Analytical Data
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Gene name
TL1A/TNFSF15 Trimer
- Application
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Alternative Names
TNFSF15; TL1; VEGI; VEGI192A; Tumor Necrosis Factor(ligand)Superfamily,Member 15; TNF Superfamily Ligand TL1A; TNF Ligand-Related Molecule 1; Vascular Endothelial Growth Inhibitor
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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 97% as determined by reducing SDS-PAGE.
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Uniprot
O95150
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Expression Region
Val67~Leu251
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Molecular Weight
25kDa
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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
TL1A, also known as TNFSF15, is a member of the tumor necrosis factor (TNF) superfamily that plays a critical role in immune regulation and inflammatory responses. This protein is primarily expressed in the vascular endothelium and local immune cells, and it is known to interact with its receptor, DLK1, to influence T cell activation and proliferation. Research has increasingly focused on TL1A due to its involvement in various autoimmune and inflammatory diseases, such as Crohn’s disease and ulcerative colitis, where it is linked to the pathogenesis and progression of these conditions. The study of TL1A/TNFSF15 trimeric recombinant proteins has gained significance, as understanding their structure and function can provide insights into the mechanisms of immune regulation. Moreover, the potential therapeutic applications of targeting TL1A in disease settings represent a promising avenue for intervention. By producing and characterizing TL1A trimers, researchers aim to dissect its molecular interactions and elucidate its role in modulating the immune response, thereby paving the way for novel treatment strategies that could alleviate the burden of inflammatory diseases. Additionally, the development of TL1A-based biomolecules could facilitate the design of biomarkers or therapeutic agents aimed at tuning immune responses in various pathological contexts.
