Recombinant Rat Erythropoietin/EPO Protein, CF Summary
Details of Functionality
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 0.07-0.4 ng/mL.
Source
Spodoptera frugiperda, Sf 21 (stably transfected)-derived rat Erythropoietin/EPO protein Ala27-Arg192
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
18.5 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.
SDS-PAGE
22-26 kDa, reducing conditions
Publications
Read Publications using 1306-RE/CF in the following applications:
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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Rat Erythropoietin/EPO Protein, CF
ECYT5
EP
EPO
epoetin
Erythropoietin
MGC138142
MVCD2
Background
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 rat EPO shares 95% amino acid sequence identity with mouse EPO and 72%-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 by 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).
Koury, M. J. (2005) Exp. Hematol. 33:1263.
Nagao, M. et al. (1992) Biochim. Biophys. Acta 1171:99.
Wen, D. et al. (1993) Blood 82:1507.
Tsuda E. et al. (1990) Eur. J. Biochem. 188:405.
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.
Koury, M.J. and M.C. Bondurant (1990) Science 248:378.
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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