Analytical Data
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Gene name
HLA-C*07:02:01&B2M&RYR (RYRPGTVAL) Monomer
- Application
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Alternative Names
HLA-C*07:02:01 & B2M & RYRPGTVAL
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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
P10321-1 (C25-I308)&P61769
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Expression Region
P10321-1 (C25-I308)&P61769 (I21-M119)&RYRPGTVAL
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Molecular Weight
14 kDa and 42-45 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 HLA-C*07:02:01, B2M, and RYR (RYRPGTVAL) monomer recombinant proteins is crucial for understanding immune responses and disease mechanisms. Human leukocyte antigen (HLA) molecules, especially Class I HLA-C, play a pivotal role in presenting peptides to CD8+ T cells, influencing the immune surveillance of infected or transformed cells. Variations in HLA alleles, like HLA-C*07:02:01, have been associated with different susceptibilities to various diseases, including infections and autoimmune disorders. The β2-microglobulin (B2M) protein is essential for the stability and surface expression of HLA Class I molecules. Therefore, studying the structural and functional aspects of these components aids in elucidating their roles in antigen presentation dynamics. The inclusion of RYR (RYRPGTVAL) as a peptide of interest adds another layer to this research, as specific peptides can modulate immune responses and potentially serve as targets for therapeutic interventions or vaccine design. By producing and characterizing the recombinant monomeric form of these proteins, researchers can investigate their interaction mechanisms, stability, and immunogenic properties, ultimately contributing to our understanding of how genetic variations affect immune responses. This research may not only shed light on fundamental immunological processes but also have implications in personalized medicine, where patient-specific HLA profiles can guide therapeutic strategies in infectious diseases and cancer treatment.
