EpoR Antibody (YA9282)
(Synonyms: Erythropoietin receptor, EPO-R, EPOR)Based on 1 Customer Validation
EpoR Antibody (YA9282) is a Mouse-derived and non-conjugated IgG3 monoclonal antibody, targeting to EpoR.
-
Host:
Mouse
-
Isotype:
IgG
-
Application:
ICC/IF, IF-Tissue, IP, ELISA
-
Reactivity :
human
-
Formulation:
Supplied in PBS(pH7.4) containing 0.1% gelatin and < 0.1% sodium azide.
-
Conjugation:
Non-conjugated
Applications
| Application |
ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
IF-Tissue
IF-Tissue: Immunofluorescence-Tissue
|
IP
IP: Immunoprecipitation
|
ELISA
ELISA: Enzyme Linked Immunosorbent Assay
|
|---|---|---|---|---|
| Dilution Ratio | 1:50-500 | 1:50-500 | 1-2μg per 100-500μg Total protein | 1:50-3000 |
Product Details
EpoR Antibody (YA9282) is a Mouse-derived and non-conjugated IgG3 monoclonal antibody, targeting to EpoR.
-
Host Mouse
-
Species Reactivityhuman
-
Calculated Molecular Weight Predicted band size: 55 kDa
OMIM: 133171
A synthesized peptide derived from human EpoR.
Endogenous
Affinity purified
Non-conjugated
Unmodified
IgG
Product Properties
-
Appearance
Solution
-
Formulation
Supplied in PBS(pH7.4) containing 0.1% gelatin and < 0.1% sodium azide.
-
Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
-
Storage & Stability
Stored at 2-8°C for 1 year, do not freeze.
-
Shipping
Shipping with blue ice.
Background
-
Function
EpoR is a Receptor for erythropoietin, which mediates erythropoietin-induced erythroblast proliferation and differentiation. Upon EPO stimulation, EPOR dimerizes triggering the JAK2/STAT5 signaling cascade (By similarity). In some cell types, can also activate STAT1 and STAT3. May also activate the LYN tyrosine kinase (By similarity)[1][2][3][4][5][6].
-
Subcellular Localization
Cell membrane
-
Expression
Tissue_Specificity: Erythroid cells and erythroid progenitor cells. -
Isoforms & Post-Translational Modification
EpoR has 3 isoforms, P19235-1: amino acid length is 508, molecular weight is 55065 Da (predicted); P19235-2: amino acid length is 241, molecular weight is 26456 Da (predicted); P19235-3: amino acid length is 328, molecular weight is 35809 Da (predicted).
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. Tyr-426 is also required for SOCS3 binding, but Tyr-454/Tyr-456 motif is the preferred binding site -
Subunit
Forms homodimers on EPO stimulation.
-
SwissProt ID
-
Synonyms
Erythropoietin receptor, EPO-R, EPOR
Documentation
-
Data Sheet (260 KB)
-
SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
-
User Guide for Antibodies (1077 KB)
References
[1]. Zhan H, et al. Engineering a soluble extracellular erythropoietin receptor (EPObp) in Pichia pastoris to eliminate microheterogeneity, and its complex with erythropoietin. Protein Eng. 1999 Jun;12(6):505-13. [Content Brief]
[2]. Winkelmann JC, et al. The gene for the human erythropoietin receptor: analysis of the coding sequence and assignment to chromosome 19p. Blood. 1990 Jul 1;76(1):24-30. [Content Brief]
[3]. Jones SS, et al. Human erythropoietin receptor: cloning, expression, and biologic characterization. Blood. 1990 Jul 1;76(1):31-5. [Content Brief]
[4]. Middleton SA, et al. Identification of a critical ligand binding determinant of the human erythropoietin receptor. Evidence for common ligand binding motifs in the cytokine receptor family. J Biol Chem. 1996 Jun 14;271(24):14045-54. [Content Brief]
[5]. Syed RS, et al. Efficiency of signalling through cytokine receptors depends critically on receptor orientation. Nature. 1998 Oct 1;395(6701):511-6. [Content Brief]
[6]. Kirito K, et al. Identification of the human erythropoietin receptor region required for Stat1 and Stat3 activation. Blood. 2002 Jan 1;99(1):102-10. [Content Brief]