Recombinant Mouse Erythropoietin/EPO (Catalog #959‑ME) stimulates proliferation in the TF‑1 human erythroleukemic cell line in a dose-dependent manner (orange line). Proliferation elicited by Recombinant Mouse ...read more
Chinese hamster ovary cell line CHO-derived recombinant mouse Erythropoietin/EPO Ala27-Arg192 Accession # P07321
Specificity
Detects human, mouse, and rat Erythropoietin/EPO in direct ELISAs and Western blots. In direct ELISAs, less than 1% cross-reactivity with recombinant mouse Thymopoietin (Tpo) is observed.
Source
N/A
Isotype
IgG
Clonality
Polyclonal
Host
Goat
Gene
EPO
Purity Statement
Antigen Affinity-purified
Endotoxin Note
<0.10 EU per 1 μg of the antibody by the LAL method.
Innovator's Reward
Test in a species/application not listed above to receive a full credit towards a future purchase.
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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Preservative
No Preservative
Concentration
LYOPH
Reconstitution Instructions
Reconstitute at 0.2 mg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Erythropoietin/EPO Antibody [Unconjugated]
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 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).
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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.
Kertesz, N. et al. (2004) Dev. Biol. 276:101.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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