Recombinant Human Erythropoietin (EPO) Protein (His), Active

Name: Recombinant Human Erythropoietin (EPO) Protein (His), Active
Brand: Beta LifeScience
SKU: BLC-05911P
Availability: InStock

Greater than 95% as determined by SDS-PAGE.

Collections: Cytokines, Cytokines and growth factors, Growth factors and receptors, Recombinant proteins

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Product Overview

Description	Recombinant Human Erythropoietin (EPO) Protein (His), Active is produced by our Mammalian cell expression system. This is a full length protein.
Purity	Greater than 95% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	The ED50 as determined in a cell proliferation assay using TF-1 human erythroleukemic cells is less than 5 ng/ml
Uniprotkb	P01588
Target Symbol	EPO
Synonyms	EPOErythropoietin; Epoetin
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	C-6His
Complete Sequence	APPRLICDSRVLERYLLEAKEAENITTGCAEHCSLNENITVPDTKVNFYAWKRMEVGQQAVEVWQGLALLSEAVLRGQALLVNSSQPWEPLQLHVDKAVSGLRSLTTLLRALGAQKEAISPPDAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEACRTGDR
Expression Range	28-193aa
Protein Length	Full Length of Mature Protein
Mol. Weight	19.2 kDa
Research Area	Signal Transduction
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 μm filtered 1xPBS, pH 7.4
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Hormone involved in the regulation of erythrocyte proliferation and differentiation and the maintenance of a physiological level of circulating erythrocyte mass. Binds to EPOR leading to EPOR dimerization and JAK2 activation thereby activating specific downstream effectors, including STAT1 and STAT3.
Subcellular Location	Secreted.
Protein Families	EPO/TPO family
Database References	HGNC: 3415 OMIM: 133170 KEGG: hsa:2056 STRING: 9606.ENSP00000252723 UniGene: Hs.2303
Associated Diseases	Microvascular complications of diabetes 2 (MVCD2)
Tissue Specificity	Produced by kidney or liver of adult mammals and by liver of fetal or neonatal mammals.

