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CD25 Protein (C-Term, Extracellular Domain)

IL2RA Origine: Souris Hôte: HEK-293T Cells Recombinant > 97 %, as determined by SDS-PAGE and HPLC
N° du produit ABIN1684666
  • Antigène Voir toutes CD25 (IL2RA) Protéines
    CD25 (IL2RA) (Interleukin 2 Receptor, alpha (IL2RA))
    Type de proteíne
    Recombinant
    Attributs du protein
    C-Term, Extracellular Domain
    Origine
    • 17
    • 8
    • 4
    • 2
    • 2
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    Souris
    Source
    • 14
    • 9
    • 8
    • 2
    • 2
    • 1
    • 1
    • 1
    HEK-293T Cells
    Specificité
    Optimized DNA sequence encoding extracellular domain of mouse CD25 including a C-terminal polyHis tag was expressed in HEK293 cells.
    Attributs du produit
    Recombinant mouse CD25 is a monomer protein consisting of23 amino acid residue subunits, due to glycosylation migrates as an approximately 50 kDa protein on SDS-PAGE.
    Pureté
    > 97 %, as determined by SDS-PAGE and HPLC
    Stérilité
    0.2 μm filtered
    niveau d'endotoxine
    Endotoxin content was assayed using a LAL gel clot method. Endotoxin level was found to be less than 0.1 ng/µg(1EU/µg).
    Top Product
    Discover our top product IL2RA Protéine
  • Restrictions
    For Research Use only
  • Buffer
    PBS solution, pH7.2
    Conseil sur la manipulation
    Avoid repeated freeze/thaw cycles.
    Stock
    -20 °C
    Stockage commentaire
    The lyophilized antibody is stable for at least 1 year from date of receipt at -20 °C. Upon reconstitution, this antibody can be stored in working aliquots at - 8 °C for one month, or at -20 °C for six months without detectable loss of activity.
    Date de péremption
    12 months
  • Antigène
    CD25 (IL2RA) (Interleukin 2 Receptor, alpha (IL2RA))
    Autre désignation
    CD25 (IL2RA Produits)
    Sujet
    G-CSF is secreted by monocytes, macrophages, and neutrophils after cell activation. It is produced also by stromal cells, fibroblasts, and endothelial cells. Epithelial carcinomas, acute myeloid leukemia cells and various tumor cell lines. The synthesis of G-CSF can be induced by bacterial endotoxins, TNF, IL1 and GM-CSF. Comparison of the primary sequence of G-CSF with those of the two other colony stimulating factors, GM-CSF and M-CSF, shows that the three factors are not related to each other. Murine and human G-CSF show a sequence homology of approximately 70 % at the DNA level and of 72 % at the protein level. The G-CSF receptorCD114, is expressed on all cells of the neutrophils and granulocytes lineage. It is expressed also in placenta cells, endothelial cells and various carcinoma cell lines. Human G-CSF is active in murine cells and vice versa. G-CSF stimulates the proliferation and differentiation of hematopoietic progenitor cells committed to the neutrophils and granulocytes lineage in a dose-dependent manner.G-CSF synergises with some other cytokines, including GM-CSF and IL4. GM-CSF and G-CSF are required, for example, to develop neutrophilic colonies in vitro. The concerted action of G-CSF and Epo is required to support the growth of mixed colonies of the early erythroid progenitors. A combination of IL4 with G-CSF has been shown to lead to synergistic suppression of the growth of some human leukemic cell lines.
    UniProt
    P01590
    Pathways
    Signalistation JAK/STAT, Growth Factor Binding, Activated T Cell Proliferation
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