Analytical Data
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Gene name
HLA-A*02:01&B2M&Vaccinia Virus(IMYDIINSV) Monomer
- Application
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Alternative Names
HLA-A*0201 & B2M & Vaccinia virus (IMYDIINSV)
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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)&IMYDIINSV
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Molecular Weight
38-41 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 study of the HLA-A*02:01/B2M/Vaccinia Virus (IMYDIINSV) monomeric recombinant protein is crucial in understanding immune responses to viral infections and developing targeted immunotherapies. HLA-A*02:01 is a prominent human leukocyte antigen (HLA) class I molecule that presents peptide fragments to CD8+ T cells, playing a key role in the adaptive immune response. Its specific involvement in recognizing viral peptides, such as IMYDIINSV derived from the Vaccinia virus, is particularly relevant for vaccine development and therapeutic interventions. The Vaccinia virus, historically utilized as a vaccine against smallpox, presents unique challenges for the immune system, making it an ideal model for studying HLA-peptide interactions and T-cell activation. The production of a monomeric recombinant protein incorporating HLA-A*02:01, beta-2 microglobulin (B2M), and the specific Vaccinia virus epitope enables detailed structural and functional analyses. This approach allows researchers to investigate how this complex interacts with T-cell receptors, subsequently influencing the design of vaccines or immunotherapies aimed at enhancing the immune recognition of viral infections. Overall, understanding the mechanisms underlying these interactions could contribute significantly to advancing strategies for controlling viral diseases and improving vaccine efficacy.
