Recombinant Human EPO-R Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-2273NP
BL-2273NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-2273NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human EPO-R Protein (C-6His)

Beta LifeScience SKU/CAT #: BL-2273NP
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Product Overview

Description Recombinant Human Erythropoietin Receptor is produced by our Mammalian expression system and the target gene encoding Ala25-Pro250 is expressed with a 6His tag at the C-terminus.
Accession P19235
Synonym EpoR; EPO-R; Erythropoietin R; erythropoietin receptor; MGC138358
Gene Background Erythropoietin (Epo), a glycoprotein produced primarily by the kidney, is the principal factor that regulates erythropoiesis by stimulating the proliferation and differentiation of erythroid progenitor cells. The biological effects of Epo are mediated by the erythropoietin receptor (Epo R). The presence of a soluble form of the Epo R has also been detected on human sera. Recombinant soluble Epo R binds Epo with high affinity and is a potent Epo antagonist.
Molecular Mass 25.9 KDa
Apmol Mass 28-38 KDa, reducing conditions
Formulation Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 8% Trehalose, 3% Glycine, 0.05% Tween 80, pH 8.0.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target Function Receptor for erythropoietin. Mediates erythropoietin-induced erythroblast proliferation and differentiation. Upon EPO stimulation, EPOR dimerizes triggering the JAK2/STAT5 signaling cascade. In some cell types, can also activate STAT1 and STAT3. May also activate the LYN tyrosine kinase.; Isoform EPOR-T acts as a dominant-negative receptor of EPOR-mediated signaling.
Subcellular Location Cell membrane; Single-pass type I membrane protein.; [Isoform EPOR-S]: Secreted. Note=Secreted and located to the cell surface.
Protein Families Type I cytokine receptor family, Type 1 subfamily
Database References
Associated Diseases Erythrocytosis, familial, 1 (ECYT1)
Tissue Specificity Erythroid cells and erythroid progenitor cells. Isoform EPOR-F is the most abundant form in EPO-dependent erythroleukemia cells and in late-stage erythroid progenitors. Isoform EPOR-S and isoform EPOR-T are the predominant forms in bone marrow. Isoform EP

