Other Proteins

Recombinant Human TACI (Legacy Tebubio ref. 167310-17). TACI, a member of the TNF Receptor superfamily, is expressed in the small intestine, spleen, thymus, peripheral blood leukocytes, activated T cells, and resting B cells. TACI can bind to both APRIL and BAFF, stimulate the activation of transcription factors NF-kappaB and AP-1, and can mediate the calcineurin-dependent activation of NF-AT (nuclear-factor of activated T cells). TACI also plays a key role in the stimulation of B and T cell function. Soluble TACI inhibits APRIL-stimulated proliferation of primary B cells by blocking the binding of APRIL to the membrane-anchored TACI receptor. Recombinant Human TACI is a soluble 159 amino acid polypeptide (17.8 kDa) comprising the TNFR homologous, cysteine-rich extracellular domain of the TACI protein.

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.