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.
Quantity
1.0 mg
Regulatory
RUO
Source
HEK293
Host
Human
Endotoxin Level
<1.0 EU/μg of recombinant protein as determined by the LAL method
Biological Activity Comment
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
Weight
20.0 kDa
Description
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.
Format
Lyophilized PowderLyophilized from a 0.2 μm filtered solution in PBS (pH 7)
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.