Other Proteins

Recombinant Human sCD40 Ligand (Legacy Tebubio ref. 167310-02). CD40, a member of the TNF receptor family, is a cell surface protein expressed on B cells, dendritic cells, monocytes, thymic epithelial cells and, at low levels, on T cells. Signaling though CD40 plays an important role in the proliferation and differentiation of B cells, and is critical for immunoglobulin (Ig) class switching. The membrane-anchored CD40 Ligand is expressed almost exclusively on activated CD4+ T lymphocytes. Failure to express CD40L leads to "immunodeficiency with hyper-IgM", a disease characterized by failure to produce IgG, IgA and IgE. The human CD40L gene codes for a 261 amino acid type II transmembrane protein, which contains a 22 amino acid cytoplasmic domain, a 24 amino acid transmembrane domain, and a 215 amino acid extracellular domain. The soluble form of CD40L is an 18 kDa protein comprising the entire TNF homologous region of CD40L and is generated in vivo by an intracellular proteolytic proce

Recombinant Human sTRAIL/Apo2L (Legacy Tebubio ref. 167310-04). TRAIL/Apo2L is a cytotoxic protein, which activates rapid apoptosis in tumor cells, but not in normal cells. TRAIL-induced apoptosis is achieved through binding to two death-signaling receptors, DR4 and DR5. These receptors belong to the TNFR superfamily of transmembrane proteins, and contain a cytoplasmic "death domain", which activates the cell's apoptotic machinery. The full length human TRAIL/Apo2L is a 281 amino acid protein, consisting of a 17 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 243 amino acid extracellular domain. Recombinant Human soluble TRAIL/Apo2L is a 168 amino acid polypeptide (19.6 kDa), consisting of the TNF-homologous portion of the extracellular domain of the full length TRAIL/Apo2L protein.

Recombinant Human sTRAIL/Apo2L (Legacy Tebubio ref. 167310-04). TRAIL/Apo2L is a cytotoxic protein, which activates rapid apoptosis in tumor cells, but not in normal cells. TRAIL-induced apoptosis is achieved through binding to two death-signaling receptors, DR4 and DR5. These receptors belong to the TNFR superfamily of transmembrane proteins, and contain a cytoplasmic "death domain", which activates the cell's apoptotic machinery. The full length human TRAIL/Apo2L is a 281 amino acid protein, consisting of a 17 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 243 amino acid extracellular domain. Recombinant Human soluble TRAIL/Apo2L is a 168 amino acid polypeptide (19.6 kDa), consisting of the TNF-homologous portion of the extracellular domain of the full length TRAIL/Apo2L protein.

Recombinant Human CTLA-4 Fc (Legacy Tebubio ref. 167310-05). CTLA-4 and CD28 are receptors of the immunoglobulin superfamily that are expressed, along with the transmembrane glycoproteins B7-1 and B7-2, by antigen-presenting cells, and with these ligands constitute crucial co-stimulatory pathways for T and B cell regulatory responses. It is through engagement with CD28 and CTLA-4 that the B7 family ligands B7-1 and B7-2 play principal roles in immunity by activating immune response and maintaining immune tolerance. Co-stimulatory signals generated by B7-1 and B7-2 interactions with CD28 serve to stimulate T cell activation and prevent anergy through the amplification of T cell receptor (TCR) signaling. In contrast, interactions of the ligands with CTLA-4 serves to maintain T cell homeostasis and self-tolerance through the disruption of stimulatory signaling from B7 isoform-bound CD28 complexes, and by inducing powerful inhibitory signals in T cells. CTLA-4, like B7-1, is only poorly ex

