Analytical Data
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Gene name
HLA-A*03:01&B2M Monomer
- Application
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Alternative Names
HLA-A*0301 & 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
NP_002107.3 (G25-T305)&P61769
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Expression Region
NP_002107.3 (G25-T305)&P61769 (I21-M119)
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Molecular Weight
40-45 kDa and 12 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 HLA-A*03:01 and beta-2-microglobulin (B2M) monomeric recombinant proteins is essential for understanding the immune system's role in health and disease. HLA-A*03:01 is a highly prevalent class I major histocompatibility complex (MHC) molecule, responsible for presenting endogenous peptides to CD8+ T cells, which plays a crucial role in the adaptive immune response. Abnormal expression or function of this MHC molecule has been linked to various autoimmune diseases and transplant rejections. B2M is a critical component of MHC class I proteins and is essential for their stability and surface expression. The investigation of the HLA-A*03:01-B2M complex is particularly relevant for vaccine design and therapeutic strategies, as it can lead to the identification of novel epitopes for T cell recognition. Moreover, understanding the structural and functional characteristics of HLA-A*03:01 in the context of B2M may provide insights into the mechanisms of immune evasion by pathogens and tumors. Recent advances in recombinant DNA technology allow for the production and purification of these proteins, facilitating detailed biophysical and functional assays. Such studies can ultimately enhance our knowledge of immune responses and contribute to the development of personalized medicine approaches in treating diseases associated with HLA-A*03:01.
