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HLA-A2:Ig Protein

Spezies: Human Wirt: Escherichia coli (E. coli) Recombinant FACS
Pubmed (2 Referenzen)
Produktnummer ABIN2688824
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  • Target
    HLA-A2:Ig (HLA-A2:Ig Fusion)
    Escherichia coli (E. coli)
    Flow Cytometry (FACS)
    BD™ DimerX
    The HLA-A2:Ig fusion protein consists of three extracellular major histocompatibility complex (MHC) class I HLA-A2 domains that are fused to the VH regions of mouse IgG1. In order for the MHC class I to be functional, i.e., capable of binding peptides, β2 Microglobulin (β2M) must be present. For this reason, BD™ DimerX consists of recombinant HLA-A2:Ig fusion protein, supplemented with recombinant β2M. Recombinant MHC molecules, such as the DimerX fusion protein, are useful for studying T-cell function by immunofluorescent staining and flow cytometric analysis of antigen-specific T cells. The MHC gene locus encodes a group of highly polymorphic, cell-surface proteins that play a broad role in the immune response to protein antigens. MHC molecules function by binding and presenting small antigenic protein fragments to antigen-specific receptors expressed by T cells (TCR). Human (human leukocyte antigen/HLA) and mouse (histocompatibility 2/H-2) MHC molecules are structurally and functionally related proteins that comprise two major classes. Class I MHC molecules consist of two separate polypeptide chains. The class I α chain is an MHC encoded, transmembrane polypeptide containing three extracellular domains: α1, α2, and α3. The second chain consists of a non-MHC encoded polypeptide called β2M. Since β2M does not contain a transmembrane domain, it associates with the α chain through noncovalent interaction. Functionally, class I MHC molecules can bind peptides derived from intracellular antigens (e.g., viral and some bacterial antigens) that are specifically recognized by CD8+ T cells. Class II MHC molecules consist of two different transmembrane proteins that can bind peptide fragments derived from extracellular proteins (e.g., bacteria and fungi) and are specifically recognized by CD4+ T cells. TCR recognize both processed peptides bound to MHC, as well as regions of the MHC molecule itself. CD4 and CD8 accessory molecules strengthen formation of the TCR-MHC complex through their interaction with non-polymorphic regions of the MHC molecule. Schematic representation of the MHC class I:Ig dimeric protein.
    The HLA-A2 protein was expressed together with human β2M in the mouse plasmacytoma cell line, J558L (ATCC TIB-6). The HLA-A2 and β2M polypeptide chains are associated noncovalently as a consequence of their coexpression within J558L cells. The HLA-A2:Ig fusion protein was purified from tissue culture supernatant by affinity chromatography. The purity of the preparation was confirmed by SDS-PAGE.
  • Applikationshinweise
    Optimal working dilution should be determined by the investigator.

    BD™ DimerX: Recombinant Soluble Dimeric Human HLA-A2:Ig Fusion Protein

    Nur für Forschungszwecke einsetzbar
  • Konzentration
    0.5 mg/mL
    4 °C
    Informationen zur Lagerung
    Store undiluted at 4°C.
  • Khilko, Jelonek, Corr, Boyd, Bothwell, Margulies: "Measuring interactions of MHC class I molecules using surface plasmon resonance." in: Journal of immunological methods, Vol. 183, Issue 1, pp. 77-94, (1995) (PubMed).

    Parker, Bednarek, Hull, Utz, Cunningham, Zweerink, Biddison, Coligan: "Sequence motifs important for peptide binding to the human MHC class I molecule, HLA-A2." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 149, Issue 11, pp. 3580-7, (1992) (PubMed).

  • Target
    HLA-A2:Ig (HLA-A2:Ig Fusion)
    Andere Bezeichnung
    HLA-A2:Ig Fusion Protein
    Sub Type
    Influenza Protein
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