Other Proteins

Recombinant Human Galectin-3 (Legacy Tebubio ref. 167450-38). Lectins, of either plant or animal origin, are carbohydrate-binding proteins that interact with glycoproteins and glycolipids on the surface of animal cells. The Galectins are lectins that recognize and interact with beta-galactoside moieties. Galectin-3 regulates a number of biological processes, including embryogenesis, inflammatory responses, cell progression and metastasis. Galectin-3 is normally expressed in epithelia of a variety of tissues, including colon and endometrium, and in various inflammatory cells, including macrophages. Galectin-3 can function intracellularly, controlling the cell cycle and preventing T-cell apoptosis, and also extracellularly, by activating various cells, including monocytes/macrophages, mast cells, neutrophils, and lymphocytes. Expression of Galectin-3 is affected by neoplastic transformation, being up-regulated in certain types of lymphomas, and in thyroid and hepatic carcinomas. Converse

Recombinant Human Galectin-3 (Legacy Tebubio ref. 167450-38). Lectins, of either plant or animal origin, are carbohydrate-binding proteins that interact with glycoproteins and glycolipids on the surface of animal cells. The Galectins are lectins that recognize and interact with beta-galactoside moieties. Galectin-3 regulates a number of biological processes, including embryogenesis, inflammatory responses, cell progression and metastasis. Galectin-3 is normally expressed in epithelia of a variety of tissues, including colon and endometrium, and in various inflammatory cells, including macrophages. Galectin-3 can function intracellularly, controlling the cell cycle and preventing T-cell apoptosis, and also extracellularly, by activating various cells, including monocytes/macrophages, mast cells, neutrophils, and lymphocytes. Expression of Galectin-3 is affected by neoplastic transformation, being up-regulated in certain types of lymphomas, and in thyroid and hepatic carcinomas. Converse

Recombinant Human Galectin-1 (Legacy Tebubio ref. 167450-39). Lectins, of either plant or animal origin, are carbohydrate-binding proteins that interact with glycoprotein and glycolipids on the surface of animal cells. The Galectins are lectins that recognize and interact with beta-galactoside moieties. Galectin-1 is an animal lectin that has been shown to interact with CD3, CD4, and CD45. It induces apoptosis of activated T cells and T leukemia cell lines, and inhibits the protein phosphatase activity of CD45. Recombinant Human Galectin-1 is a 14.5 kDa protein containing 134 amino acid residues.

Recombinant Human Galectin-1 (Legacy Tebubio ref. 167450-39). Lectins, of either plant or animal origin, are carbohydrate-binding proteins that interact with glycoprotein and glycolipids on the surface of animal cells. The Galectins are lectins that recognize and interact with beta-galactoside moieties. Galectin-1 is an animal lectin that has been shown to interact with CD3, CD4, and CD45. It induces apoptosis of activated T cells and T leukemia cell lines, and inhibits the protein phosphatase activity of CD45. Recombinant Human Galectin-1 is a 14.5 kDa protein containing 134 amino acid residues.

Recombinant Human sCD30 Ligand (Legacy Tebubio ref. 167450-42). CD30 ligand (CD30L) is a type-II membrane-associated glycoprotein belonging to the TNF superfamily and is expressed primarily on certain B cells, T cells, and monocytes. CD30L binds specifically to CD30 (receptor), which is expressed on activated, but not resting, B and T cells, in lymphomas and various chronically inflamed tissues. CD30L/CD30 interactions initiate a signaling cascade that can ultimately lead to the activation of NF-kappaB. CD30L/CD30 signaling exerts pleiotropic effects on normal cells, including cell death, differentiation, and cell division. Certain diseases, including Hodgkin's lymphoma, allergic inflammation, diabetes (in NOD mice), and mycobacterial infection can also be affected by CD30L/CD30 signaling. The CD30L gene encodes for a 234 amino acid type II transmembrane protein, which contains a 37 amino acid cytoplasmic sequence, a 25 amino acid transmembrane domain and a 172 amino acid extracellular

Recombinant Human sCD30 Ligand (Legacy Tebubio ref. 167450-42). CD30 ligand (CD30L) is a type-II membrane-associated glycoprotein belonging to the TNF superfamily and is expressed primarily on certain B cells, T cells, and monocytes. CD30L binds specifically to CD30 (receptor), which is expressed on activated, but not resting, B and T cells, in lymphomas and various chronically inflamed tissues. CD30L/CD30 interactions initiate a signaling cascade that can ultimately lead to the activation of NF-kappaB. CD30L/CD30 signaling exerts pleiotropic effects on normal cells, including cell death, differentiation, and cell division. Certain diseases, including Hodgkin's lymphoma, allergic inflammation, diabetes (in NOD mice), and mycobacterial infection can also be affected by CD30L/CD30 signaling. The CD30L gene encodes for a 234 amino acid type II transmembrane protein, which contains a 37 amino acid cytoplasmic sequence, a 25 amino acid transmembrane domain and a 172 amino acid extracellular

Recombinant Murine GDNF (Legacy Tebubio ref. 167450-44). GDNF is a disulfide-linked, homodimeric neurotrophic factor structurally related to Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. GDNF signals through a multicomponent receptor system, composed of a RET and one of the four GFRalpha (alpha1-alpha4) receptors. GDNF specifically promotes dopamine uptake and survival, and morphological differentiation of midbrain neurons. Using a Parkinson's disease mouse model, GDNF has been shown to improve conditions such as bradykinesia, rigidity, and postural instability. The functional murine GDNF ligand is a disulfide-linked homodimer consisting of two 15.1 kDa polypeptide chains called monomers. Each monomer contains seven conserved cysteine residues, including Cys-101, which is used for inter-chain disulfide bridging, and others that are involved in the intramolecular ring format

Recombinant Murine GDNF (Legacy Tebubio ref. 167450-44). GDNF is a disulfide-linked, homodimeric neurotrophic factor structurally related to Artemin, Neurturin and Persephin. These proteins belong to the cysteine-knot superfamily of growth factors that assume stable dimeric protein structures. GDNF signals through a multicomponent receptor system, composed of a RET and one of the four GFRalpha (alpha1-alpha4) receptors. GDNF specifically promotes dopamine uptake and survival, and morphological differentiation of midbrain neurons. Using a Parkinson's disease mouse model, GDNF has been shown to improve conditions such as bradykinesia, rigidity, and postural instability. The functional murine GDNF ligand is a disulfide-linked homodimer consisting of two 15.1 kDa polypeptide chains called monomers. Each monomer contains seven conserved cysteine residues, including Cys-101, which is used for inter-chain disulfide bridging, and others that are involved in the intramolecular ring format

Recombinant Rat CNTF (Legacy Tebubio ref. 167450-50). CNTF is a potent neural factor that was originally characterized as a vital factor for the survival of chick ciliary neurons in vitro. CNTF is also important for the survival of other neural cell types, including primary sensory neurons, motor neurons, basal forebrain neurons and type 2 astrocytes. CNTF is highly conserved across species and exhibits cross-species bioactivity. Recombinant Rat CNTF is synthesized as a 199 amino acid polypeptide (22.7 kDa) lacking a hydrophobic N-terminal signal for secretion.