Weight | 1 lbs |
---|---|
Dimensions | 9 × 5 × 2 in |
accession | P19235 |
express system | HEK293 |
product tag | C-hFc-Avi |
purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
background | The erythropoietin (epo) receptor is a member of the cytokine receptor family. It is expressed almost exclusively on erythroid precursor cells and controls the development of red blood cells. The epo receptor has no intrinsic kinase activity, but binds intracellular tyrosine kinases to elicit its signals. Alterations in the transmission of the signalling cascade lead to clinically abnormal red blood cell production. |
molecular weight | The protein has a predicted MW of 52.58 kDa. Due to glycosylation, the protein migrates to 55-70 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Human EPO R/Erythropoietin R Protein 2128
$315.00 – $1,050.00
Summary
- Expression: HEK293
- Functional: Yes (ELISA)
- Amino Acid Range: Ala25-Pro250
Human EPO R/Erythropoietin R Protein 2128
protein |
---|
Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
---|
The erythropoietin (epo) receptor is a member of the cytokine receptor family. It is expressed almost exclusively on erythroid precursor cells and controls the development of red blood cells. The epo receptor has no intrinsic kinase activity, but binds intracellular tyrosine kinases to elicit its signals. Alterations in the transmission of the signalling cascade lead to clinically abnormal red blood cell production. |
Protein names Erythropoietin receptor (EPO-R) |
Gene names EPOR,EPOR |
Protein family Type I cytokine receptor family, Type 1 subfamily |
Mass 9606Da |
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. |
Subellular location Cell membrane; Single-pass type I membrane protein.; [Isoform EPOR-S]: Secreted. Note=Secreted and located to the cell surface. |
Tissues 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 EPOR-T is the most abundant from in early-stage erythroid progenitor cells. |
Structure Forms homodimers on EPO stimulation. The tyrosine-phosphorylated form interacts with several SH2 domain-containing proteins including LYN (By similarity), the adapter protein SH2B2, PTPN6 (By similarity), PTPN11, JAK2, PI3 kinases, STAT5A/B, SOCS3, CRKL (By similarity). Interacts with INPP5D/SHIP1 (By similarity). The N-terminal SH2 domain of PTPN6 binds Tyr-454 and inhibits signaling through dephosphorylation of JAK2 (By similarity). SH2B2 binding also inhibits the JAK-STAT signaling. Binding to PTPN11, preferentially through the N-terminal SH2 domain, promotes mitogenesis and phosphorylation of PTPN11 (By similarity). Binding of JAK2 (through its N-terminal) promotes cell-surface expression (By similarity). Interacts with RHEX; this interaction occurs in a erythropoietin (EPO)-dependent manner (PubMed:25092874). Interaction with the ubiquitin ligase NOSIP mediates EPO-induced cell proliferation. Interacts with ATXN2L. |
Post-translational modification On EPO stimulation, phosphorylated on C-terminal tyrosine residues by JAK2. The phosphotyrosine motifs are also recruitment sites for several SH2-containing proteins and adapter proteins which mediate cell proliferation. Phosphorylation on Tyr-454 is required for PTPN6 interaction, Tyr-426 for PTPN11. Tyr-426 is also required for SOCS3 binding, but Tyr-454/Tyr-456 motif is the preferred binding site.; Ubiquitination at Lys-281 mediates receptor internalization, whereas ubiquitination at Lys-453 promotes trafficking of activated receptors to the lysosomes for degradation (By similarity). Ubiquitinated by NOSIP; appears to be either multi-monoubiquitinated or polyubiquitinated. Ubiquitination mediates proliferation and survival of EPO-dependent cells. |
Domain Th |
Target Relevance information above includes information from UniProt accession: P19235 |
The UniProt Consortium |
Publications
pmid | title | authors | citation |
---|---|---|---|
We haven't added any publications to our database yet. |
relevant to this product |
---|
# | ||
---|---|---|
Please enter your product and batch number here to retrieve product datasheet, SDS, and QC information. |
Only logged in customers who have purchased this product may leave a review.
Reviews
There are no reviews yet.