Cat: IPD-X29806

Recombinant Human HLA-A*02:01&B2M&Vaccinia Virus(VLYNGVNYL) Monomer Protein (HEK293),Avi & His

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Analytical Data

  • Gene name

    HLA-A*02:01&B2M&Vaccinia Virus(VLYNGVNYL) Monomer

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    HLA-A*0201 & B2M & Vaccinia virus (VLYNGVNYL)

  • Species

    Human

  • Source

    HEK293

  • Tag

    C-Avi;C-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    AAA59606.1 (G25-I308)&P61769

  • Expression Region

    AAA59606.1 (G25-I308)&P61769 (I21-M119)&VLYNGVNYL

  • Molecular Weight

    40-43 kDa and 10 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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.

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Protein Description

The study of HLA-A*02:01 and its interaction with the β2-microglobulin (B2M) is pivotal in understanding immune responses, particularly in the context of viral infections. HLA-A*02:01 is one of the most prevalent human leukocyte antigen (HLA) class I molecules, crucial for presenting peptides derived from intracellular pathogens, such as viruses, to CD8+ cytotoxic T lymphocytes. The incorporation of viral peptides, such as the YLAKLTALV epitope derived from the Vaccinia virus, into the HLA-A*02:01 structure significantly enhances our understanding of how the immune system recognizes and combats viral infections. Research on monomeric recombinant proteins of HLA-A*02:01 in complex with B2M and the Vaccinia virus peptide provides valuable insights into the molecular mechanisms of immune recognition. This knowledge is vital for developing effective vaccines and immunotherapies against viral diseases, leveraging the strength of the adaptive immune system to elicit targeted responses. Moreover, studying the stability and conformation of these complexes expands our comprehension of peptide-MHC interactions and informs therapeutic strategies aimed at manipulating immune responses in various contexts, including cancer and infectious diseases. The characterization of the HLA-A*02:01/B2M/Vaccinia virus (YLAKLTALV) monomer not only deepens our fundamental understanding of T-cell activation but also holds promise for clinical applications in designing more effective immunotherapeutic agents.

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