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H5166

Sigma-Aldrich

Erythropoietin human

EPO, recombinant, expressed in HEK 293 cells, suitable for cell culture

Synonym(s):

EPO

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About This Item

CAS Number:
11096-26-7
MDL number:
MFCD00131025
UNSPSC Code:
12352202
NACRES:
NA.77

biological source

human

Quality Level

100

recombinant

expressed in HEK 293 cells

Assay

≥95% (SDS-PAGE)

form

lyophilized powder

potency

≤5.0 ng/mL ED50

quality

endotoxin tested

mol wt

dimer 36 kDa (glycosylated)

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

technique(s)

cell culture | mammalian: suitable

impurities

≤1 EU/μg

UniProt accession no.

P01588

storage temp.

−20°C

Gene Information

human ... EPO(2056)

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General description

EPO has been cloned from various species including human, murine, canine, and others. The mature proteins from the various species are highly conserved and exhibit greater than 80% amino acid sequence identity. EPO contains three N-linked glycosylation sites. The glycosylation of erythropoietin is required for the biological activities of erythropoietin in vivo.

Biochem/physiol Actions

Erythropoietin (EPO), produced primarily by the kidney, is the primary regulatory factor of erythropoiesis. It promotes the proliferation, differentiation, and survival of the erythroid progenitors. Erythropoietin stimulates erythropoiesis by inducing growth and differentiation of burst forming units and colony forming units into mature red blood cells. EPO produced by kidney cells is increased in response to hypoxia or anemia. The biological effects of erythropoietin are mediated by the erythropoietin receptor, which binds EPO with high affinity and is a potent EPO antagonist.
Erythropoietin is a glycoprotein that is the principal regulator of red blood cell growth and differentiation.

Preparation Note

Human EPO is expressed as a glycosylated 36 kDa monomer in human HEK 293 cells. Production in human HEK 293 cells offers authentic glycosylation. Glycosylation contributes to stability in cell growth media and other applications.

Analysis Note

The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line).

Storage Class Code

11 - Combustible Solids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Rajasekhar N V S Suragani et al.
Nature medicine, 20(4), 408-414 (2014-03-25)
Erythropoietin (EPO) stimulates proliferation of early-stage erythrocyte precursors and is widely used for the treatment of chronic anemia. However, several types of EPO-resistant anemia are characterized by defects in late-stage erythropoiesis, which is EPO independent. Here we investigated regulation of
Claudia S Robertson et al.
JAMA, 312(1), 36-47 (2014-07-25)
There is limited information about the effect of erythropoietin or a high hemoglobin transfusion threshold after a traumatic brain injury. To compare the effects of erythropoietin and 2 hemoglobin transfusion thresholds (7 and 10 g/dL) on neurological recovery after traumatic
Mawadda Alnaeeli et al.
Diabetes, 63(7), 2415-2431 (2014-03-22)
Obesity-induced white adipose tissue (WAT) inflammation and insulin resistance are associated with macrophage (Mф) infiltration and phenotypic shift from "anti-inflammatory" M2-like to predominantly "proinflammatory" M1-like cells. Erythropoietin (EPO), a glycoprotein hormone indispensable for erythropoiesis, has biological activities that extend to
Lamia Lamrani et al.
Blood, 124(7), 1136-1145 (2014-06-22)
Thrombosis is common in patients suffering from myeloproliferative neoplasm (MPN), whereas bleeding is less frequent. JAK2(V617F), the main mutation involved in MPN, is considered as a risk factor for thrombosis, although the direct link between the mutation and hemostatic disorders
Léon Kautz et al.
Nature genetics, 46(7), 678-684 (2014-06-02)
Recovery from blood loss requires a greatly enhanced supply of iron to support expanded erythropoiesis. After hemorrhage, suppression of the iron-regulatory hormone hepcidin allows increased iron absorption and mobilization from stores. We identified a new hormone, erythroferrone (ERFE), that mediates
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