Gene Functions References

Increases in plasma erythropoietin and erythropoietin receptor activation are mechanisms implicated in the increase of plasma FGF23 in acute kidney injury. PMID: 29395333
the implication of alpha-7-nAChR-JAK-2/STAT-3-Nrf-2 signaling cascade in the radiomitigative potential of EPO against ARS PMID: 29220591
Pro-inflammatory proteins S100A9 and tumor necrosis factor-alpha suppress erythropoietin elaboration in myelodysplastic syndromes PMID: 28983059
EPO levels in the coronary artery disease (CAD) group were higher than those in the non-CAD group. The correlation between red cell distribution width and EPO levels was statistically significant among CAD patients. PMID: 28885393
CD133(+) cells contributed to the local production of erythropoietin, as observed by detection of circulating human erythropoietin. CD133(+) cells appear therefore an effective source for cell repair, able to restore renal functions, including erythropoietin release, and to limit long term maldifferentiation and fibrosis. PMID: 27853265
Circulating anti-EPO are detected in a significant proportion of treatment-naive HCV-infected patients and are independently associated with anemia, suggesting a further implication of autoimmunity in the pathophysiology of HCV-related anemia. PMID: 28603097
the T allele of SNP rs60684937 located at 67,419,130 bp on chromosome 17 was associated with increased plasma EPO and a relatively increased expression of a non-coding transcript of PRKAR1A in sickle cell disease patients PMID: 28173069
study describes a gain-of-function variant in EPO in an extended kindred with familial erythrocytosis, including 10 affected family members in four generations; this mutation, a single-nucleotide deletion (c.32delG), introduces a frameshift in exon 2 PMID: 29514032
Here, using zebrafish, murine, and human models, the authors show that erythropoietin (EPO) signaling, together with the GATA1 transcriptional target, AKAP10, regulates heme biosynthesis during erythropoiesis at the outer mitochondrial membrane. PMID: 28553927
Reduction in central venous blood pressure prompts an increase in plasma EPO concentration independent of hemoconcentration and hence suggests CVP per se as an acute regulator of EPO synthesis PMID: 27169519
EPO (7q22) and SEC-61(7p11) emerged as new candidate genes susceptible to genetic losses with 57.7% deletions identified in regions on chromosome 7. PMID: 27282568
The current controversy may derive from a context-dependent mode of action of Epo, namely opposite skeletal actions during bone regeneration and steady-state bone remodeling. PMID: 26822707
High EPO expression is associated with monoclonal gammopathy of undetermined significance and multiple myeloma. PMID: 26919105
age 3 plasma levels of EPO were found related to childhood asthma PMID: 27434124
EPO induces an EMT-like process in mammary non-tumorigenic epithelial cells PMID: 28247960
these results suggested that quercetin's cytoprotective effects in HepG2 cells are mediated via EPO production. PMID: 29080630
Serum Epo and VEGF may be markers of severity of hypoxia-ischaemia and brain injury as they are closely related to hypoxic exposure. PMID: 27902983
CIS interacted with phosphorylated EpoR at Y401, which was critical for the activation of STAT5 and ERK. PMID: 28038963
EPO dependent regulation pathway of FGF23 gene expression PMID: 29073196
Fetal plasma EPO concentrations are selectively increased in monochorionic twin pregnancies with intrauterine growth restriction. PMID: 27161360
this study shows that EPO is involved in the pathogenesis of sepsis-induced acute kidney injury PMID: 27266727
Erythropoietin is superior to the standard prognostic scores in predicting 28-day mortality in patients with acute-on-chronic liver failure. PMID: 27981303
EPO levels were also found correlated positively with heme, TNF-alpha, IL-10, IP-10 and MCP-1 during cerebral malaria. PMID: 27441662
Three single nucleotide polymorphisms are associated with increased risk of diabetic retinopathy in a Chinese Han population. PMID: 27190272
Pharmacokinetic animal studies revealed strongly 15.6-fold plasma half-life extension for the PASylated EPO (83.16 +/- 13.28 h) in comparison to epoetin alpha (8.5 +/- 2.4 h) and darbepoetin alpha (25.3 +/- 2.2h). PMID: 28168382
Secreted MIR122 reached the kidney and reduced expression of erythropoietin, contributing to inflammation-induced anemia. PMID: 27477940
this paper shows that Epo could directly down-regulate pro-inflammatory T cell responses without affecting T cell activation status PMID: 27208431
findings suggest that erythropoietin levels in anemia of unknown etiology, although elevated, remain inappropriately low, particularly when compared with other forms of anemia. This suggests a relative erythropoietin deficiency or a blunted erythroid cell response. PMID: 26747131
Plasma IGFBP-1 was significantly associated with plasma EPO concentration in acute kidney injury, suggesting an unknown mechanism related to systemic stress conditions for EPO regulation in AKI. PMID: 26479890
Our results suggest that EPO/EPOR pathway promotes gastric cancer formation, proliferation, migration, and decreases apoptosis PMID: 27086036
These results suggest that both EpoR-positive and EpoR-negative cancer cells could be regulated by exogenous Epo. However, an increased response to erythropoietin was observed in the EpoR-positive cells. Thus, erythropoietin increases the risk of tumor progression in colon cancer and should not be used to treat anemia in this type of cancer. PMID: 27543111
Overexpression of EPO is associated with clear cell renal cell carcinoma. PMID: 27468719
EPO may play an important role in stem cell mobilization through up regulating HGF in mesenchymal stem cells and inducing migration of hematopoietic stem/progenitor cells PMID: 27865586
A review of contemporary aspects of EPO relating to chronic liver disease. [review] PMID: 26919118
Hepatic EPO synthesis is not enhanced in cirrhosis. PMID: 26924722
Conclusion: Anemia in cancers was not because of inadequate Epo or Fe levels, but because of improper Epo response. PMID: 26838000
In multivariate survival analysis, age, Epo and EpoR were independent prognostic factors related to overall survival in hepatocellular carcinoma. PMID: 26097591
Suggest that hypoxia prevents EPO suppression, and exaggerates the plasma volume reduction induced by bed rest. PMID: 27081163
Inadequate erythropoietin response may partly explain anemia in anorexia nervosa. PMID: 26049959
these findings suggest that TGF-beta suppression and EPO stimulation promote erythropoiesis of CD34(+)CD31(+) progenitor cells derived from hPSCs. PMID: 26012423
Our findings have important potential clinical implications, indicating that EPO supplementation in rhabdomyosarcoma patients may have the unwanted side effect of tumor progression. PMID: 26412593
suggest that rhEPO regulates apoptosis-related genes and affects apoptosis in the hippocampus of aging rats by upregulating SIRT. PMID: 26261574
Higher levels of endogenous erythropoietin are associated with incident heart failure in older adults. PMID: 26721912
Erythropoietin protects mouse renal tubular basement membrane by promoting bone marrow cells to generate and secrete miR-144, which, in turn, inhibits activation of the tPA/MMP9-mediated proteolytic network. PMID: 26469975
The review describes the induction of erythropoietin gene expression in liver, reproouctive and hemopoietic systems during hypoxia or a state of proliferation. PMID: 26995951
Our data suggest that rs507392 and rs551238 in the erythropoietin gene probably act to lessen the risk for diabetic retinopathy (DR) in a Chinese cohort with type 2 diabetes mellitus (T2DM). PMID: 25675872
Data suggest maternal circulating 25-hydroxyvitamin D during mid-pregnancy and at delivery is inversely related to serum EPO; an indirect relation observed between circulating vitamin D and circulating hemoglobin is at least partly mediated by EPO. PMID: 26447159
This review gleans these different strategies and highlights the leading molecular recognition elements that have potential roles in rHuEPO doping detection. PMID: 25058943
The addition of salt (even low concentrations of the strong chaotrope salt guanidinium hydrochloride) also exponentially decreased the initial rate of soluble erythropoietin non-native aggregation at 37 degrees C storage PMID: 25628168
In very preterm infants, whether elevated perinatal erythropoietin (EPO) concentrations are associated with increased risks of indicators of brain damage, was determined. PMID: 25793991

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.