Measured by its ability to induce apoptosis of TF‑1 human erythroleukemic cells. Migone, T. et al. (2002) Immunity 16:479. The ED50 for this effect is 15-75 ng/mL.
Source
E. coli-derived mouse TL1A/TNFSF15 protein Ile76-Leu252, with an N-terminal Met
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
20 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using 1896-TL/CF in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse TL1A/TNFSF15 Protein, CF
MGC129934
MGC129935
TL1A
TL1Vascular endothelial cell growth inhibitor
TNF superfamily ligand TL1A
TNFSF15
tumor necrosis factor (ligand) superfamily, member 15
tumor necrosis factor ligand superfamily member 15
vascular endothelial growth inhibitor-192A
VEGI
VEGI192A
VEGITNF ligand-related molecule 1
Background
TL1A is a type II transmembrane protein belonging to the TNF superfamily and has been designated TNF superfamily member 15 (TNFSF15). Mouse TL1A is a 252 amino acid residues (aa) protein consisting of a 35 aa N-terminal cytoplasmic domain, a 24 aa transmembrane region and 193 aa C-terminal extracellular domain (1). TL1A is expressed predominantly in endothelial cells and its expression is stimulated by TNF-a and IL-1a (1). Non-endothelial cells of the gut mucosa, including lamina propria lymphocytes and tissue macrophages, also express TL1A and at higher levels in chronic inflammatory bowel disorders (2). TL1A binds with high affinity to death receptor 3 (DR3), which is now designated TNF receptor superfamily member 25 (TNFRSF25). DR3 was formerly designated TNFRSF12 when it was thought to be the receptor for TWEAK/TNFSF12. Depending on the cell type, DR3-TL1A interactions have different effects. Ligation of DR3 on activated T cells by TL1A provides a costimulatory signal to increase IL-2 responsiveness and the secretion of proinflamatory cytokines (1). The promotion of survival of activated T cells by TL1a results from the activation of the transcription factor NF-kappa-B. In a tumor erythroleukemic cell line, TF-1, DR3-TL1A signaling increases production of the NF-kB-dependent antiapoptotic protein c-IAP2, promoting survival in these cells (3). In HUVEC cells, which express both DR3 and TL1A, ligation of DR3 by TL1A regulates cell apoptosis (4). These effects of TL1A are blocked by the secreted, soluble decoy receptor 3 (DcR3), also known as TR6 and TNFRSF6B, which compete with DR3 for binding to TL1A (1-4). Consistent with the observed in vitro activities, TL1A promotes ex vivo splenocyte expansion and enhances in vivo graft-versus-host-response. The level of TL1A in cells of gut mucosa, in patients with bowel inflammatory disorders, correlates with the severity of inflammation, and TL1A may play a role in a Th1-mediate pathological conditions such as Crohn’s disease (2). Mouse and human TL1A share 73% homology in their C-terminal domains.
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