Other Proteins

Animal-Free Recombinant Human C5a (Legacy Tebubio ref. 167AF-300-70). Complement 5a (C5a) is an enzymatically generated glycoprotein belonging to the anaphylatoxin family of structurally and functionally related proteins. Generated upon the activation of the complement system, C5a, together with C4a, C3a, and the membrane attack complex (C5b-9), functions as a central player in host defense by inducing smooth muscle cell contraction, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes through cell degranulation. In addition to acting as a direct mediator of localized inflammatory response, C5a also initiates both the synthesis and release of IL-8 from monocytes and bronchial epithelial cells, stimulates the proliferation of neurons and hepatocytes, and functions as a potent chemoattractant. Where C5a deficiency, a rare defect of the complement pathway caused by the mutation of the C5a gene, is associated with susceptibility to severe infecti

Animal-Free Recombinant Human sRANK Ligand (E.coli derived) (Legacy Tebubio ref. 167AF-310-01). 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 cells. These dendritic cells then stimulate naive T-cell proliferation in a mixed lymphocyte reaction, promote the survival of RANK+ T-cells, and regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells, including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilag

Animal-Free Recombinant Human sRANK Ligand (E.coli derived) (Legacy Tebubio ref. 167AF-310-01). 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 cells. These dendritic cells then stimulate naive T-cell proliferation in a mixed lymphocyte reaction, promote the survival of RANK+ T-cells, and regulate T-cell-dependent immune response. RANKL, which is expressed in a variety of cells, including osteoblasts, fibroblasts, activated T-cells and bone marrow stromal cells, is also capable of interacting with a decoy receptor called OPG. Binding of soluble OPG to sRANKL inhibits osteoclastogenesis by interrupting the signaling between stromal cells and osteoclastic progenitor cells, thereby leading to excess accumulation of bone and cartilag

Animal-Free Recombinant Human sCD40 Ligand (Legacy Tebubio ref. 167AF-310-02). CD40, a member of the TNF receptor superfamily, 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 intrac

Animal-Free Recombinant Human sCD40 Ligand (Legacy Tebubio ref. 167AF-310-02). CD40, a member of the TNF receptor superfamily, 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 intrac

Animal-Free Recombinant Human sTNF Receptor Type I (Legacy Tebubio ref. 167AF-310-07). 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-b

Animal-Free Recombinant Human sTNF Receptor Type I (Legacy Tebubio ref. 167AF-310-07). 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-b

Animal-Free Recombinant Human 4-1BB Ligand (Legacy Tebubio ref. 167AF-310-11). 4‐1BBL, a member of the TNF superfamily, is expressed in B cells, dendritic cells, activated T cells and macrophages. 4‐1BBL binds to its receptor 4‐1BB, and provides a co‐stimulatory signal for T cell activation and expansion. The human 4‐1BBL gene codes for a 254 amino acid type II transmembrane protein containing a 28 amino acid cytoplasmic domain, a 21 amino acid transmembrane protein domain, and a 205 amino acid extracellular domain. The soluble form of 4‐1BBL contains the TNF‐like portion of the extracellular domain of 4‐1BBL. Recombinant Human 4‐1BB Ligand is a soluble 19.5 kDa protein consisting of 185 amino acid residues.

Animal-Free Recombinant Human 4-1BB Ligand (Legacy Tebubio ref. 167AF-310-11). 4‐1BBL, a member of the TNF superfamily, is expressed in B cells, dendritic cells, activated T cells and macrophages. 4‐1BBL binds to its receptor 4‐1BB, and provides a co‐stimulatory signal for T cell activation and expansion. The human 4‐1BBL gene codes for a 254 amino acid type II transmembrane protein containing a 28 amino acid cytoplasmic domain, a 21 amino acid transmembrane protein domain, and a 205 amino acid extracellular domain. The soluble form of 4‐1BBL contains the TNF‐like portion of the extracellular domain of 4‐1BBL. Recombinant Human 4‐1BB Ligand is a soluble 19.5 kDa protein consisting of 185 amino acid residues.