Analytical Data
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Gene name
LIGHT/TNFSF14
- Application
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Alternative Names
CD258; TR2; HVEML; LIGHT; LTg; Herpes virus entry mediator ligand; Herpesvirus entry mediator ligand
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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 90% as determined by SDS-PAGE.
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Uniprot
O43557
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Expression Region
His62~Val240
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Molecular Weight
27kDa
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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
LIGHT (Lymphotoxin-like inducible protein that competes with glycoprotein D for herpesvirus entry mediator) is a member of the tumor necrosis factor (TNF) superfamily, specifically encoded by the TNFSF14 gene. This protein plays a critical role in immune regulation, influencing the activation and proliferation of T cells, dendritic cells, and other immune cells through its interaction with receptors such as HVEM (herpesvirus entry mediator) and TR2. Research has highlighted its dual function in promoting immune responses during viral infections and contributing to autoimmune diseases, making it a pivotal target for therapeutic intervention. LIGHT's ability to act as a pro-inflammatory cytokine has led to its investigation in various contexts, such as tumor immunology, where it may enhance anti-tumor immunity, as well as in chronic inflammatory diseases. The recombination and study of LIGHT/TNFSF14 protein facilitate the understanding of its biological functions and the molecular mechanisms underlying its interactions with receptors. Moreover, engineered recombinant LIGHT proteins can be utilized to develop novel therapeutic strategies aimed at modulating immune responses, with potential applications in cancer therapy, vaccine development, and the treatment of autoimmune disorders. Thus, continued exploration of LIGHT's role in the immune system holds promise for innovative approaches in immunotherapy and disease management.
