Analytical Data
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Gene name
HLA-G&B2M&Peptide (RIIPRHLQL) Tetramer
- Application
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Alternative Names
HLA G antigen; sHLA-G; b2 microglobulin; HLA G; HLAG; HLA-G; MHC Class I Antigen G; MHC class Ib antigen; MHC-G; sHLA-G
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Species
Rhesus Macaque
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Source
HEK293
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Tag
C-Avi;C-8*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O02948 (G25-T305)&Q6V7J5
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Expression Region
O02948 (G25-T305)&Q6V7J5 (I21-M119)&RIIPRHLQL
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Molecular Weight
260-265 kDa under Non reducing (N)
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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-G is a non-classical major histocompatibility complex (MHC) class I molecule that plays a crucial role in immune tolerance, particularly during pregnancy and transplantation. Its unique properties, such as limited polymorphism and the ability to inhibit NK cell activity and modulate T cell responses, make it a significant focus of study in immunology. Beta-2-microglobulin (B2M) is an essential component of MHC class I molecules that stabilizes their structure and facilitates peptide presentation. The specific peptide RIIPRHLQL, derived from HLA-G, has been shown to bind to the HLA-G molecule, influencing immune cell interactions. The study of HLA-G in tandem with B2M and specific peptides like RIIPRHLQL aims to elucidate the molecular mechanisms underlying immune evasion in various pathological conditions, including cancers and autoimmune diseases. Creating and characterizing HLA-G/B2M/RIIPRHLQL tetramer recombinant proteins offers a method to investigate the antigen-specific T cell responses in detail, providing insights into how HLA-G may contribute to immune regulation and the development of novel therapeutic strategies. This research not only enhances our understanding of HLA-G’s role in immune modulation but also sets the foundation for potential applications in improving transplant outcomes and cancer immunotherapy.
