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Mouse (Murine) EPO Protein expressed in CHO Cells - ABIN2666935
Shoemaker, Mitsock: Murine erythropoietin gene: cloning, expression, and human gene homology. in Molecular and cellular biology 1986
Show all 8 references for ABIN2666935
Rat (Rattus) EPO Protein expressed in CHO Cells - ABIN2666807
Nagao, Suga, Okano, Masuda, Narita, Ikura, Sasaki: Nucleotide sequence of rat erythropoietin. in Biochimica et biophysica acta 1992
Show all 6 references for ABIN2666807
Mouse (Murine) EPO Protein expressed in Escherichia coli (E. coli) - ABIN1305139
JACOBSON, GOLDWASSER, FRIED, PLZAK: Role of the kidney in erythropoiesis. in Nature 1957
Show all 6 references for ABIN1305139
Human EPO Protein expressed in CHO Cells - ABIN2666933
Chin, Yu, Beleslin-Cokic, Liu, Shen, Mohrenweiser, Noguchi: Production and processing of erythropoietin receptor transcripts in brain. in Brain research. Molecular brain research 2000
Show all 6 references for ABIN2666933
Human EPO Protein expressed in Wheat germ - ABIN1352975
Zhang, Wang, Wang, Shi, Deng, Fu: rhEPO/EPO discrimination with ultrasensitive electrochemical biosensor based on sandwich-type nano-Au/ZnO sol-gel/nano-Au signal amplification. in Biosensors & bioelectronics 2013
Human EPO Protein expressed in HEK-293 Cells - ABIN2181033
FRIED, GOLDWASSER, JACOBSON, PLZAK: Studies on erythropoiesis. III. Factors controlling erythropoietin production. in Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.) 1957
Data show that erythropoietin (EPO) mRNA was upregulated in the lung, from the metamorphic climax (stage 60) onward.
Three single nucleotide polymorphisms are associated with increased risk of diabetic retinopathy in a Chinese Han population.
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).
Secreted MIR122 reached the kidney and reduced expression of erythropoietin, contributing to inflammation-induced anemia.
this paper shows that Epo could directly down-regulate pro-inflammatory T cell responses without affecting T cell activation status
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.
Plasma IGFBP-1 (show IGFBPI Proteins) 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.
Our results suggest that EPO/EPOR (show EPOR Proteins) pathway promotes gastric cancer formation, proliferation, migration, and decreases apoptosis
These results suggest that both EpoR (show EPOR Proteins)-positive and EpoR (show EPOR Proteins)-negative cancer cells could be regulated by exogenous Epo. However, an increased response to erythropoietin was observed in the EpoR (show EPOR Proteins)-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.
Overexpression of EPO is associated with clear cell renal cell carcinoma (show MOK Proteins).
EPO may play an important role in stem cell mobilization through up regulating HGF (show HGF Proteins) in mesenchymal stem cells and inducing migration of hematopoietic stem/progenitor cells
This study showed that polycythemia alone and increased levels of plasma Epo blunt the hypercapnic ventilatory response (HCVR); mice with an augmented level of cerebral Epo also had a decreased HCVR.
Epo gene regulation in EPO-producing cells is a complex process that utilizes multiple regulatory influences.
this study shows that EPO could directly promote tumor progression via EPO receptor-expressing macrophages
pharmacologic downstream inhibition of the Bmp-Smad (show SMAD1 Proteins) pathway by dorsomorphin, which targets the BMP receptors, improves the hepcidin (show HAMP Proteins) responsiveness to EPO in Tmprss6 (show TMPRSS6 Proteins) KO mice.
In mice, inflammation increases blood levels of MIR122, which reduces expression of Epo in the kidney.
findings reveal a novel function of LRRK2 (show LRRK2 Proteins) in regulating EPO expression and imply a potentially novel relationship between PD genes and hematopoiesis.
PI3K, MAPK/ERK (show MAPK1 Proteins) 1 (show MAPK3 Proteins)/2, and p38 (show CRK Proteins)-signaling proteins are not the main regulators of local production of erythropoietin after 30% loss of circulating blood volume.
The here presented data unearthed EPO-dependent erythroferrone expression acts as an erythropoiesis-driven regulator of iron metabolism under phenylhydrazine-induced hemolytic anemia.
genetic analysis suggests that tubulointerstitial cellular crosstalk modulates renal EPO production under conditions of epithelial HIF activation in the kidney.
DNA methyltransferase (show DNMT1 Proteins) inhibition restores erythropoietin production in fibrotic murine kidneys
EPO might play a role as a survival factor or as a mitogen in developing cartilage tissue.
Pyruvate-fortified cardioplegia evokes myocardial erythropoietin signaling in swine undergoing cardiopulmonary bypass.
A single intramuscular injection of recombinant adeno (show ADORA2A Proteins)-associated virus carrying mutant Epo (R76E) preserves retinal ganglion cells and visual function in glaucomatous mice.
The zebrafish epo cDNA was cloned and the expression of zepo mRNA was mainly in the heart and liver.
characterization of zebrafish epo and epor (show EPOR Proteins) demonstrates the conservation of an ancient program that ensures proper red blood cell numbers during normal homeostasis and under hypoxic conditions
This gene is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. The protein is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. This protein also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.