Analytical Data
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Gene name
PE-Labeled HLA-G&B2M&Peptide (RIIPRHLQL) Tetramer
- Application
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Alternative Names
HLA-G; MHC-G; HLAG; Leukocyte Antigen G; b2 microglobulin; HLA class I histocompatibility antigen, alpha chain G
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P17693
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Expression Region
Met29~His117
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Molecular Weight
14kDa
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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 PE-labeled HLA-G/B2M/Peptide (RIIPRHLQL) tetramer is a recombinant protein designed for research into immune responses and its implications in various diseases, particularly those involving immune tolerance, such as cancer and pregnancy. HLA-G is an atypical major histocompatibility complex (MHC) class I molecule known for its role in modulating the immune system by inhibiting natural killer (NK) cell activity and promoting immune tolerance in the maternal-fetal relationship. The combination of HLA-G with β2-microglobulin (B2M) ensures proper folding and stability of the protein, facilitating its use in tetramer assays. The inclusion of the specific peptide RIIPRHLQL enhances the binding affinity of the tetramer to T cells that express T cell receptors (TCRs) specific to the HLA-G/peptide complex. This tetramer allows for the direct visualization and quantification of T cells engaged in immune responses tailored to HLA-G, potentially unveiling the intricate dynamics of immune evasion in tumors and the mechanisms behind successful pregnancy maintenance. Utilizing this PE-labeled tetramer will enable researchers to isolate and characterize HLA-G-specific T cells, advancing the understanding of their role in immune regulation and providing insights for therapeutic interventions targeting immune tolerance in various clinical settings.
