Analytical Data
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Gene name
HLA-A*02:01&B2M&EBV EBNA(FMVFLQTHI) Monomer
- Application
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Alternative Names
HLA-A*0201 & B2M & EBV EBNA (FMVFLQTHI)
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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)&FMVFLQTHI
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Molecular Weight
41-43 kDa and 10 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
The HLA-A*02:01/B2M/EBV EBNA (FMVFLQTHI) monomeric recombinant protein is critical for advancing our understanding of immune recognition and response to Epstein-Barr Virus (EBV) infections, which are linked to various cancers and other diseases. HLA-A*02:01 is one of the most common human leukocyte antigen (HLA) class I molecules, playing a pivotal role in presenting peptide antigens to CD8+ T cells. The EBV EBNA (Epstein-Barr Nuclear Antigen) peptide, specifically FMVFLQTHI, is recognized by cytotoxic T lymphocytes (CTLs, a key component of the immune system), highlighting its potential as a target for immunotherapy. By developing a monomeric form of this complex, researchers aim to facilitate structural and functional studies that enhance the understanding of peptide-HLA interactions. This knowledge is not only crucial for vaccine development and therapeutic strategies against EBV-associated malignancies but also provides insights into peptide presentation mechanisms and CTL activation. The recombinant protein can serve as a valuable tool in assessing T cell responses in various clinical settings, fostering advancements in personalized medicine and cancer immunotherapy.
