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Bcakground
Erythropoietin (EPO)is a 34 kDa glycoprotein hormone in the type I cytokine family and is related to thrombopoietin (1). Its three N-glycosylation sites, four alpha helices, and N- to C-terminal disulfide bond are conserved across species (2, 3). Glycosylation of (EPO is required for biological activities in vivo (4). Mature mouse (EPO shares 95% amino acid sequence identity with rat (EPO and 73%-82% with bovine, canine, equine, feline, human, ovine, and porcine EPO. Epo is primarily produced in the kidney by a population of fibroblast-like cortical interstitial cells adjacent to the proximal tubules (5). It is also produced in much lower, but functionally significant amounts by fetal hepatocytes and in adult liver and brain (6-8). (EPO promotes erythrocyte formation by preventing the apoptosis of early erythroid precursors which express the (EPO receptor (EPO R) (8, 9). (EPO R has also been described in brain, retina, heart, skeletal muscle, kidney, endothelial cells, and a variety of tumor cells (7, 8, 10, 11). Ligand induced dimerization of (EPO R triggers JAK2-mediated signaling pathways followed by receptor/ligand endocytosis and degradation (1, 12). Rapid regulation of circulating (EPO allows tight control of erythrocyte production and hemoglobin concentrations. Anemia or other causes of low tissue oxygen tension induce (EPO production by stabilizing the hypoxia-induceable transcription factors HIF-1 alpha and HIF-2 alpha (1, 6). (EPO additionally plays a tissue-protective role in ischemia by blocking apoptosis and inducing angiogenesis (7, 8, 13).
Reference
1. Koury, M. J. (2005) Exp. Hematol. 33:1263.
2. Shoemaker, C.B. and L.D. Mitsock (1986) Mol. Cell. Biol 6:849.
3. Wen, D. et al. (1993) Blood 82:1507.
4. Tsuda E. et al. (1990) Eur. J. Biochem. 188:405.
5. Lacombe, C. et al. (1988) J. Clin. Invest. 81:620.
6. Eckardt, K. U. and A. Kurtz (2005) Eur. J. Clin. Invest. 35 Suppl. 3:13.
7. Sharples, E. J. et al. (2006) Curr. Opin. Pharmacol. 6:184.
8. Rossert, J. and K. Eckardt (2005) Nephrol. Dial. Transplant 20:1025.
9. Koury, M.J. and M.C. Bondurant (1990) Science 248:378.
10. Acs, G. et al. (2001) Cancer Res. 61:3561.
11. Hardee, M.E. et al. (2006) Clin. Cancer Res. 12:332.
12. Verdier, F. et al. (2000) J. Biol. Chem. 275:18375.
13. Kertesz, N. et al. (2004) Dev. Biol. 276:101.
Specifications
| Synonyms | ECYT5; EP; EPO; epoetin; Erythropoietin; MGC138142; MVCD2 |
| Accession # | Q0VED9 |
| Source | Human embryonic kidney cell, HEK293-derived mouse Erythropoietin/EPO protein |
| Ala27-Arg192 | |
| Predicted Moleucular weight | 18.6 kDa |
Components and Storage
| Formulation | Solution protein |
| Dissolved in sterile PBS buffer | |
| This solution can then be diluted into other aqueous buffers, Centrifuge the vial prior to opening. | |
| Storage and Stability | Avoid repeated freeze-thaw cycles |
| It is recommended that the protein be aliquoted for optimal storage | |
| 12 months from date of receipt, -20 to -70 °C as supplied | |
| Shipping | Shipping with dry ice |
Quality
| Purity | > 95%, determined by SDS-PAGE |
| Endotoxin Level | <0.010 EU per 1 ug of the protein by the LAL method |
| Activity | Measured in a cell proliferation assay using TF-1 human erythroleukemic cells |
| The EC50 for this effect is 0.1-0.4 ng/mL |
SDS-PAGE
Bioactivity
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