Analytical Data
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Gene name
HLA-C*08:01&B2M Monomer
- Application
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Alternative Names
HLA-C*0801 & B2M
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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
QOC77848.1 (C25-I308)&P61769
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Expression Region
QOC77848.1 (C25-I308)&P61769 (I21-M119)
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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
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Protein Description
HLA-C*08:01 and β2-microglobulin (β2M) are critical components of the major histocompatibility complex (MHC) class I pathway, playing essential roles in mediating immune responses. HLA-C*08:01, a specific allele of the class I MHC molecule, presents peptides to CD8+ T cells, thus influencing immune recognition and response to pathogens and tumors. The study of its recombinant protein, in conjunction with β2M, is of paramount importance for understanding various immunological processes, including allogeneic transplantation, autoimmune diseases, and viral infections. The development of an HLA-C*08:01/β2M monomer allows for an in-depth analysis of ligand binding, T cell receptor interactions, and the structural dynamics of this crucial immune component. Moreover, elucidating the structure-function relationship of this complex aids in identifying peptide epitopes relevant for therapeutic applications and vaccine design. Enhanced understanding of HLA-C*08:01's diverse roles could provide insights into population-based differences in immune responses and susceptibility to diseases, supporting the advancement of personalized medicine strategies. Thus, the comprehensive study of HLA-C*08:01 and β2M not only contributes to basic immunology knowledge but also to the development of novel therapeutic interventions in various immune-related conditions.
