Analytical Data
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Gene name
HLA-G&B2M&Peptide (RIIPRHLQL) Monomer
- 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
Cynomolgus
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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
E0WKX9 (G25-T305)&Q8SPW0
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Expression Region
E0WKX9 (G25-T305)&Q8SPW0 (I21-M119)&RIIPRHLQL
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Molecular Weight
55-65 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-G is a non-classical major histocompatibility complex (MHC) Class I molecule that plays a crucial role in the immune system, particularly in the context of pregnancy and tumor immune evasion. Its unique ability to inhibit both natural killer (NK) cells and T-cell responses makes it a subject of intense research for therapeutic applications, including organ transplantation and cancer immunotherapy. B2M (Beta-2-microglobulin) is an essential component of MHC Class I molecules, stabilizing their structure and facilitating peptide presentation. The specific peptide RIIPRHLQL, derived from the human cytomegalovirus, serves as a model to explore the interactions between HLA-G, B2M, and the peptide, aiming to understand how these components contribute to immune modulation. The development of recombinant monomeric proteins of HLA-G, B2M, and RIIPRHLQL enables in-depth biophysical and structural studies, which are crucial for deciphering their molecular interactions and functions. These studies provide insights into potential therapeutic strategies to manipulate immune responses in various clinical settings, offering promise for enhancing transplant acceptance and improving cancer immunotherapy outcomes.
