Recombinant Human EPO-R Protein (Fc Tag)

Name: Recombinant Human EPO-R Protein (Fc Tag)
Brand: Beta LifeScience
SKU: BLA-1356P
Availability: InStock

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

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Product Overview

Host Species	Human
Accession	P19235
Synonym	EPO R EPO Receptor EPO-R epor EPOR_HUMAN Erythropoietin receptor Erythropoietin receptor precursor MGC138358
Description	Recombinant Human EPO-R Protein (Fc Tag) was expressed in HEK293. It is a Protein fragment
Source	HEK293
AA Sequence	Theoretical sequence:APPPNLPDPKFESKAALLAARGPEELLCFTERLEDLVCF WEEAASAGVGPGNYSFSYQLEDEPWKLCRLHQAPTARGAVRFWCSLPT ADTSSFVPLELRVTAASGAPRYHRVIHINEVVLLDAPVGLVARLADES GHVVLRWLPPPETPMTSHIRYEVDVSAGNGAGSVQRVEILEGRTECVL SNLRGRTRYTFAVRARMAEPSFGGFWSAWSEPVSLLTPSDLDPRIPKV DKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEV TCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLT VLHQDWLNGKEYKCRVSNKALPAPIEKTISKAKGQPREPQVYTLPPSR DELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGS FFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
Purity	>95% SDS-PAGE.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	The ED50 of ab84001 is typically 0.15-2.5 ng/ml as measured by its ability to neutralize EPO-mediated proliferation of TF-1 cells.
Formulation	Lyophilised
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. After reconstitution store at -20°C. Avoid freeze / thaw cycle.

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	HGNC: 3416 OMIM: 133100 KEGG: hsa:2057 STRING: 9606.ENSP00000222139 UniGene: Hs.631624
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

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
EpoR role in the proliferation and survival of non-small cell lung cancer cells PMID: 29345289
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
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
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
High EPOR expression is associated with monoclonal gammopathy of undetermined significance and multiple myeloma. PMID: 26919105
EPO-mediated EPOR signaling reduced the viability of myeloma cell lines and of malignant primary plasma cells in vitro PMID: 27581518
this study shows that EPO could directly promote tumor progression via EPO receptor-expressing macrophages PMID: 27262376
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
Overexpression of EPOR is associated with clear cell renal cell carcinoma. PMID: 27468719
HIF-1alpha and EPO-R may be an indicator of the aggressiveness of invasive breast cancers PMID: 27629849
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
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
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
A new point mutation in EPOR induces a short deletion in congenital erythrocytosis. PMID: 26010769
Data show that erythropoietin receptor antagonist EMP9 suppressed hemoglobin synthesis in xenografts of HeLa cells. PMID: 25874769
Data suggest that erythropoietin receptor (EPOR) could be a target to overcome therapeutic resistance toward ionizing radiation or temozolomide. PMID: 25544764
transmembrane domain and the juxtamembrane region of the erythropoietin receptor in micelles PMID: 25418301
while EPO can stimulate NO production, NO in turn can regulate EPOR expression in endothelial cells during hypoxia PMID: 24518819
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
This study reveals high EPOR level as a potential novel positive prognostic marker in human lung lung adenocarcinoma. PMID: 24155958
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
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
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
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
Sp1 may significantly affect the number of EPO-R molecules present on the surface of activated CD4(+) lymphocytes PMID: 23577103
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
TAL1 binds to the EPO-R promoter to activate EPO-R expression PMID: 22982397
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
Erythropoietin is capable of downregulating erythropoietin receptor when it acts early within HepG2 cells. PMID: 22227182
the biology of the EpoR in ovarian cancer cells PMID: 22552716
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
a critical role for membrane raft in recruitment and assembly of Epo-R and signal intermediates into discrete membrane signaling units PMID: 22509308
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
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
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
STAT5 phosphorylation levels of EPO and TPO receptors are elevated in bone marrow cells of patients with paroxysmal nocturnal hemoglobinuria. PMID: 22093990
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
EPOR signalling in tumour cells is involved in the control of glioma growth. PMID: 21749867
EPO-R cytosolic lysine residues enhance receptor function, most probably through ubiquitination and/or other post-translational modifications. PMID: 21291419
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
Detected is a novel heterozygous frameshift mutation in exon 8 of the EPOR resulting in primary familial and congenital polycythaemia. PMID: 21437635
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
High EpoR is associated with angiogenesis in glioma. PMID: 20614229
Tumor vessels exhibited EpoR, pJAK-2, and pSTAT-5 immunoreactivity PMID: 20336349
results suggest that spermatozoa express EPO receptor on plasma membrane, which might act to protect these cells from damage after ejaculation. PMID: 20884294
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
a regulatory role of EPO/EPOR pathway in human circulating endothelial precursors homeostasis PMID: 20700488
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
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.