Recombinant Human Erythropoietin alpha, Liquid

Synonyms Epoetin

Accession P01588

GeneID 2056

Source CHO

Molecular Weight Mature human EPO, containing 166 amino acid residues, has a predicted molecular mass of approximately 21 kDa. As a result of glycosylation, the recombinant protein migrates with an apparent molecular mass of 36-40 kDa in SDS-PAGE.

Quantity 500IU/2000IU/150000IU

AA Sequence APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDR

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

Concentration See the label.

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 was found to be no less than 1.5 × 105 IU/mg.

Physical Appearance Clear colorless liquid.

Formulation Sterile filtered liquid in sodium citrate buffer (1 liter of ddH2O containing 5.9 g of sodium citrate, 5.8 g of sodium chloride and 0.06 g of citric acid).

Endotoxin Less than 0.01 EU/μg of rHuEPO-α as determined by LAL method.

Stability & Storage Do not freeze.

- 6 months from date of receipt, 2 to 8 °C as supplied.

- 3 months, 2 to 8 °C under sterile conditions after opening.

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. The cDNAs for EPO have been cloned from human, murine, canine, etc. The mature proteins from the various species are highly conserved, exhibiting greater than 80% sequence identity at the amino acid level. Human EPO cDNA encodes a 193 amino acid residue precursor protein that is processed to yield a 165 amino acid residue mature protein. EPO contains one O-linked and three N-linked glycosylation sites. Glycosylation of EPO is required for EPO biological activities in vivo. EPO exhibits structural as well as amino sequence identity to the amino terminal 153 amino acid region of thrombopoietin.