Analytical Data
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Gene name
EPO/Erythropoietin Protein
- Application
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Alternative Names
/
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Species
Horse
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Source
HEK293
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Tag
C- hFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q867B1
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Expression Region
27-192aa
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Molecular Weight
47.3
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Erythropoietin (EPO) is a glycoprotein hormone primarily produced by the kidneys that plays a crucial role in the regulation of red blood cell production in response to hypoxia. Its recombinant form, rhEPO, has been widely studied and utilized in clinical settings to treat conditions such as anemia, particularly in patients with chronic kidney disease, cancer, or those undergoing chemotherapy. The recombinant production of EPO has revolutionized therapeutic approaches, enabling higher purity and reduced risk of contamination that was often observed with urine-derived EPO. Research into rhEPO has not only elucidated its structure and mechanisms of action but has also expanded its applications beyond anemia treatment, exploring potential benefits in areas such as tissue protection in ischemic conditions and performance enhancement in sports, although the latter has raised ethical concerns regarding doping. The advancements in biotechnological methods, such as genetic engineering in mammalian cell systems, have led to the efficient production of EPO with desired pharmacokinetic properties, making it a key focus of ongoing research in regenerative medicine and hematology. Overall, the study of recombinant EPO continues to offer insights into erythropoiesis and novel therapeutic strategies for various hematological disorders.
