Analytical Data
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Gene name
HLA-A*24:02&B2M Monomer
- Application
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Alternative Names
HLA-A*2402 & 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
AAA59600.1 (G25-T305)&P61769
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Expression Region
AAA59600.1 (G25-T305)&P61769 (I21-M119)
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Molecular Weight
36-41 kDa and 14 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*24:02 and beta-2 microglobulin (B2M) monomeric recombinant protein is crucial for understanding immune responses in the context of various diseases, particularly in the field of immunotherapy and vaccine development. HLA-A*24:02 is one of the most prevalent human leukocyte antigens in certain Asian populations and plays a significant role in presenting peptides to CD8+ T cells, thus influencing the body's immune response to tumors and viral infections. The beta-2 microglobulin is an essential component of the major histocompatibility complex (MHC) class I molecule, contributing to its stability and function. Research involving the recombinant expression of HLA-A*24:02 in combination with B2M facilitates the study of this complex's structure and function, enabling the elucidation of its interactions with specific peptides and T cell receptors. Understanding these molecular dynamics is pertinent for identifying potential therapeutic targets and designing personalized medicine approaches for patients with HLA-A*24:02, as it may help in developing effective cancer vaccines or immunotherapies. Furthermore, the production of monomeric forms of HLA-A*24:02 and B2M allows for in-depth biochemical analyses and high-resolution structural studies, which are essential for advancing our knowledge of immune evasion mechanisms employed by pathogens and tumors. Thus, the exploration of HLA-A*24:02 and B2M monomer recombinant proteins represents a significant avenue for immunological research, with potential implications for enhancing clinical outcomes in various diseases linked to immune dysfunction.
