Recombinant Human Erythropoietin/EPO (Tissue Culture Grade) Summary
Details of Functionality
Calibrated against the second international reference preparation of erythropoietin. Annable, L. et al. (1972) Bull. Hlth. Org. 47:99. Measured in a cell proliferation assay using TF‑1 human erythroleukemic cells. Kitamura, T. et al. (1989) J. Cell Physiol. 140:323. The ED50 for this effect is 0.015-0.075 units/mL.
Chinese Hamster Ovary cell line, CHO-derived human Erythropoietin/EPO protein Ala28-Arg193
<0.10 EU per 1 μg of the protein by the LAL method.
21 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Reconstitute at 500 U/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Erythropoietin/EPO (Tissue Culture Grade)
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 the EPO protein is required for biological activities in vivo (4). The mature human EPO protein shares 75% - 84% amino acid sequence identity with bovine, canine, equine, feline, mouse, ovine, porcine, and rat 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 erythropoietin 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 erythropoietin 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).
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Lacombe, C. et al. (1988) J. Clin. Invest. 81:620.
Eckardt, K.U. and A. Kurtz (2005) Eur. J. Clin. Invest. 35 Suppl. 3:13.
Sharples, E.J. et al. (2006) Curr. Opin. Pharmacol. 6:184.
Rossert, J. and K. Eckardt (2005) Nephrol. Dial. Transplant 20:1025.
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Acs, G. et al. (2001) Cancer Res. 61:3561.
Hardee, M.E. et al. (2006) Clin. Cancer Res. 12:332.
Verdier, F. et al. (2000) J. Biol. Chem. 275:18375.
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