Other Proteins

Recombinant Human sTRAIL Receptor-1 (Legacy Tebubio ref. 167310-18). TRAIL Receptor-1/DR4 and TRAIL Receptor-2/DR5 belong to the TNFR superfamily of transmembrane proteins, and contain a cytoplasmic "death domain," which can activate the cell's apoptotic machinery. These receptors are activated by binding to either membrane-anchored or soluble TRAIL/Apo2L. The DR4 and DR5 receptors are both produced as type I transmembrane proteins, which contain an extracellular domain, a transmembrane domain, and a cytoplasmic domain. The recombinant soluble forms of DR4 and DR5 consist of the TNFR-homologous, cysteine-rich portion of their respective extracellular domains. Recombinant Human soluble TRAIL Receptor-1/DR4 is a 22.7 kDa protein (215 amino acid residues) consisting of the TNFR homologous, cysteine-rich portion of the extracellular domain.

Recombinant Human sTRAIL Receptor-1 (Legacy Tebubio ref. 167310-18). TRAIL Receptor-1/DR4 and TRAIL Receptor-2/DR5 belong to the TNFR superfamily of transmembrane proteins, and contain a cytoplasmic "death domain," which can activate the cell's apoptotic machinery. These receptors are activated by binding to either membrane-anchored or soluble TRAIL/Apo2L. The DR4 and DR5 receptors are both produced as type I transmembrane proteins, which contain an extracellular domain, a transmembrane domain, and a cytoplasmic domain. The recombinant soluble forms of DR4 and DR5 consist of the TNFR-homologous, cysteine-rich portion of their respective extracellular domains. Recombinant Human soluble TRAIL Receptor-1/DR4 is a 22.7 kDa protein (215 amino acid residues) consisting of the TNFR homologous, cysteine-rich portion of the extracellular domain.

Recombinant Human sTRAIL Receptor-2 (Legacy Tebubio ref. 167310-19). TRAIL Receptor-1/DR4 and TRAIL Receptor-2/DR5 belong to the TNFR superfamily of transmembrane proteins, and contain a cytoplasmic "death domain," which can activate the cell's apoptotic machinery. These receptors are activated by binding to either membrane-anchored or soluble TRAIL/Apo2L. The DR4 and DR5 receptors are both produced as type I transmembrane proteins, which contain an extracellular domain, a transmembrane domain, and a cytoplasmic domain. The recombinant soluble forms of DR4 and DR5 consist of the TNFR-homologous, cysteine-rich portion of their respective extracellular domains. Recombinant Human soluble TRAIL Receptor-2/DR5 is a 14.9 kDa protein (133 amino acid residues) consisting of the TNFR-homologous, cysteine-rich portion of the extracellular domain.

Recombinant Human sTRAIL Receptor-2 (Legacy Tebubio ref. 167310-19). TRAIL Receptor-1/DR4 and TRAIL Receptor-2/DR5 belong to the TNFR superfamily of transmembrane proteins, and contain a cytoplasmic "death domain," which can activate the cell's apoptotic machinery. These receptors are activated by binding to either membrane-anchored or soluble TRAIL/Apo2L. The DR4 and DR5 receptors are both produced as type I transmembrane proteins, which contain an extracellular domain, a transmembrane domain, and a cytoplasmic domain. The recombinant soluble forms of DR4 and DR5 consist of the TNFR-homologous, cysteine-rich portion of their respective extracellular domains. Recombinant Human soluble TRAIL Receptor-2/DR5 is a 14.9 kDa protein (133 amino acid residues) consisting of the TNFR-homologous, cysteine-rich portion of the extracellular domain.

Recombinant Human TWEAK Receptor (Legacy Tebubio ref. 167310-21). TWEAKR belongs to the TNF family of transmembrane proteins, and contains a cytoplasmic "death domain", which can activate a cell's apoptotic machinery. It is expressed in the spleen, thymus, peripheral blood lymphocytes, colon, and small intestine. Signal transduction by TWEAKR can be activated by either membrane-anchored or soluble TWEAK. Recombinant Human soluble TWEAKR is a 53 amino acid polypeptide (5.6 kDa) comprising the entire extracellular domain of the full-length TWEAKR protein.

Recombinant Human TWEAK Receptor (Legacy Tebubio ref. 167310-21). TWEAKR belongs to the TNF family of transmembrane proteins, and contains a cytoplasmic "death domain", which can activate a cell's apoptotic machinery. It is expressed in the spleen, thymus, peripheral blood lymphocytes, colon, and small intestine. Signal transduction by TWEAKR can be activated by either membrane-anchored or soluble TWEAK. Recombinant Human soluble TWEAKR is a 53 amino acid polypeptide (5.6 kDa) comprising the entire extracellular domain of the full-length TWEAKR protein.

Recombinant Human AITRL (Legacy Tebubio ref. 167310-22). AITRL, a member of the TNF superfamily, is expressed in endothelial cells, and signals through the AITR receptor. AITRL regulates T cell proliferation and survival, and effectuates the interaction between T lymphocytes and endothelial cells. The AITRL gene codes for a type II transmembrane protein comprised of 177 amino acids, including a 28 amino acid cytoplasmic region, a 21 amino acid transmembrane domain and a 128 amino acid extracellular domain. Recombinant Human soluble AITRL is a 14.4 kDa protein, containing 127 amino acid residues corresponding to the extracellular domain of AITRL.

Recombinant Human AITRL (Legacy Tebubio ref. 167310-22). AITRL, a member of the TNF superfamily, is expressed in endothelial cells, and signals through the AITR receptor. AITRL regulates T cell proliferation and survival, and effectuates the interaction between T lymphocytes and endothelial cells. The AITRL gene codes for a type II transmembrane protein comprised of 177 amino acids, including a 28 amino acid cytoplasmic region, a 21 amino acid transmembrane domain and a 128 amino acid extracellular domain. Recombinant Human soluble AITRL is a 14.4 kDa protein, containing 127 amino acid residues corresponding to the extracellular domain of AITRL.

Recombinant Human GITR/TNFRSF18 Fc (Legacy Tebubio ref. 167310-22R). GITR, also known as tumor necrosis factor receptor superfamily 18 (TNFRSF18), is a member of the receptor family bearing the same name that is expressed on the surfaces of cells involved in both adaptive and innate immunity, including CD4+ T cells, CD8+ T cells, natural killer cells, B cells, macrophages, and dendritic cells. Like all other TNFRSF members, GITR regulates the duration, phenotype, and degree by which the immune system responds to antigens. The National Cancer Institute regards GITR as the 12th most important molecule involved in immunotherapy, as it plays a major role in modulating both inflammatory and immune responses. The receptor has attracted the attention of immunologists for its potential as a costimulatory immune checkpoint molecule in immunotherapy. Expressed in peripheral tissues as well as endothelial cells, GITR inhibits T cell receptor-induced apoptosis via its cross-linking mechanism, ther