Analytical Data
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Gene name
HLA-E*01:03&B2M Monomer
- Application
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Alternative Names
HLA-E*0103 & 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
P13747 (G22-I305)&P61769
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Expression Region
P13747 (G22-I305)&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
Related Products
Protein Description
HLA-E*01:03 is a variant of the HLA-E gene, which encodes a non-classical major histocompatibility complex (MHC) class I molecule that plays a crucial role in the immune response by presenting signals to immune cells, particularly natural killer (NK) cells. It is known for its ability to bind and present specific peptide sequences, often derived from the leader peptides of other MHC class I molecules, thereby influencing NK cell activity and tolerance. Understanding the structure and function of HLA-E*01:03, especially in the context of its interaction with β2-microglobulin (B2M), is vital for elucidating its role in immune regulation, transplantation, and autoimmune diseases. Recombinant protein studies of the HLA-E*01:03 & B2M monomer allow for the investigation of its structural features, binding affinity, and the nuances of its interaction with various peptides, providing insights into its potential applications in immunotherapy and vaccine development. This research aims to deepen our understanding of how HLA-E contributes to immune evasion in tumors and its implications for designing targeted therapies leveraging this unique MHC molecule.
