Analytical Data
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Gene name
HLA-A*03:01&B2M&KRAS G12V(YMLDLQPET) Monomer
- Application
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Alternative Names
HLA-A*0301 & B2M & KRASG12D (VVVGADGVGK)
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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
P04439-1 (G25-T305)&P61769
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Expression Region
P04439-1 (G25-T305)&P61769 (I21-M119)&YMLDLQPET
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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 HLA-A*03:01 molecule, along with its associated beta-2-microglobulin (B2M), plays a crucial role in the immune response by presenting peptide antigens to T cells. In particular, the KRAS G12V mutation, often associated with various cancers, generates a specific peptide (YMLDLQPET) that can be recognized by T cells in an HLA-A*03:01 context. The study of the HLA-A*03:01/B2M/KRAS G12V (YMLDLQPET) monomeric recombinant protein is vital for understanding tumor immunology and developing targeted immunotherapies. As KRAS mutations are prevalent in cancers such as pancreatic, colorectal, and lung cancer, this research may pave the way for new therapeutic strategies, including vaccination approaches that can elicit a potent immune response against tumor cells displaying this neoantigen. By characterizing the binding affinity and stability of the KRAS G12V peptide with the HLA-A*03:01 molecule, researchers can better comprehend how to harness the immune system to recognize and destroy cancer cells, ultimately improving treatment outcomes for patients with KRAS-driven tumors. Additionally, this work contributes to the broader field of personalized medicine, where targeting specific mutations can enhance the efficacy of immunotherapies.
