EPO Rat

Recombinant erythropoietin (rhEPO) is produced using cells transfected with the EPO gene or EPO cDNA linked to an expression vector . This recombinant DNA is integrated into the genome of the host cell, which then stably expresses the EPO protein over time . The production of rhEPO typically involves mammalian host cells, such as Chinese hamster ovary (CHO) cells, due to the complex glycosylation patterns required for its biological activity .

Glycosylation is a critical aspect of EPO’s structure and function. EPO has three N-glycosylation sites, four alpha helices, and an N- to C-terminal disulfide bond that are conserved across species . The glycosylation of EPO is essential for its biological activities in vivo, including its therapeutic efficacy, in vivo activity, and half-life . The glycosylation pattern of glycoproteins is species-dependent, which is why mammalian cells are preferred for producing glycosylated biopharmaceuticals .

Recombinant human erythropoietin (rhEPO) is widely used as a therapeutic agent for treating anemia, particularly in patients with chronic kidney disease (CKD), malignancies, and AIDS . It also supports autologous blood collection and represents one of the largest markets for biopharmaceuticals . The administration of rhEPO and its analogues provides significant benefits in preventing and reversing anemia in these conditions .