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EPO Protéine

EPO Origine: Humain Hôte: CHO Cells Recombinant > 98 % by SDS-PAGE and HPLC analyses. Active
N° du produit ABIN871802
  • Antigène Voir toutes EPO Protéines
    EPO (Erythropoietin (EPO))
    Type de proteíne
    Recombinant
    Activité biologique
    Active
    Origine
    • 15
    • 9
    • 6
    • 4
    • 3
    • 3
    • 2
    • 2
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    Humain
    Source
    • 19
    • 15
    • 7
    • 7
    • 3
    • 2
    • 1
    • 1
    • 1
    CHO Cells
    Séquence
    APPRLICDSR VLERYLLEAK EAENITTGCA EHCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQPWEP LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGDR
    Pureté
    > 98 % by SDS-PAGE and HPLC analyses.
    Stérilité
    0.2 μm filtered
    niveau d'endotoxine
    Less than 1EU/µg of rHuEPO-alpha as determined by LAL method.
    Top Product
    Discover our top product EPO Protéine
  • Restrictions
    For Research Use only
  • Format
    Lyophilized
    Reconstitution
    We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at < -20° C. Further dilutions should be made in appropriate buffered solutions.
    Stock
    4 °C/-20 °C
  • Antigène
    EPO (Erythropoietin (EPO))
    Autre désignation
    EPO (EPO Produits)
    Synonymes
    EPO Protein, EP Protein, MVCD2 Protein, erythropoietin Protein, erythropoietin S homeolog Protein, erythropoietin a Protein, EPO Protein, epo Protein, epo.S Protein, Epo Protein, epoa Protein
    Classe de substances
    Hormone
    Sujet
    Erythropoietin (EPO), a glycoprotein produced primarily by the kidney, is the principal factor that regulates erythropoiesis by stimulating the proliferation and differentiation of erythroid progenitor cells. The production of EPO by kidney cells is increased in response to hypoxia or anemia. Recombinant EPO has been approved for the treatment of anemia associated with chronic renal failure as well as for anemia of AZT treated AIDS patients. The cDNAs for EPO have been cloned from human, murine, canine, etc. The mature proteins from the various species are highly conserved, exhibiting greater than 80% sequence identity at the amino acid level. Human EPO cDNA encodes a 193 amino acid residue precursor protein that is processed to yield a 165 amino acid residue mature protein. EPO contains one O-linked and three N-linked glycosylation sites. Glycosylation of EPO is required for EPO biological activities in vivo. EPO exhibits structural as well as amino sequence identity to the amino terminal 153 amino acid region of thrombopoietin.
    Pathways
    Signalistation JAK/STAT, Hormone Activity, Negative Regulation of intrinsic apoptotic Signaling, Negative Regulation of Transporter Activity
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