Gene Functions References

  1. Here, we present two crystal structures of the human JAK2 FERM and SH2 domains bound to Leptin receptor (LEPR) and Erythropoietin receptor (EPOR), which identify a novel dimeric conformation for JAK2. PMID: 30044226
  2. EpoR role in the proliferation and survival of non-small cell lung cancer cells PMID: 29345289
  3. These results highlight the high intrinsic specificity of transmembrane domain interactions, demonstrate that a single methyl group can dictate specificity, and define the minimal chemical difference that can modulate the specificity of transmembrane domain interactions and the activity of transmembrane proteins. PMID: 28869036
  4. Study reports for the first evidence that EPOR modulates breast cancer cell morphology changes upon tamoxifen treatment, which result in increased formation of cell protrusions and subsequent cell death and, proposes sustained AKT phosphorylation in EPOR-overexpressing cells as a mechanism that can lead to EPOR-induced tamoxifen resistance. PMID: 28714517
  5. Authors retrospectively investigated whether TFR2 isoforms and EPOR are differentially expressed in MDS patients and whether the expression is associated with patients' clinical outcomes. PMID: 26914246
  6. High EPOR expression is associated with monoclonal gammopathy of undetermined significance and multiple myeloma. PMID: 26919105
  7. EPO-mediated EPOR signaling reduced the viability of myeloma cell lines and of malignant primary plasma cells in vitro PMID: 27581518
  8. this study shows that EPO could directly promote tumor progression via EPO receptor-expressing macrophages PMID: 27262376
  9. 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 treatment within a physiological relevant range in humans does not exert direct effects in a subcutaneous WAT. PMID: 27640183
  10. Overexpression of EPOR is associated with clear cell renal cell carcinoma. PMID: 27468719
  11. HIF-1alpha and EPO-R may be an indicator of the aggressiveness of invasive breast cancers PMID: 27629849
  12. These results identify EPOR as the secondbona fidehydroxylation-dependent substrate of VHL that potentially influences oxygen homeostasis and contributes to the complex genotype-phenotype correlation in VHL disease. PMID: 26846855
  13. 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. PMID: 26412593
  14. erythrocyte lineage enforces exclusivity through upregulation of EKLF and its lineage-specific cytokine receptor (EpoR) while inhibiting both FLI-1 and the receptor TpoR (also known as MPL) for the opposing megakaryocyte lineage PMID: 26159733
  15. A new point mutation in EPOR induces a short deletion in congenital erythrocytosis. PMID: 26010769
  16. Data show that erythropoietin receptor antagonist EMP9 suppressed hemoglobin synthesis in xenografts of HeLa cells. PMID: 25874769
  17. Data suggest that erythropoietin receptor (EPOR) could be a target to overcome therapeutic resistance toward ionizing radiation or temozolomide. PMID: 25544764
  18. transmembrane domain and the juxtamembrane region of the erythropoietin receptor in micelles PMID: 25418301
  19. while EPO can stimulate NO production, NO in turn can regulate EPOR expression in endothelial cells during hypoxia PMID: 24518819
  20. In HBV-related HCC, the levels of EpoR mRNA and protein in non-tumour cirrhotic livers were positively correlated with tumour cell differentiation, which is a favourable predictor of disease-specific survival. PMID: 23496059
  21. This study reveals high EPOR level as a potential novel positive prognostic marker in human lung lung adenocarcinoma. PMID: 24155958
  22. 3 novel EPOR mutations in primary familial and congenital polycythemia--Del1377-1411, a C1370A and G1445--were chimerized with EGFR to study signalling and metabolism of the chimeric receptors. PMID: 24533580
  23. Data show that erythropoietin receptor (EPOR) protein is expressed in breast cancer cells, where it appears to promote proliferation by an EPO-independent mechanism in estrogen receptor alpha (ERalpha) expressing breast cancer cells. PMID: 24502950
  24. Epo-R is expressed in bone marrow-derived macrophages from multiple myeloma and monoclonal gammopathy of undetermined significance patients. The Epo/Epo-R pathway may be involved in the regulation of angiogenic response occurring in MM. PMID: 23881169
  25. Data suggest that adipose tissue-specific disruption of EPO receptor does not alter adipose tissue expansion, adipocyte morphology, insulin resistance, inflammation, or angiogenesis. PMID: 23885016
  26. Sp1 may significantly affect the number of EPO-R molecules present on the surface of activated CD4(+) lymphocytes PMID: 23577103
  27. EPOR expression may be involved in tumor progression and proliferation in HER2-positive breast cancer.EPOR contributes to the mechanism of trastuzumab resistance in breast cancer. PMID: 23117856
  28. TAL1 binds to the EPO-R promoter to activate EPO-R expression PMID: 22982397
  29. High EPOR expression in OSCC is associated with an aggressive tumor behavior and poorer prognosis in the univariate analysis among patients with OSCC. PMID: 22639817
  30. Erythropoietin is capable of downregulating erythropoietin receptor when it acts early within HepG2 cells. PMID: 22227182
  31. the biology of the EpoR in ovarian cancer cells PMID: 22552716
  32. The absence of functional Epo receptor activity in human skeletal muscle indicates that the long-term effects are indirect and probably related to an increased oxidative capacity in this tissue PMID: 22384088
  33. a critical role for membrane raft in recruitment and assembly of Epo-R and signal intermediates into discrete membrane signaling units PMID: 22509308
  34. New knowledge concerning regulated EPOR expression and trafficking therefore is provided, together with new insight into mechanisms via which mutated EPOR-T polycythemia alleles dysregulate the erythron. PMID: 22253704
  35. These data support that EpoR is functional in melanoma and EpoR activation may promote melanoma progression, and suggest that Epo may stimulate angiogenesis and increase survival of melanoma cells under hypoxic condition in vivo. PMID: 21860424
  36. The expression of EPOR and TPOR on CD34+ CD59+ bone marrow cells are significantly higher than those on CD34+ CD59- cells of paroxysmal nocturnal hemoglobinuria patients. PMID: 22338178
  37. STAT5 phosphorylation levels of EPO and TPO receptors are elevated in bone marrow cells of patients with paroxysmal nocturnal hemoglobinuria. PMID: 22093990
  38. ETV6-RUNX1 directly activates ectopic expression of a functional EPOR and provides cell survival signals that may contribute critically to persistence of covert premalignant clones in children. PMID: 21900195
  39. EPOR signalling in tumour cells is involved in the control of glioma growth. PMID: 21749867
  40. EPO-R cytosolic lysine residues enhance receptor function, most probably through ubiquitination and/or other post-translational modifications. PMID: 21291419
  41. The Epo/EpoR complex plays a critical role in the adhesion and migration of rat fibroblasts, and its functional inactivation is associated with PLC-gammal-dependent reduction of cell-matrix adhesion and this also affects cell migration. PMID: 21360263
  42. Detected is a novel heterozygous frameshift mutation in exon 8 of the EPOR resulting in primary familial and congenital polycythaemia. PMID: 21437635
  43. EPOR is expressed in cells of acute leukemia, but the expression level in low. The EPOR expression rate shows no significant difference between AML and ALL. PMID: 19099624
  44. High EpoR is associated with angiogenesis in glioma. PMID: 20614229
  45. Tumor vessels exhibited EpoR, pJAK-2, and pSTAT-5 immunoreactivity PMID: 20336349
  46. results suggest that spermatozoa express EPO receptor on plasma membrane, which might act to protect these cells from damage after ejaculation. PMID: 20884294
  47. EpoR signaling is absolutely required for Parvovirus B19 replication in ex vivo-expanded erythroid progenitor cells after initial virus entry and at least partly accounts for the remarkable tropism of B19V infection for human erythroid progenitors. PMID: 20861249
  48. a regulatory role of EPO/EPOR pathway in human circulating endothelial precursors homeostasis PMID: 20700488
  49. Data show that sEpoR is detectable as a 27kDa protein in the serum of dialysis patients, and that higher serum sEpoR levels correlate with increased erythropoietin requirements. PMID: 20169072
  50. EpoR mRNA was detected in essentially all cell types examined, including primary endothelial, renal, cardiac, and neuronal cells but 10- to 100-fold lower than Epo-responsive cells PMID: 20124513


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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.

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