EPO Mouse

Erythropoietin (EPO) is a glycoprotein hormone that plays a crucial role in the production of red blood cells. It is part of the type I cytokine family and is closely related to thrombopoietin . Recombinant Erythropoietin (EPO) from mouse is a laboratory-produced version of this hormone, designed to mimic the natural EPO found in mice.

Erythropoietin is a 34 kDa glycoprotein with three N-glycosylation sites, four alpha helices, and an N- to C-terminal disulfide bond . These structural features are conserved across species, ensuring that the hormone can perform its biological functions effectively. The glycosylation of EPO is essential for its biological activity, including its stability and interaction with the EPO receptor (EpoR).

Recombinant mouse Erythropoietin is typically produced using mammalian cell lines, such as the mouse myeloma cell line NS0 . The protein is then purified to achieve a high level of purity, often greater than 90%, as determined by SDS-PAGE under reducing conditions . The endotoxin level is kept below 0.10 EU per 1 μg of the protein to ensure its safety for research and therapeutic applications .

The biological activity of recombinant mouse Erythropoietin is measured using a cell proliferation assay with TF-1 human erythroleukemic cells . The effective dose (ED50) for this activity ranges from 0.4 to 2 ng/mL . This assay helps to confirm that the recombinant protein retains its functional properties and can stimulate the proliferation of erythroid progenitor cells.

Recombinant mouse Erythropoietin is used in various research applications, including studies on erythropoiesis, hypoxia, and the regulation of red blood cell production. It is also used in the development of therapeutic agents for treating anemia and other conditions related to red blood cell deficiency .

The recombinant protein is typically lyophilized and stored at -20 to -70°C to maintain its stability . Once reconstituted, it can be stored at 2 to 8°C for up to one month under sterile conditions . It is important to avoid repeated freeze-thaw cycles to preserve the protein’s activity.