Analytical Data
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Gene name
HLA-C*03:03&B2M Monomer
- Application
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Alternative Names
HLA-C*0303&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
QDK63961.1 (G25-I308)&P61769
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Expression Region
QDK63961.1 (G25-I308)&P61769 (I21-M119)
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Molecular Weight
42-47 kDa and 13 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-C*03:03 and beta-2-microglobulin (B2M) monomer recombinant proteins are key components in understanding the human immune response, particularly in the context of major histocompatibility complex (MHC) class I molecules. HLA-C is a crucial molecule involved in the presentation of peptide antigens to CD8+ T cells, thereby playing a significant role in cellular immunity. Variants like HLA-C*03:03 can influence susceptibility to various diseases, including autoimmune disorders and infections. B2M serves as an essential structural component of MHC class I molecules, stabilizing their structural integrity and facilitating their expression on the cell surface. The study of HLA-C*03:03 and B2M monomer proteins provides insights into their molecular interactions, peptide-binding mechanisms, and their potential role in disease association. Recent advancements in recombinant protein technology allow for the production of these proteins in sufficient quantities for detailed biochemical and structural studies, enabling researchers to explore their functions and implications in immunology, therapeutic interventions, and vaccine development. Understanding the specifics of HLA-C*03:03's peptide repertoire and its interaction with B2M could lead to discoveries that enhance the effectiveness of immunotherapies and improve personalized medicine approaches for patients with HLA-associated diseases.
