Analytical Data
-
Gene name
HLA-A*02:01&B2M&EBV LMP2(FLYALALLL) Monomer
- Application
-
Alternative Names
HLA-A*0201 & B2M & EBV LMP2 (FLYALALLL)
-
Species
Human
-
Source
HEK293
-
Tag
C-Avi;C-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
AAA59606.1 (G25-I308)&P61769
-
Expression Region
AAA59606.1 (G25-I308)&P61769 (I21-M119)&FLYALALLL
-
Molecular Weight
40-43 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 research on the HLA-A*02:01/B2M/EBV LMP2 (FLYALALLL) monomeric recombinant protein is grounded in the need to understand the immune response to Epstein-Barr Virus (EBV), which is associated with various malignancies such as lymphomas and nasopharyngeal carcinoma. Human Leukocyte Antigen (HLA) class I molecules, particularly HLA-A*02:01, play a crucial role in presenting viral peptides to cytotoxic T lymphocytes, facilitating the immune system's ability to target and destroy infected cells. The EBV LMP2 (Latent Membrane Protein 2) serves as a critical antigen for T-cell recognition, and the specific peptide FLYALALLL is known to be presented by HLA-A*02:01. By developing a monomeric recombinant protein consisting of HLA-A*02:01, beta-2-microglobulin (B2M), and the EBV LMP2 peptide, researchers aim to study the structural and functional properties of this complex. Understanding the interactions of this monomeric protein can provide insights into the mechanisms of immune recognition and evasion by EBV, potentially leading to the development of therapeutic vaccines or immunotherapies that can enhance the body’s immune response against EBV-associated diseases. This research not only contributes to the fundamental understanding of HLA-peptide interactions but also holds the promise of improving clinical outcomes for patients affected by EBV-related malignancies.
