EPO Protein
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- Target See all EPO Proteins
- EPO (Erythropoietin (EPO))
- Protein Type
- Recombinant
- Biological Activity
- Active
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Origin
- Human
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Source
- CHO Cells
- 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.
- Sterility
- 0.2 μm filtered
- Endotoxin Level
- Less than 1EU/µg of rHuEPO-alpha as determined by LAL method.
- Top Product
- Discover our top product EPO Protein
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- Restrictions
- For Research Use only
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- Format
- Lyophilized
- 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.
- Storage
- 4 °C/-20 °C
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- Target
- EPO (Erythropoietin (EPO))
- Alternative Name
- EPO (EPO Products)
- Synonyms
- EPO Protein, EP Protein, MVCD2 Protein, erythropoietin Protein, erythropoietin S homeolog Protein, erythropoietin a Protein, EPO Protein, epo Protein, epo.S Protein, Epo Protein, epoa Protein
- Target Type
- Hormone
- 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.
- Pathways
- JAK-STAT Signaling, Hormone Activity, Negative Regulation of intrinsic apoptotic Signaling, Negative Regulation of Transporter Activity
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