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EPO Authentic Glycan Structure


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EPO (HuXp) expressed from human cells exhibits authentic glycan structure.
Erythropoietin (EPO) is a 34 kD glycoprotein hormone which is related to thrombopeietin. This protein promotes erythrocyte formation by preventing the apoptosis of early erythroid precursors. It has been shown glycosylation of EPO is required for biological activities in vivo. Currently, commercially available recombinant human EPO proteins are produced from CHO cells. These recombinant proteins differ from the native human EPO by having higher apparent molecular mass of 37 kD (as indicated by migration on SDS-PAGE) and lower content of neutral glycans. HumanZyme has produced EPO (HuXp) from engineered human 293 cells. Similar to the native human protein, EPO (HuXp) exhibits a lower apparent molecular mass and substantially higher content of neutral glycans. Furthermore, EPO (HuXp) has more abundant and diverse glycan profiles than the CHO cell produced version. The most abundant glycans in EPO (HuXp) are tetra-antennary complex types whereas those in CHO EPO are elongated bi-antennary complex types.

Authentic Erythropoietin, human cell expressed ...

 



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