietin receptor (NP_000112.1) precursor was expressed with the C-terminal fused Fc region of human IgG1.
Bio-activity 1. Measured by its binding ability in a functional ELISA. Immobilized CD131 at 10 μg/ml (100 μl/well) can bind biotinylated recombinant human EPOR with a linear range of 0.16-4 μg/ml.
2. Measured by its ability to inhibit EPO-dependent proliferation of TF-1 human erythroleukemic cells. The ED50 for this effect is typically 4-16 ng/mL in the presence of 0.1 U/mL Recombinant Human EPO.
Research Area Immunology |Signal Transduction |Transcription Factors and Regulators |HIF Transcription Factors
Formulation Lyophilized from sterile PBS, 8% sucrose, 0.5% Tween-20, pH 7.4
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Erythropoietin (EPO) is the major glycoprotein hormone regulator of mammalian erythropoiesis, and is produced by kidney and liver in an oxygen-dependent manner. The biological effects of EPO are mediated by the specific erythropoietin receptor (EPOR/EPO Receptor) on bone marrow erythroblasts, which transmits signals important for both proliferation and differentiation along the erythroid lineage. EPOR protein is a type â…  single-transmembrane cytokine receptor, and belongs to the homodimerizing subclass which functions as ligand-induced or ligand-stabilized homodimers. EPOR signaling prevents neuronal death and ischemic injury. Recent studies have shown that EPO and EPOR protein may be involved in carcinogenesis, angiogenesis, and invasion.
Reference
  • Divoky V, et al. (2002) Mouse surviving solely on human erythropoietin receptor (EpoR): model of human EpoR-linked disease. Blood 99(10): 3873-4.
  • Carruthers SG. (2009) A truncated erythropoietin receptor EPOR-T is associated with hypertension susceptibility. Clin Pharmacol Ther. 86(2): 134-6.
  • Baltaziak M, et al. (2009) Relationships of P53 and Bak with EPO and EPOR in human colorectal cancer. Anticancer Res. 29(10):4151-6.