Analytical Data
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Gene name
HLA-A*02:06&B2M Monomer
- Application
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Alternative Names
HLA-A*0206 & B2M
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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
AAW30168.1 (G25-T305)&P61769
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Expression Region
AAW30168.1 (G25-T305)&P61769 (I21-M119)
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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 HLA-A*02:06 and β2-microglobulin (B2M) monomer recombinant protein represents a significant focus in immunological research due to its role in antigen presentation and immune response. Human leukocyte antigen (HLA) molecules are vital for the recognition of foreign peptides by T cells, and HLA-A*02:06 is one of the most prevalent class I alleles in the population, associated with various diseases, including autoimmunity and cancer. The binding of peptides to HLA molecules is critical for the activation of cytotoxic T lymphocytes, which can target and destroy infected or malignant cells. The importance of B2M lies in its stabilization of the HLA-A molecule on the cell surface, allowing for effective immunological functions. Studying the HLA-A*02:06/B2M complex can provide insights into the mechanisms of T cell activation, the design of T cell-based therapies, and the development of vaccines. Through recombinant technology, researchers can produce this monomeric protein in a controlled environment, enabling detailed structural and functional analyses. Understanding the interactions between HLA-A*02:06 and its peptide ligands, as well as its role in immune evasion by tumors, could pave the way for novel therapeutic strategies aimed at enhancing anti-tumor immunity and improving clinical outcomes in cancer treatment. Furthermore, the availability of this recombinant protein contributes to the development of assays for peptide-HLA binding studies, facilitating advancements in personalized medicine and immunotherapy. Overall, the research surrounding HLA-A*02:06 and B2M monomer recombinant proteins is crucial in the broader context of immune system modulation and therapeutic interventions.
