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EPO Protein (His tag)

Protéine Recombinant EPO exprimée dans Escherichia coli (E. coli).
N° du produit ABIN7668705

Aperçu rapide pour EPO Protein (His tag) (ABIN7668705)

Antigène

Voir toutes EPO Protéines
EPO (Erythropoietin (EPO))

Type de proteíne

Recombinant

Activité biologique

Inactive

Origine

  • 18
  • 12
  • 5
  • 4
  • 3
  • 3
  • 2
  • 2
  • 2
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
Humain

Source

  • 20
  • 15
  • 9
  • 8
  • 4
  • 2
  • 1
  • 1
  • 1
Escherichia coli (E. coli)

Pureté

> 95 %
  • Purification/Conjugué

    Cette EPO protéine est marqué à la His tag.

    Fonction

    Recombinant Human EPO protein (His tag)

    Séquence

    Ala 28-Arg 193

    Stérilité

    0.2 μm filtered

    niveau d'endotoxine

    < 10 EU/mg of the protein as determined by the LAL method.
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  • Restrictions

    For Research Use only
  • Format

    Lyophilized

    Reconstitution

    It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis.

    Buffer

    Lyophilized from sterile PBS, pH 7.4.
    Normally 5 % -8 % trehalose, mannitol and 0.01 % Tween 80 are added as protectants before lyophilization.

    Stock

    4 °C,-20 °C,-80 °C

    Stockage commentaire

    Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.

    Date de péremption

    12 months
  • Antigène

    EPO (Erythropoietin (EPO))

    Autre désignation

    EPO

    Classe de substances

    Hormone

    Sujet

    Erythropoietin (EPO) is a 34 kDa glycoprotein hormone in the type I cytokine family and is related to thrombopoietin. Its three N-glycosylation sites, four alpha helices, and N-to C-terminal disulfide bond are conserved across species. Glycosylation of the EPO protein is required for biological activities in vivo. The mature human EPO protein shares 75 % -84 % amino acid sequence identity with bovine, canine, equine, feline, mouse, ovine, porcine, and rat EPO. EPO is primarily produced in the kidney by a population of fibroblast-like cortical interstitial cells adjacent to the proximal tubules. It is also produced in much lower, but functionally significant amounts by fetal hepatocytes and in adult liver and brain. EPO promotes erythrocyte formation by preventing the apoptosis of early erythroid precursors which express the erythropoietin receptor (EPO R). EPO R has also been described in brain, retina, heart, skeletal muscle, kidney, endothelial cells, and a variety of tumor cells. Ligand induced dimerization of EPO R triggers JAK2-mediated signaling pathways followed by receptor/ligand endocytosis and degradation. Rapid regulation of circulating EPO allows tight control of erythrocyte production and hemoglobin concentrations. Anemia or other causes of low tissue oxygen tension induce erythropoietin production by stabilizing the hypoxia-induceable transcription factors HIF-1 alpha and HIF-2 alpha. EPO additionally plays a tissue-protective role in ischemia by blocking apoptosis and inducing angiogenesis.,EPO,Epoetin,Erythropoietin

    Poids moléculaire

    calculated_mw: 18.2 kDa

    observed_mw: 20 kDa

    UniProt

    P01588

    Pathways

    Signalistation JAK/STAT, Hormone Activity, Negative Regulation of intrinsic apoptotic Signaling, Negative Regulation of Transporter Activity
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