Animal-Free TL1A/TNFSF15 Protein, Human (His)

The TL1A protein (VEGI protein), belongs to the tumor necrosis factor (TNF) family and is a receptor for TNFRSF25 and TNFRSF6B. TL1A is involved in the activation of NF-κB and C-Jun pathways, which can be used as a regulator of mucosal immunity and participate in the immune pathway of inflammatory bowel disease (IBD) pathogenesis^[1][2]. TL1A originates from endothelial cells and inhibits the proliferation of breast cancer, epithelial and myeloid tumor cells^[3]. The human TL1A protein has a transmembrane domain (36-56 a.a.) that can be cleaved into membrane-type and soluble peptide fragments. Animal-Free TL1A/TNFSF15 Protein, Human (His) is the extracullar part of TL1A protein (Q58-L251), produced in E.coli with C-terminal His-tag.

TL1A (Tumor necrosis factor-like cytokine 1A), also known as TNF ligand-related molecule 1 and vascular endothelial cell growth inhibitor (VEGI), is the receptor for TNFRSF25 and TNFRSF6B, acts as a regulator of mucosal immunity and participates in immunological pathways involved in the inflammatory bowel diseases (IBD) pathogenesis^[1]. TL1A belongs to the tumor necrosis factor family, derived from endothelial cell. It is a ligand for DR3 and decoy receptor TR6/DcR3, the interaction with DR3 promotes T cell expansion during an immune response, whereas TR6 has an opposing effect. Moreover, DR3 is the death domain-containing receptor, that is upregulated during T cell activation. TL1A shows an inducible expression by TNF and IL-1alpha, and induces NF-kappaB activation and apoptosis in DR3-expressing cell lines. Meanwhile, TL1A acts as a costimulator that increases IL-2 responsiveness and secretion of proinflammatory cytokines^[2]. In addition, TL1A activates c-Jun N-terminal kinase. TL1A also activates caspase-3 leading to PARP cleavage, and inhibits the proliferation of breast carcinoma, epithelial, and myeloid tumor cells. TL1A promotes proliferation of normal human fibroblast cells. These results suggest that VEGI, a new member of the TNF family, has a signaling pathway similar to TNF and is most likely a multifunctional cytokine^[3]. Human TL1A protein has two glycosylated domains and one transmembrane domain (36-56 a.a.), and can be cleaved into membrane-type peptide fragments and soluble peptide fragments. The protein sequence of human is much different from mouse and rat with similarities of 68.42% and 70.45%, respectively.

TL1A (1 ng/mL; 15 min) interacts with TR6-Fc, results in NF-κB activation^[2].
TL1A (72-251 a.a.; 1 ng/mL; 72 h) increases IL-2 responsiveness and induces cytokine release in anti-CD3- and anti-CD28-treated T cells^[2].
TL1A (1 μg/mL; 12-24 h) induces IκB degradation in U-937 cells^[3].

TL1A (human, 72-251 a.a.; 3 mg/kg; i.v.; daily for 5 d) enhances in vivo and ex vivo splenic alloactivation in C57BL/6 mice^[2].

Measure by its ability to induce TF-1 cells proliferation. The ED₅₀ for this effect is < 0.2 ng/mL.

Human

E. coli

C-His

O95150 (Q58-L251)

9966  [NCBI]

MQLRAQGEACVQFQALKGQEFAPSHQQVYAPLRADGDKPRAHLTVVRQTPTQHFKNQFPALHWEHELGLAFTKNRMNYTNKFLLIPESGDYFIYSQVTFRGMTSECSEIRQAGRPNKPDSITVVITKVTDSYPEPTQLLMGTKSVCEVGSNWFQPIYLGAMFSLQEGDKLMVNVSDISLVDYTKEDKTFFGAFLL

Approximately 22.95 kDa

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a solution containing 1X PBS, pH 8.0.

<0.1 EU per 1 μg of the protein by the LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Furfaro F, et al. TL1A: A New Potential Target in the Treatment of Inflammatory Bowel Disease. Curr Drug Targets. 2021;22(7):760-769.  [Content Brief]

  [2]. Migone TS, et al. TL1A is a TNF-like ligand for DR3 and TR6/DcR3 and functions as a T cell costimulator. Immunity. 2002 Mar;16(3):479-92.  [Content Brief]

  [3]. Haridas V, et al. VEGI, a new member of the TNF family activates nuclear factor-kappa B and c-Jun N-terminal kinase and modulates cell growth. Oncogene. 1999 Nov 11;18(47):6496-504.  [Content Brief]