EPO is predominantly synthesized and secreted by tubular and juxtatubular capillary, endothelial, and interstitial cells of the kidney. Approximately 10-15% of the total amount of EPO comes from extrarenal sources and is predominantly produced by hepatocytes and Kupffer cells of the liver. Approximately 40% of the molecular mass of EPO is due to its glycosylation. Glycosylation is an important factor determining the pharmacokinetic behaviour of EPO in vivo. Non-glycosylated Epo has an extremely short biological half life. Recombinant Human EPO is a glycosylated protein that runs at approximately 35 kDa owing to its glycosylation.
Alternative Names
Erythropoietin Recombinant Human Erythropoietin-Alpha (EPO)
Appearance
Lyophilized Powder
Reconstitution
A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS (pH 7)
Molecular Weight
20.0 kDa
Quantity
500 µg
Source
HEK293
Usage
For research use only. Not for diagnostic or therapeutic use.
Accession Number
P01588
Endotoxin Level
<1.0 EU/μg of recombinant protein as determined by the LAL method
Bioactivity
Activity was determined by the dose-dependent proliferation assay using a factor-dependent human erythroleukemic cell line TF-1 and was found to be less than 0.2ng/ml,
Gel Image
Gene Id
2056
Gene Name
EPO
Purity
>95% as determined by SDS-PAGE
Storage
The lyophilized protein is stable for at least one year from date of receipt at -70°C. Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8°C for one month, or at -20°C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles.