The Quantikine Mouse Epo Immunoassay is a 4.5 hour solid-phase ELISA designed to measure mouse Epo in cell culture supernates, tissue homogenates, serum, and plasma. It contains antibodies raised against recombinant Epo and has been shown to accurately quantitate the recombinant factor. Results obtained using natural mouse Epo showed linear curves that were parallel to the standard curves ob...tained using the Quantikine kit standards. These results indicate that the Quantikine Mouse Epo kit can be used to determine relative mass values for naturally occurring mouse Epo.
Natural and recombinant mouse Epo. Recombinant rat Epo has 100% cross-reactivity in this kit. This kit is not validated for use with rat samples, because rat sample dilution is not linear.
Store the unopened product at 2 - 8 °C. Do not use past expiration date.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Mouse Erythropoietin/EPO Quantikine ELISA Kit
Erythropoietin (Epo) is a 34-39 kDa secreted glycoprotein that is a member of the type I
cytokine superfamily. The mouse Epo gene encodes a 192 amino acid (aa) residue precursor
that contains a 26 aa signal peptide and a 166 aa mature protein containing three potential
N-linked glycosylation sites (1-4). Mouse Epo lacks the O-linked glycosylation site found in
human Epo. Although carbohydrate chains are not required for in vitro receptor binding, they
are required for in vivo Epo bioactivity. Depending on the cell source, different Epo isoforms
are produced that differ in their glycan compositions and sialic acid contents (5-8). Mature
mouse and rat Epo share 94% aa sequence identity. They also share from 80%-82% aa identity
with mature human, porcine, rhesus monkey and feline Epo (2, 3). Epo is primarily produced
by cells in the kidney (interstitial peritubular renal fibroblasts) and liver (hepatocytes and
Ito cells), where its production is up-regulated by hypoxia. Other tissues and cells, including
neural tissues (astrocytes and neurons), testis (Sertoli cells), uterus, placenta, and erythroid
progenitors, have also been shown to produce Epo (9-14).
Epo is best known for its role in red blood cell formation. While Epo is not a lineage
commitment factor, it inhibits apoptosis and induces burst forming unit-erythroid
(BFU-E) differentiation into colony forming unit-erythroid (CFU-E), and the subsequent
proliferation and maturation of CFU-E into early normoblasts (10, 15, 16). Apart from its role
in erythropoiesis, Epo also acts on various non-hematopoietic cells to function as a viability
and proliferation factor. Epo can stimulate myoblast proliferation while suppressing its
differentiation, resulting in the expansion of the progenitor cell population (17). Epo is a tissueprotective factor that protects against ischemic and toxic injuries to neuronal, cardiovascular
and renal tissues (18, 19). Epo has also been shown to promote angiogenesis in various
physiologic and pathologic conditions (20, 21).
Epo binds and signals via the high-affinity preformed homodimeric Epo receptor (Epo R) that is
composed of two Epo R subunits. Each Epo R subunit is a type I transmembrane glycoprotein
that belongs to the type I cytokine receptor superfamily (18, 22-24). Its extracellular domain
contains the characteristic two fibronectin type III domains and a WSxWS motif near the
plasma membrane (24, 25). Binding of Epo to the Epo R homodimer results in conformational
change and phosphorylation and activation of the non-receptor protein kinase JAK2, which
activates the downstream signaling cascade (26). An alternative Epo heteromeric receptor
complex that transduces cell-protective signals and containing the beta common receptor ( beta CR)
subunit in addition to the Epo R subunit has been described. beta CR also belongs to the
type I cytokine receptor superfamily and is a subunit that is shared by the heteromeric IL-3,
IL-5 and GM-CSF receptor complexes. Epo binds with lower affinity to the heteromeric receptor
consisting of a Epo R subunit and a beta CR homodimer (18).