Analytical Data
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Gene name
HLA-A*02:01&B2M&P53 R175H(HMTEVVRHC) Monomer
- Application
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Alternative Names
MHC; HLA-A; P53; TP53; Antigen NY-CO-13; BCC7; FLJ92943; LFS1; TRP53
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Species
Human
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Source
HEK293
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Tag
C-Avi;C-8*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A0A140T913 (G25-T305)&P61769
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Expression Region
A0A140T913 (G25-T305)&P61769 (I21-M119)&HMTEVVRHC
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Molecular Weight
51-60 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-A*02:01 in conjunction with beta-2-microglobulin (B2M) and the p53 R175H mutant protein (HMTEVVRHC) is critical due to their roles in immune response and cancer biology. HLA-A*02:01 is one of the most prevalent human leukocyte antigen (HLA) class I molecules, crucial for presenting peptides to cytotoxic T lymphocytes, thereby initiating immune responses against tumors. The p53 tumor suppressor gene is frequently mutated in cancers, with the R175H variant significantly affecting its function and stability, leading to oncogenesis. Understanding the structure and interaction of the HLA-A*02:01/B2M complex with the p53 R175H peptide is essential for developing immunotherapies, as it aids in defining how the immune system recognizes cancerous cells. The monomeric recombinant protein of this complex provides a valuable tool for structural and functional studies. This research can facilitate the design of targeted therapies and vaccines that enhance the immune system's ability to recognize and destroy p53-mutant tumors, ultimately improving cancer treatment outcomes. The insights gained from this study not only contribute to our understanding of tumor immunogenicity but also hold potential for devising innovative strategies in cancer immunotherapy.
