Analytical Data
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Gene name
Peptide Ready HLA-E*01:03&B2M Monomer
- Application
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Alternative Names
MHC; HLA-E*01:03; Peptide Ready
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Species
Human
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Source
HEK293
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Tag
C-8*His;C-Avi
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P13747 (G25-I305)&P61769
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Expression Region
P13747 (G25-I305)&P61769 (I21-M119)&RIIPRHLQL
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Molecular Weight
50-60 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 research on Peptide Ready HLA-E*01:03&B2M monomer recombinant protein is essential for understanding immune responses and potential therapeutic applications. HLA-E is a non-classical Major Histocompatibility Complex (MHC) class I molecule that plays a crucial role in the immune system by presenting peptides to natural killer (NK) cells and certain T cells. Its primary function is to regulate immune responses, particularly in the context of viral infections and tumor recognition. The HLA-E*01:03 variant has gained interest due to its distinct peptide binding characteristics and its association with immunity in various diseases. The coupling of HLA-E with Beta-2-Microglobulin (B2M) is vital for its stability and proper surface expression. Generating a recombinant form of HLA-E*01:03&B2M allows researchers to explore its structure and function in detail, paving the way for potential applications in immunotherapy, vaccine development, and understanding the mechanisms of immune evasion by pathogens and tumors. This research is particularly relevant in the context of developing novel strategies for combating viral infections and cancer, where the modulation of NK cell activity could significantly enhance therapeutic efficacy. Insights gained from studying this recombinant protein could lead to improved diagnostic and therapeutic tools in precision medicine.











