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Human EPOR Protein expressed in Human Cells - ABIN2003291
Jones, DAndrea, Haines, Wong: Human erythropoietin receptor: cloning, expression, and biologic characterization. in Blood 1990
Show all 6 Pubmed References
this study shows that EPO (show EPO Proteins) could directly promote tumor progression via EPO (show EPO Proteins) receptor-expressing macrophages
No evidence of in vivo activation of the Epo-R in WAT could be documented despite detectable levels of Epo-R mRNA. CONCLUSION: Thus, in contradiction to animal studies, Epo (show EPO Proteins) treatment within a physiological relevant range in humans does not exert direct effects in a subcutaneous WAT.
Our results suggest that EPO (show EPO Proteins)/EPOR pathway promotes gastric cancer formation, proliferation, migration, and decreases apoptosis
These results suggest that both EpoR-positive and EpoR-negative cancer cells could be regulated by exogenous Epo (show EPO Proteins). However, an increased response to erythropoietin (show EPO Proteins) was observed in the EpoR-positive cells. Thus, erythropoietin (show EPO Proteins) increases the risk of tumor progression in colon cancer and should not be used to treat anemia in this type of cancer.
Overexpression of EPOR is associated with clear cell renal cell carcinoma (show MOK Proteins).
HIF-1alpha (show HIF1A Proteins) and EPO-R may be an indicator of the aggressiveness of invasive breast cancers
In multivariate survival analysis, age, Epo (show EPO Proteins) and EpoR were independent prognostic factors related to overall survival in hepatocellular carcinoma.
These results identify EPOR as the secondbona fidehydroxylation-dependent substrate of VHL (show VHL Proteins) that potentially influences oxygen homeostasis and contributes to the complex genotype-phenotype correlation in VHL (show VHL Proteins) disease.
We report for a first time that functional EpoR is expressed in human rhabdomyosarcoma cell lines as well as by primary tumors from RMS patients.
erythrocyte lineage enforces exclusivity through upregulation of EKLF (show KLF1 Proteins) and its lineage-specific cytokine receptor (show EBI3 Proteins) (EpoR) while inhibiting both FLI-1 (show FLI1 Proteins) and the receptor TpoR (show MPL Proteins) (also known as MPL (show MPL Proteins)) for the opposing megakaryocyte lineage
these results have revealed that phosphorylation of Tyr (show TYR Proteins)-343, Tyr (show TYR Proteins)-460, and Tyr (show TYR Proteins)-464 in EpoR underlies JAK2 (show JAK2 Proteins) V617F mutant-induced tumorigenesis.
A solution NMR study of the mouse erythropoietin receptor (mEpoR) comprising the transmembrane domain and the juxtamembrane regions reconstituted in dodecylphosphocholine (DPC) micelles.
These data indicate that EpoR signaling is associated with cardiac remodeling following chronic iron deficiency.
We propose that the CID (show CENPA Proteins)-dependent dimerization system combined with the EpoR intracellular domain and the Gata1 (show GATA1 Proteins) gene regulatory region generates a novel peroral strategy for the treatment of anemia.
transmembrane domain and the juxtamembrane region of the erythropoietin receptor in micelles
EpoR and its activity are downstream effectors of Klotho (show KL Proteins) enabling it to function as a cytoprotective protein against oxidative injury.
Expression of EPOR in rod photoreceptors, Muller cells, and amacrine, horizontal, and ganglion cells of the peripheral retina is not required for the maturation, function, and survival of these cells in aging tissue.
Data indicate a Cbl (show CBL Proteins)/p85 (show ECM1 Proteins)/epsin-1 (show EPN1 Proteins) pathway in erythropoietin receptor (EpoR) endocytosis.
Data from knockout mice suggest that adipose tissue-specific disruption of EPO (show EPO Proteins) receptor does not alter adipose tissue expansion, adipocyte morphology, insulin (show INS Proteins) resistance, inflammation, or angiogenesis.
the EPO (show EPO Proteins)-EPOR system may play a role in glucose metabolism within adipocytes.
This gene encodes the erythropoietin receptor which is a member of the cytokine receptor family. Upon erythropoietin binding, this receptor activates Jak2 tyrosine kinase which activates different intracellular pathways including: Ras/MAP kinase, phosphatidylinositol 3-kinase and STAT transcription factors. The stimulated erythropoietin receptor appears to have a role in erythroid cell survival. Defects in the erythropoietin receptor may produce erythroleukemia and familial erythrocytosis. Dysregulation of this gene may affect the growth of certain tumors. Alternate splicing results in multiple transcript variants.
, Erythropoietin receptor
, type I single-transmembrane cytokine receptor
, erythropoietin receptor-like