Other Proteins

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

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

Recombinant Human TL-1A (Legacy Tebubio ref. 167310-23). TL-1A belongs to the TNF superfamily of ligands. It is expressed predominantly in endothelial cells, and to a lesser extent in the placenta, lung, kidney, skeletal muscle, pancreas, small intestine and colon. TL-1A inhibits endothelial cell proliferation and angiogenesis, and has been shown to induce NF-kappaB activation, caspase activity, and apoptosis in responding cell lines. TL-1A interacts with TNFRSF25/DR3 receptor, but can also bind to a decoy receptor TNFRSF21/DR6. Recombinant Human TL-1A is a 22.0 kDa polypeptide of 194 amino acid residues.

Recombinant Human TL-1A (Legacy Tebubio ref. 167310-23). TL-1A belongs to the TNF superfamily of ligands. It is expressed predominantly in endothelial cells, and to a lesser extent in the placenta, lung, kidney, skeletal muscle, pancreas, small intestine and colon. TL-1A inhibits endothelial cell proliferation and angiogenesis, and has been shown to induce NF-kappaB activation, caspase activity, and apoptosis in responding cell lines. TL-1A interacts with TNFRSF25/DR3 receptor, but can also bind to a decoy receptor TNFRSF21/DR6. Recombinant Human TL-1A is a 22.0 kDa polypeptide of 194 amino acid residues.

Recombinant Human HVEM-Fc (Legacy Tebubio ref. 167310-27). HVEM belongs to the TNF Receptor superfamily of transmembrane proteins, and plays a role in the activation of T-cells and other lymphocytes. It is expressed in various cells and tissues, including spleen, thymus, lung, macrophages, and T-cells. HVEM activation induces a signaling cascade that results in the induction of transcription factors NF-kappaB and AP-1. LIGHT (TNFSF14) and TNF-beta (TNFSF1) function as the ligands for HVEM, which can also bind specifically to herpes simplex virus glycoprotein D. Soluble HVEM, which tends to form disulfide-linked heterodimeric complexes in solution, can act as a "receptor decoy" resulting in inhibition of the activity of the HVEM ligands, LIGHT and TNF-beta. Recombinant Human HVEM-Fc Chimera is a 376 amino acid fusion protein that contains an N-terminal domain corresponding to the extracellular region of HVEM, and a C-terminal domain corresponding to residues 102 to 330 of human IgG1. Th

Recombinant Human HVEM-Fc (Legacy Tebubio ref. 167310-27). HVEM belongs to the TNF Receptor superfamily of transmembrane proteins, and plays a role in the activation of T-cells and other lymphocytes. It is expressed in various cells and tissues, including spleen, thymus, lung, macrophages, and T-cells. HVEM activation induces a signaling cascade that results in the induction of transcription factors NF-kappaB and AP-1. LIGHT (TNFSF14) and TNF-beta (TNFSF1) function as the ligands for HVEM, which can also bind specifically to herpes simplex virus glycoprotein D. Soluble HVEM, which tends to form disulfide-linked heterodimeric complexes in solution, can act as a "receptor decoy" resulting in inhibition of the activity of the HVEM ligands, LIGHT and TNF-beta. Recombinant Human HVEM-Fc Chimera is a 376 amino acid fusion protein that contains an N-terminal domain corresponding to the extracellular region of HVEM, and a C-terminal domain corresponding to residues 102 to 330 of human IgG1. Th

Recombinant Human sOX40 Ligand (Legacy Tebubio ref. 167310-28). OX40L, a member of the TNF superfamily of structurally related proteins, exists primarily as a type II membrane bound, non-covalently linked homotrimeric protein. It is expressed on antigen presenting cells (APCs), such as dendritic cells and activated B cells, and also on various other cells such as vascular endothelial cells, mast cells, and natural killer cells. OX40L signals specifically through the OX40 receptor, which is expressed predominantly on CD4+T cells but also on certain activated CD8+T cells. OX40/OX40L functions as a costimulatory signal, which is required for a productive interaction between antigen presenting cells and their target T cells. It enhances cell proliferation and survival, and increases expression of RANTES, IL-2, IL-3, and IFNgamma. OX40/OX40L signaling plays an important role in immuno-regulatory communication, enabling the immune system to distinguish between "friend vs. foe" during activat

Recombinant Human sOX40 Ligand (Legacy Tebubio ref. 167310-28). OX40L, a member of the TNF superfamily of structurally related proteins, exists primarily as a type II membrane bound, non-covalently linked homotrimeric protein. It is expressed on antigen presenting cells (APCs), such as dendritic cells and activated B cells, and also on various other cells such as vascular endothelial cells, mast cells, and natural killer cells. OX40L signals specifically through the OX40 receptor, which is expressed predominantly on CD4+T cells but also on certain activated CD8+T cells. OX40/OX40L functions as a costimulatory signal, which is required for a productive interaction between antigen presenting cells and their target T cells. It enhances cell proliferation and survival, and increases expression of RANTES, IL-2, IL-3, and IFNgamma. OX40/OX40L signaling plays an important role in immuno-regulatory communication, enabling the immune system to distinguish between "friend vs. foe" during activat

Recombinant Human sCD100 (Legacy Tebubio ref. 167310-29). The Semphorins are a large family of phylogenetically conserved proteins that play a pivotal role in maintaining homeostasis in the immune system. Twenty members of this family have been identified and categorized into eight subclasses based on sequence similarity and distinctive structural features. CD100, also known as Sema4D, is a 150 kDa transmembrane class IV semaphorin. Studies have shown that CD100 can induce monocyte migration, T cell activation, and B cell survival, as well as T/B cell and T/DC "cooperation". The CD100 precursor contains 862 amino acids, including a 21 amino acids signal sequence, a 713 amino acids extracellular domain, a 21 amino acids transmembrane sequence, and a 107 amino acids cytoplasmic region. The extracellular sequence contains several structural features, including a 479 amino acids "sema" domain, a 79 amino acids Ig-like sequence, and a 52 amino acids "Plexin-type repeat". Recombinant Human s