Analytical Data
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Gene name
HLA-B*27:05&B2M Monomer
- Application
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Alternative Names
HLA-B*2705 & 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
ACR83851.1 (G25-V309)&P61769
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Expression Region
ACR83851.1 (G25-V309)&P61769 (I21-M119)
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Molecular Weight
48-53 kDa and 17 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
The research into the recombinant protein HLA-B*27:05 and beta-2-microglobulin (B2M) monomer primarily stems from its critical role in understanding autoimmune diseases, particularly ankylosing spondylitis (AS). HLA-B27 is a major histocompatibility complex (MHC) class I molecule that is strongly associated with AS, a chronic inflammatory condition that primarily affects the spine and sacroiliac joints. The structure and function of HLA-B*27:05, in conjunction with B2M, are essential for presenting antigens to T cells, thus triggering immune response. However, the presence of the HLA-B27 allele is not solely responsible for AS; it is believed that certain conformational and molecular characteristics of the HLA-B27 molecule may predispose individuals to autoimmune pathology. The creation of HLA-B*27:05 and B2M monomer as a recombinant protein allows for detailed structural and functional studies, facilitating the exploration of its epitopes and interaction with T cell receptors. Furthermore, understanding the molecular basis of how HLA-B*27:05 contributes to disease mechanisms may uncover new therapeutic targets and diagnostics for AS and related conditions, making this research pivotal for advancing both basic immunology and clinical outcomes in patients with HLA-B27-related disorders.
