Analytical Data
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Gene name
HLA-A*33:03&B2M Monomer
- Application
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Alternative Names
HLA-A*3303 & 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
AAA79865.1 (G25-T305)&P61769
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Expression Region
AAA79865.1 (G25-T305)&P61769 (I21-M119)
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Molecular Weight
43-48 kDa and 16 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
HLA-A*33:03 and beta-2-microglobulin (B2M) form a crucial component of the major histocompatibility complex (MHC) class I molecules, which play a key role in the immune response by presenting endogenous peptides to CD8+ T cells. The HLA-A*33:03 allele is of particular interest due to its association with various diseases and its role in organ transplantation and autoimmune disorders. Understanding the structural and functional properties of the HLA-A*33:03/B2M monomer is vital for elucidating its mechanism in immune recognition and for developing immunotherapies. Recombinant proteins of HLA-A*33:03 in complex with B2M allow researchers to investigate the peptide binding characteristics, enhance the understanding of T cell recognition, and facilitate the development of vaccines and therapeutics targeting specific diseases. Furthermore, studying this complex can inform the development of predictive models for transplant compatibility and graft rejection, ultimately improving patient outcomes in transplantation settings. The generation of this monomeric form also provides a platform for high-throughput screening of potential therapeutic peptides and can aid in the design of T cell-based immunotherapies. As such, the research on HLA-A*33:03/B2M recombined proteins not only contributes to fundamental immunological knowledge but also has important implications for translational medicine.
