Cytokines & Chemokines

Recombinant Human Chemerin (Legacy Tebubio ref. 167300-66). Chemerin is a secreted chemoattractant protein that can signal through the chemokine-like receptor-1 (CMKLR1). It is expressed in various tissues, including white adipose tissue, and circulates in blood as an inactive 143 amino acid precursor protein. Biologically active Chemerin is generated by proteolytic removal of C-terminal residues by several circulating proteases. Chemerin acts as a chemoattractant for cells expressing the CMKLR1 receptor, which includes certain dendritic cells, macrophages, and adipocytes. Recombinant Human Chemerin is a 15.6 kDa protein consisting of 135 amino acid residues.

Recombinant Human Chemerin (Legacy Tebubio ref. 167300-66). Chemerin is a secreted chemoattractant protein that can signal through the chemokine-like receptor-1 (CMKLR1). It is expressed in various tissues, including white adipose tissue, and circulates in blood as an inactive 143 amino acid precursor protein. Biologically active Chemerin is generated by proteolytic removal of C-terminal residues by several circulating proteases. Chemerin acts as a chemoattractant for cells expressing the CMKLR1 receptor, which includes certain dendritic cells, macrophages, and adipocytes. Recombinant Human Chemerin is a 15.6 kDa protein consisting of 135 amino acid residues.

Recombinant Human MIF (Legacy Tebubio ref. 167300-69). Macrophage migration inhibitory factor (MIF) is a small secreted protein that can act as a pleiotropic pro-inflammatory cytokine, as well as an enzyme. MIF pro-inflammatory activity can be initiated by signaling through CD74 and CD44, resulting in the secretion of TNF-a, IL-1, IL-6, IL-8, and various MMPs. The enzymatic activity of MIF is characterized by its ability to act as a tautomerase, capable of catalyzing the keto-to-enol isomerization of keto-phenylpyruvate and L-dopachrome. It appears as though MIF catalytic activity is dependent upon a trimeric configuration and a free N-terminal proline residue. Insect cell-derived Recombinant Human MIF is a 15 kDa protein containing 124 amino acid residues, including an N-terminal His-tag.

Recombinant Human MIF (Legacy Tebubio ref. 167300-69). Macrophage migration inhibitory factor (MIF) is a small secreted protein that can act as a pleiotropic pro-inflammatory cytokine, as well as an enzyme. MIF pro-inflammatory activity can be initiated by signaling through CD74 and CD44, resulting in the secretion of TNF-a, IL-1, IL-6, IL-8, and various MMPs. The enzymatic activity of MIF is characterized by its ability to act as a tautomerase, capable of catalyzing the keto-to-enol isomerization of keto-phenylpyruvate and L-dopachrome. It appears as though MIF catalytic activity is dependent upon a trimeric configuration and a free N-terminal proline residue. Insect cell-derived Recombinant Human MIF is a 15 kDa protein containing 124 amino acid residues, including an N-terminal His-tag.

Recombinant Human GPR15L (Legacy Tebubio ref. 167300-71). GPR15L is a newly identified ligand for GPR15, a member of the G protein-coupled receptor (GPCR) family. Upon ligation, GPR15L acts as a potent chemoattractant for GPR15-expressing T cells and together they mediate lymphocyte recruitment to the large intestine and skin. GPR15L is constitutively expressed by colon epithelial cells where its expression is minimally altered by intestinal inflammation. Conversely, GPR15L is nearly undetectable in adult epidermis but highly upregulated during wound healing and inflammation, particularly in psoriasis. Significant expression of GPR15L is also seen in additional mucosal epithelial cells, including those of the stomach, esophagus, and urinary tract. While maintaining similar expression patterns and intramolecular disulfide cysteine bridges found in members of the CC chemokine family, GPR15L differs from classic CC and CXC chemokines, whose active sites are found on the N-terminus, in tha

Recombinant Human GPR15L (Legacy Tebubio ref. 167300-71). GPR15L is a newly identified ligand for GPR15, a member of the G protein-coupled receptor (GPCR) family. Upon ligation, GPR15L acts as a potent chemoattractant for GPR15-expressing T cells and together they mediate lymphocyte recruitment to the large intestine and skin. GPR15L is constitutively expressed by colon epithelial cells where its expression is minimally altered by intestinal inflammation. Conversely, GPR15L is nearly undetectable in adult epidermis but highly upregulated during wound healing and inflammation, particularly in psoriasis. Significant expression of GPR15L is also seen in additional mucosal epithelial cells, including those of the stomach, esophagus, and urinary tract. While maintaining similar expression patterns and intramolecular disulfide cysteine bridges found in members of the CC chemokine family, GPR15L differs from classic CC and CXC chemokines, whose active sites are found on the N-terminus, in tha

Recombinant Murine GPR15L (Legacy Tebubio ref. 167300-72). GPR15L is a newly identified ligand for GPR15, a member of the G protein‐coupled receptor (GPCR) family. Upon ligation, GPR15L acts as a potent chemoattractant for GPR15‐expressing T cells and together they mediate lymphocyte recruitment to the large intestine and skin. GPR15L is constitutively expressed by colon epithelial cells where its expression is minimally altered by intestinal inflammation. Conversely, GPR15L is nearly undetectable in adult epidermis but highly upregulated during wound healing and inflammation, particularly in psoriasis. Significant expression of GPR15L is also seen in additional mucosal epithelial cells, including those of the stomach, esophagus, and urinary tract. While maintaining similar expression patterns and intramolecular disulfide cysteine bridges found in members of the CC chemokine family, GPR15L differs from classic CC and CXC chemokines, whose active sites are found on the N‐terminus, in th

Recombinant Murine GPR15L (Legacy Tebubio ref. 167300-72). GPR15L is a newly identified ligand for GPR15, a member of the G protein‐coupled receptor (GPCR) family. Upon ligation, GPR15L acts as a potent chemoattractant for GPR15‐expressing T cells and together they mediate lymphocyte recruitment to the large intestine and skin. GPR15L is constitutively expressed by colon epithelial cells where its expression is minimally altered by intestinal inflammation. Conversely, GPR15L is nearly undetectable in adult epidermis but highly upregulated during wound healing and inflammation, particularly in psoriasis. Significant expression of GPR15L is also seen in additional mucosal epithelial cells, including those of the stomach, esophagus, and urinary tract. While maintaining similar expression patterns and intramolecular disulfide cysteine bridges found in members of the CC chemokine family, GPR15L differs from classic CC and CXC chemokines, whose active sites are found on the N‐terminus, in th

Recombinant Human TWEAK (Legacy Tebubio ref. 167310-06). TWEAK belongs to the TNF family of ligands, and signals through TWEAKR, also known as TNFRSF12A. TWEAK is expressed in a variety of tissues, including the adult heart, pancreas, skeletal muscle, small intestine, spleen and peripheral blood lymphocytes. TWEAK has the ability to induce NF-kappaB activation and chemokine secretion, and to exert an apoptotic activity in certain cells, such as HT-29 human adenocarcinoma cells when cultured in the presence of IFN-gamma. TWEAK also promotes proliferation and migration of endothelial cells. The human TWEAK gene encodes for a 249 amino acid type II transmembrane protein, which contains a 21 amino acid cytoplasmic domain, a 21 amino acid transmembrane domain, and a 207 amino acid extracellular domain. Recombinant Human TWEAK is a soluble 17.0 kDa polypeptide (154 amino acid residues) comprising the TNF-homologous region of TWEAK, and is generated by proteolytic processing of the full lengt