Analytical Data
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Gene name
14 (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 reducing 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
TNFSF14, also known as TRAIL (TNF-Related Apoptosis-Inducing Ligand) or LIGHT, is a member of the tumor necrosis factor (TNF) superfamily, playing a critical role in immune regulation and apoptosis. Research into TNFSF14 has gained momentum due to its potential therapeutic applications in cancer and autoimmune diseases. This protein acts primarily through its receptors, promoting apoptosis in tumor cells and modulating the immune response by influencing T cell activation and dendritic cell function. As a dual-function cytokine, TNFSF14 simultaneously enhances anti-tumor immunity while regulating inflammation, making it a key focus for developing novel immunotherapies. Recombinant TNFSF14 has been produced for various studies to evaluate its effects in preclinical models, leading to insights on its mechanisms of action and potential efficacy. Ongoing research aims to optimize its therapeutic applications, investigate combination therapies, and understand its role in the tumor microenvironment, positioning TNFSF14 as a promising candidate in the fight against cancer. Additionally, studies are exploring its involvement in lymphoid development and tissue homeostasis, further expanding its significance in health and disease.