Recombinant Human CTLA-4 Fc (Legacy Tebubio ref. 167310-05). CTLA-4 and CD28 are receptors of the immunoglobulin superfamily that are expressed, along with the transmembrane glycoproteins B7-1 and B7-2, by antigen-presenting cells, and with these ligands constitute crucial co-stimulatory pathways for T and B cell regulatory responses. It is through engagement with CD28 and CTLA-4 that the B7 family ligands B7-1 and B7-2 play principal roles in immunity by activating immune response and maintaining immune tolerance. Co-stimulatory signals generated by B7-1 and B7-2 interactions with CD28 serve to stimulate T cell activation and prevent anergy through the amplification of T cell receptor (TCR) signaling. In contrast, interactions of the ligands with CTLA-4 serves to maintain T cell homeostasis and self-tolerance through the disruption of stimulatory signaling from B7 isoform-bound CD28 complexes, and by inducing powerful inhibitory signals in T cells. CTLA-4, like B7-1, is only poorly ex

Recombinant Human sTNF Receptor Type I (Legacy Tebubio ref. 167310-07). TNFRI belongs to the TNFR superfamily of transmembrane proteins, and is expressed in most cell types. Binding of either TNF-alpha or TNF-beta to TNFRI initiates a signal transduction pathway that results in the activation of the transduction factor NF-kappaB, whose target genes are involved in the regulation of inflammatory responses, and, in certain cells induce apoptosis. Soluble TNF Receptor I (sTNFRI) is capable of inhibiting TNF-alpha and TNF-beta activities by acting as a decoy receptor that serves as a sink for the TNF ligands. The human TNFRI gene encodes for a 455 amino acid type I transmembrane protein, which contains a 21 amino acid signal sequence, a 190 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 221 amino acid cytoplasmic domain. Recombinant Human sTNF Receptor Type I is an 18.3 kDa protein (162 amino acid residues) comprising the cysteine-rich, ligand-binding portion

Recombinant Human sTNF Receptor Type I (Legacy Tebubio ref. 167310-07). TNFRI belongs to the TNFR superfamily of transmembrane proteins, and is expressed in most cell types. Binding of either TNF-alpha or TNF-beta to TNFRI initiates a signal transduction pathway that results in the activation of the transduction factor NF-kappaB, whose target genes are involved in the regulation of inflammatory responses, and, in certain cells induce apoptosis. Soluble TNF Receptor I (sTNFRI) is capable of inhibiting TNF-alpha and TNF-beta activities by acting as a decoy receptor that serves as a sink for the TNF ligands. The human TNFRI gene encodes for a 455 amino acid type I transmembrane protein, which contains a 21 amino acid signal sequence, a 190 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 221 amino acid cytoplasmic domain. Recombinant Human sTNF Receptor Type I is an 18.3 kDa protein (162 amino acid residues) comprising the cysteine-rich, ligand-binding portion

Recombinant Human sRANK Receptor (Legacy Tebubio ref. 167310-08). RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic cell-membrane protein, which, by interacting with RANKL, augments the ability of dendritic. These dendritic cells then stimulate naive T-cell proliferation, and promote the survival of RANK + T-cells. RANK is also expressed in a variety of tissues, including skeletal muscle, thymus, liver, colon, small intestine, and adrenal gland. The RANK/RANKL interaction is important in the regulation of osteoclastogenesis, and in dendritic cell-mediated T-cell immune responses. Impairments in RANK signaling have been implicated in the induction of expansile osteolysis and Paget's disease of bone (PDB2). Recombinant Human sRANK Receptor is a 19.3 kDa polypeptide containing the TNFR-homologous, cysteine-rich portion of t

Recombinant Human sRANK Receptor (Legacy Tebubio ref. 167310-08). RANKL and RANK are members of the TNF superfamily of ligands and receptors that play an important role in the regulation of specific immunity and bone turnover. RANK (receptor) was originally identified as a dendritic cell-membrane protein, which, by interacting with RANKL, augments the ability of dendritic. These dendritic cells then stimulate naive T-cell proliferation, and promote the survival of RANK + T-cells. RANK is also expressed in a variety of tissues, including skeletal muscle, thymus, liver, colon, small intestine, and adrenal gland. The RANK/RANKL interaction is important in the regulation of osteoclastogenesis, and in dendritic cell-mediated T-cell immune responses. Impairments in RANK signaling have been implicated in the induction of expansile osteolysis and Paget's disease of bone (PDB2). Recombinant Human sRANK Receptor is a 19.3 kDa polypeptide containing the TNFR-homologous, cysteine-rich portion of t