Recombinant Human Erythropoietin alpha Fc

Synonyms Epoetin

Source CHO

Molecular Weight Recombinant Human EPO/Fc produced in CHO is a dimeric, glycosylated, polypeptide chain consisting of two mature human EPO molecules linked to the Fc portion of human IgG1. The Fc component contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. As a result of glycosylation, the recombinant protein migrates with an apparent molecular mass of 140 kDa in non-reducing SDS-PAGE.

Quantity 2µg/10µg/1mg

Purity > 98 % by SDS-PAGE and HPLC analyses.

Biological Activity Fully biologically active when compared to standard. The Specific Activity was measured by the stimulation of reticulocyte production in normocyth-aemic mice and is no less than 5.0 × 105 IU/mg.

Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder.

Formulation Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH 7.4.

Endotoxin Less than 1 EU/μg of rHuEPO-Fc a as determined by LAL method.

Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.

Stability & Storage 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.

- 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Usage This material is offered by Shanghai PrimeGene Bio-Tech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE.

Reference 1. Hanicki Z. 1988. Pol Arch Med Wewn, 80: 290-3.

2. Haniu M, Narhi LO, Arakawa T, et al. 1993. Protein Sci, 2: 1441-51.

3. Baranowska-Daca EandKsiazek A. 1994. Ann Univ Mariae Curie Sklodowska Med, 48 Suppl 3: 51-60.

4. Chow KM, Szeto CC, Li PK. 2003. Am J Kidney Dis, 41: 266-7; author reply 7.

5. Maurer MH, Schabitz WR, Schneider A. 2008. Curr Med Chem, 15: 1407-11.

Background Erythropoietin (EPO), a glycoprotein produced primarily by the kidney, is the principal factor that regulates erythropoiesis by stimulating the proliferation and differentiation of erythroid progenitor cells. The production of EPO by kidney cells is increased in response to hypoxia or anemia. Recombinant EPO has been approved for the treatment of anemia associated with chronic renal failure as well as for anemia of AZT treated AIDS patients.