Analytical Data
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Gene name
HLA-A*02:01&B2M&KRAS G12C(KLVVVGACGV) Monomer
- Application
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Alternative Names
HLA-A*0201 & B2M & KRASG12C (KLVVVGACGV)
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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)&KLVVVGACGV
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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
The study of the HLA-A*02:01/B2M/KRAS G12C (KLVVVGACGV) monomer recombinant protein is pivotal in the field of cancer immunotherapy and precision medicine. Human Leukocyte Antigen (HLA) A*02:01 is one of the most common HLA class I molecules, playing a crucial role in presenting peptide antigens to cytotoxic T cells. The KRAS G12C mutation is prevalent in various cancers, particularly non-small cell lung cancer (NSCLC), and is associated with a poor prognosis. The specific peptide KLVVVGACGV derived from the mutated KRAS protein has been identified as a target for T cell recognition. Studying this monomeric form allows for detailed analysis of the interaction between HLA molecules and tumor-derived peptides, providing insights into T cell activation and immune responses against cancer. This research aims to enhance our understanding of how mutant KRAS peptides can be effectively presented by HLA-A*02:01, paving the way for the development of targeted immunotherapies. By using recombinant proteins, scientists can explore the structure-function relationship of these complexes, potentially leading to novel therapeutic strategies that harness the body’s immune system to eliminate cancer cells harboring the KRAS G12C mutation. This work is essential for creating personalized cancer vaccines and improving the efficacy of immune checkpoint inhibitors, thereby contributing to more effective treatment options for patients with KRAS-driven tumors.
