Analytical Data
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Gene name
HLA-A*11:01&B2M&EBV LMP2(SSCSSCPLSK) Monomer
- Application
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Alternative Names
HLA-A*1101 & B2M & EBV LMP2 (SSCSSCPLSK)
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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
AAV53343.1 (G25-T305)&P61769
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Expression Region
AAV53343.1 (G25-T305)&P61769 (I21-M119)&SSCSSCPLSK
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Molecular Weight
40-43 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
Related Products
Protein Description
The study of HLA-A*11:01, Beta-2-Microglobulin (B2M), and the Epstein-Barr Virus (EBV) LMP2 peptide (SSCSSCPLSK) monomeric recombinant protein is driven by the need to understand the immune response to EBV, a virus associated with various malignancies and autoimmune diseases. HLA-A*11:01 is a class I major histocompatibility complex (MHC) molecule critical for presenting viral antigens to CD8+ cytotoxic T cells, thereby initiating an adaptive immune response. The LMP2 protein, derived from EBV, plays a pivotal role in viral latency and immune evasion. Investigating the interaction between HLA-A*11:01 and the EBV LMP2 peptide offers insights into how the virus eludes immune detection and contributes to pathogenesis. The recombinant production of this protein allows for detailed structural and functional analyses, including binding affinity studies and T cell activation assays, which can elucidate the specificity of T cell responses and the potential for developing targeted immunotherapies. Additionally, this research has implications for vaccine development against EBV and provides a framework for understanding MHC-peptide interactions in the context of viral infections, paving the way for novel strategies to enhance immune recognition and clearance of EBV-associated diseases. Understanding these interactions is critical for harnessing the immune system's power, potentially leading to advancements in treatment and prevention strategies against EBV-related health issues.
