Analytical Data
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Gene name
Erythropoietin receptor/EpoR
- Application
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Species
Dog
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Source
E. coli
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Tag
N- His-GB1 & C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q2KL21
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Expression Region
25-250aa
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Molecular Weight
36.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Erythropoietin receptor (EpoR) is a critical regulator in erythropoiesis, the process of red blood cell production, which is pivotal for maintaining adequate oxygen delivery throughout the body. EpoR is primarily expressed in erythroid progenitor cells in the bone marrow, where it binds to erythropoietin (Epo), a glycoprotein hormone produced by the kidneys in response to low oxygen levels. The EpoEpoR interaction initiates a cascade of signaling pathways, mainly involving the JAK2-STAT5 pathway, which promotes cell proliferation, differentiation, and survival. Research on recombinant EpoR proteins has gained momentum due to their potential therapeutic applications, particularly in treating anemia associated with chronic kidney disease, cancer, or other conditions that impair erythropoiesis. Moreover, understanding EpoR structure and function can provide insights into the development of novel drugs and biotherapeutics. In recent years, advances in recombinant DNA technology and protein expression systems have enabled the production of EpoR proteins for structural and functional studies, allowing researchers to explore their interactions with Epo and other signaling molecules. These studies are crucial for unraveling the complexities of erythropoiesis and for developing effective treatments for related disorders.
