H5166
Erythropoietin 人
EPO, recombinant, expressed in HEK 293 cells, suitable for cell culture
别名:
EPO
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关于此项目
Biological source:
human
Recombinant:
expressed in HEK 293 cells
Assay:
≥95% (SDS-PAGE)
Form:
lyophilized powder
Mol wt:
dimer 36 kDa (glycosylated)
Impurities:
≤1 EU/μg
biological source
human
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.
storage temp.
−20°C
Quality Level
Gene Information
human ... EPO(2056)
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 is a glycoprotein that is the principal regulator of red blood cell growth and differentiation.
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.
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).
存储类别
11 - Combustible Solids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
胰岛素激素类产品
常规特殊物品
此项目有
Hal E Broxmeyer
The Journal of experimental medicine, 210(2), 205-208 (2013-02-13)
Erythropoietin (EPO), a humoral regulator of erythropoiesis and replacement therapy for selected red blood cell disorders in EPO-deficient patients, has been implicated in a wide range of activities on diverse cell, tissue, and organ types. EPO signals via two receptors
Dhiraj Joshi et al.
Journal of vascular surgery, 60(1), 191-201 (2013-09-24)
Managing critical limb ischemia (CLI) is challenging. Furthermore, ischemic myopathy prevents good functional outcome after revascularization. Hence, we have focused on limiting the tissue damage rather than angiogenesis, which has traditionally been the motivation to develop nonsurgical treatments for CLI.
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
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
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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