Analytical Data
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Gene name
HLA-A*02:01&B2M&EBV LMP2A(CLGGLLTMV) Monomer
- Application
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Alternative Names
HLA-A*0201 & B2M & EBV LMP2A (CLGGLLTMV)
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Species
Human
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Source
HEK293
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Tag
C-Avi;C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
AAA59606.1 (G25-I308)&P61769
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Expression Region
AAA59606.1 (G25-I308)&P61769 (I21-M119)&CLGGLLTMV
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Molecular Weight
40-43 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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.
Quality inspection process
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Protein Description
HLA-A*02:01 is a highly prevalent human leukocyte antigen (HLA) class I molecule that plays a crucial role in the immune response by presenting antigens to CD8+ T cells. The binding affinity and presentation of specific peptide ligands, such as the Epstein-Barr virus (EBV) latent membrane protein 2A (LMP2A) peptide (CLGGLLTMV), are vital for T cell recognition and subsequent immune activation. The study of HLA-A*02:01 in conjunction with beta-2-microglobulin (B2M), a component essential for the stability and surface expression of HLA molecules, is fundamental for understanding immune surveillance against EBV-associated malignancies. Monomeric recombinant proteins of HLA-A*02:01 and B2M, when complexed with the LMP2A peptide, facilitate the investigation of T cell responses in vitro and serve as potential candidates for immunotherapy. This research is particularly relevant given the association of EBV with various cancers, including Hodgkin's lymphoma and nasopharyngeal carcinoma. By elucidating the molecular interactions and the immunological implications of this HLA-peptide complex, researchers aim to advance the development of targeted therapeutic strategies that harness the immune system to combat EBV-related diseases.
