Enzymes

Recombinant Human TIGAR-TAT (Legacy Tebubio ref. 167150-14T). TIGAR is a p53-inducible enzyme that catalyzes the hydrolysis of fructose-2-6 bisphosphate (F-2-6-BP) to fructose-6-phosphate and inorganic phosphate. F-2-6-BP is a powerful activator of 6-phosphofructose-1 kinase, the rate limiting enzyme of glycolysis. By lowering the intracellular level of F-2-6-BP, TIGAR expression leads to increased glucose processing via the pentose phosphate pathway, the major cellular source for NADPH. Protein transduction using TAT fusion proteins represents an alternative methodology for introducing transcription factors and other intracellular proteins into primary, as well as transformed, cells. Recombinant Human TIGAR-TAT expressed in E.coli is a 31.6 kDa protein containing 283 amino acid residues, including the 269 residues of full-length TIGAR fused to a 14-residue C-terminal peptide containing the TAT transduction domain (GGGYGRKKRRQRRR).

Recombinant Human TIGAR-TAT (Legacy Tebubio ref. 167150-14T). TIGAR is a p53-inducible enzyme that catalyzes the hydrolysis of fructose-2-6 bisphosphate (F-2-6-BP) to fructose-6-phosphate and inorganic phosphate. F-2-6-BP is a powerful activator of 6-phosphofructose-1 kinase, the rate limiting enzyme of glycolysis. By lowering the intracellular level of F-2-6-BP, TIGAR expression leads to increased glucose processing via the pentose phosphate pathway, the major cellular source for NADPH. Protein transduction using TAT fusion proteins represents an alternative methodology for introducing transcription factors and other intracellular proteins into primary, as well as transformed, cells. Recombinant Human TIGAR-TAT expressed in E.coli is a 31.6 kDa protein containing 283 amino acid residues, including the 269 residues of full-length TIGAR fused to a 14-residue C-terminal peptide containing the TAT transduction domain (GGGYGRKKRRQRRR).

Recombinant Human sFas Ligand (Legacy Tebubio ref. 167310-03H). Fas Ligand (FasL) is a member of the TNF superfamily that is expressed on the cell surface of activated T cells. Binding of FasL to Fas Receptor triggers apoptosis in Fas-bearing cells. FasL has the ability to kill T cells and activated B cells, which leads to down-regulation of the immune response. The mechanism of Fas-induced apoptosis involves recruitment of pro-caspase 8 through an adaptor molecule called FADD, followed by processing of the pro-enzyme into active forms. These active caspases then cleave various cellular substrates, leading to the eventual cell death. Both human and murine sFasL are fully active on human and murine cells. Recombinant Human soluble Fas Ligand is a 17.9 kDa protein comprising the TNF-homologous region of FasL and contains an 8-residue N-terminal His-Tag.

Recombinant Human sFas Ligand (Legacy Tebubio ref. 167310-03H). Fas Ligand (FasL) is a member of the TNF superfamily that is expressed on the cell surface of activated T cells. Binding of FasL to Fas Receptor triggers apoptosis in Fas-bearing cells. FasL has the ability to kill T cells and activated B cells, which leads to down-regulation of the immune response. The mechanism of Fas-induced apoptosis involves recruitment of pro-caspase 8 through an adaptor molecule called FADD, followed by processing of the pro-enzyme into active forms. These active caspases then cleave various cellular substrates, leading to the eventual cell death. Both human and murine sFasL are fully active on human and murine cells. Recombinant Human soluble Fas Ligand is a 17.9 kDa protein comprising the TNF-homologous region of FasL and contains an 8-residue N-terminal His-Tag.

Recombinant Human sFas Receptor (Legacy Tebubio ref. 167310-20). Fas and Fas Ligand (FasL) belong to the TNF superfamily, and are type I and type II transmembrane proteins, respectively. Binding of FasL to Fas triggers apoptosis in Fas-bearing cells. The mechanism of apoptosis involves recruitment of pro-caspase 8 through an adaptor molecule called FADD, followed by processing of the pro-enzyme into active forms. These active caspases then cleave various cellular substrates, leading to the eventual cell death. sFasR is capable of inhibiting FasL-induced apoptosis by acting as a decoy receptor that serves as a sink for FasL. The full length Fas (receptor) is a 319 amino acid type I transmembrane protein, which contains a 157 amino acid extracellular domain, a 17 amino acid transmembrane domain, and a 145 amino acid cytoplasmic domain. Recombinant Human soluble Fas (sFas Receptor) is a 157 amino acid polypeptide (17.6 kDa) corresponding to the TNFR-homologous cysteine-rich extracellular

Recombinant Human sFas Receptor (Legacy Tebubio ref. 167310-20). Fas and Fas Ligand (FasL) belong to the TNF superfamily, and are type I and type II transmembrane proteins, respectively. Binding of FasL to Fas triggers apoptosis in Fas-bearing cells. The mechanism of apoptosis involves recruitment of pro-caspase 8 through an adaptor molecule called FADD, followed by processing of the pro-enzyme into active forms. These active caspases then cleave various cellular substrates, leading to the eventual cell death. sFasR is capable of inhibiting FasL-induced apoptosis by acting as a decoy receptor that serves as a sink for FasL. The full length Fas (receptor) is a 319 amino acid type I transmembrane protein, which contains a 157 amino acid extracellular domain, a 17 amino acid transmembrane domain, and a 145 amino acid cytoplasmic domain. Recombinant Human soluble Fas (sFas Receptor) is a 157 amino acid polypeptide (17.6 kDa) corresponding to the TNFR-homologous cysteine-rich extracellular

Recombinant Human ApoE3 (Legacy Tebubio ref. 167350-02). ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solubilization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in the liver and brain, and to some extent in almost every organ. ApoE is an important constituent of all plasma lipoproteins. Its interaction with specific ApoE receptor enables uptake of chylomicron remnants by liver cells, which is an essential step during normal lipid metabolism. It also binds with the LDL receptor (apo B/E). Defects in ApoE are a cause of hyperlipoproteinemia type III. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. E3 is the most c

Recombinant Human ApoE3 (Legacy Tebubio ref. 167350-02). ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solubilization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in the liver and brain, and to some extent in almost every organ. ApoE is an important constituent of all plasma lipoproteins. Its interaction with specific ApoE receptor enables uptake of chylomicron remnants by liver cells, which is an essential step during normal lipid metabolism. It also binds with the LDL receptor (apo B/E). Defects in ApoE are a cause of hyperlipoproteinemia type III. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. E3 is the most c

Recombinant Human ApoE4 (Legacy Tebubio ref. 167350-04). ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism. In addition to facilitating solubilization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism. Significant quantities of ApoE are produced in the liver and brain, and to some extent in almost every organ. ApoE is an important constituent of all plasma lipoproteins. Its interaction with specific ApoE receptor enables uptake of chylomicron remnants by liver cells, which is an essential step during normal lipid metabolism. It also binds with the LDL receptor (apo B/E). Defects in ApoE are a cause of hyperlipoproteinemia type III. ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution. Individuals hete