Analytical Data
-
Gene name
HLA-A*24:02&B2M&p53 Monomer(TYSPALNKMF)
- Application
-
Alternative Names
HLA-A*2402 & B2M & p53 (TYSPALNKMF)
-
Species
Human
-
Source
HEK293
-
Tag
C-Avi;C-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
AAA59600.1 (G25-T305)&P61769
-
Expression Region
AAA59600.1 (G25-T305)&P61769 (I21-M119)&TYSPALNKMF
-
Molecular Weight
39-42 kDa and 10 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Related Products
Protein Description
The study of the HLA-A*24:02/B2M/p53 monomer (TYSPALNKMF) recombinant protein is rooted in the significant role of the immune system in cancer immunotherapy. HLA-A*24:02 is a prevalent human leukocyte antigen (HLA) class I molecule that presents tumor-associated peptides, such as those derived from the mutant p53 protein, to cytotoxic T cells, thereby eliciting an immune response. The p53 tumor suppressor gene is frequently mutated in various cancers, leading to the expression of abnormal peptides that can be recognized by the immune system. The B2M (beta-2-microglobulin) is essential for the stability and presentation of the HLA complex on the cell surface. By studying the HLA-A*24:02/B2M/p53 monomer, researchers aim to understand the mechanisms of T cell activation and the specific immune responses generated against p53-derived peptides in cancer patients. This understanding is crucial for developing targeted immunotherapies that can enhance the effectiveness of existing cancer treatments. Furthermore, the recombinant protein serves as a valuable tool for investigating the immunogenicity of p53 peptides, facilitating the design of vaccine candidates that could potentially improve patient outcomes in cancers associated with p53 mutations. Overall, this research holds promise for advancing the field of personalized cancer immunotherapy and improving therapeutic strategies against tumors driven by p53 dysregulation.
