Results for Other Proteins ( 64512 )
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Animal-Free Recombinant Rat GDNF (Legacy Tebubio ref. 167AF-450-51). 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 rat GDNF ligand is a disulfide-linked homodimer consisting of two 15 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 forma
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Animal-Free Recombinant Rat GDNF (Legacy Tebubio ref. 167AF-450-51). 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 rat GDNF ligand is a disulfide-linked homodimer consisting of two 15 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 forma
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Animal-Free Recombinant Bovine FGF-basic (Legacy Tebubio ref. 167AF-450-62). FGF‐basic is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF‐basic is a non‐glycosylated, heparin‐binding growth factor that is expressed in the brain, pituitary, kidney, retina, bone, testis, adrenal gland, liver, monocytes, epithelial cells and endothelial cells. FGF‐basic signals through FGFR 1b, 1c, 2c, 3c and 4. Recombinant Bovine FGF‐basic is a 17.1 kDa protein consisting of 154 amino acid residues.
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Animal-Free Recombinant Bovine FGF-basic (Legacy Tebubio ref. 167AF-450-62). FGF‐basic is one of 23 known members of the FGF family. Proteins of this family play a central role during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF‐basic is a non‐glycosylated, heparin‐binding growth factor that is expressed in the brain, pituitary, kidney, retina, bone, testis, adrenal gland, liver, monocytes, epithelial cells and endothelial cells. FGF‐basic signals through FGFR 1b, 1c, 2c, 3c and 4. Recombinant Bovine FGF‐basic is a 17.1 kDa protein consisting of 154 amino acid residues.
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Alpha-Synuclein is a major component of Lewy bodies in the affected neurons in Parkinson's disease. This protein consists of a conserved degenerative amino-terminal domain and an acidic carboxyl-terminal with higher sequence divergence. α-Synuclein is predominantly expressed in brain, specifically in cerebellum, thalamus, neocortex, hippocampus, and striatum regions. Other tissues express α-Synuclein at very low levels. The physiological role of α-synuclein is not yet well understood. However, the presence of imperfect KTKEGV lipid interacting repeats suggests that it may be involved in synaptic vesicle homeostasis.
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Alpha-Synuclein is a major component of Lewy bodies in the affected neurons in Parkinson's disease. This protein consists of a conserved degenerative amino-terminal domain and an acidic carboxyl-terminal with higher sequence divergence. α-Synuclein is predominantly expressed in brain, specifically in cerebellum, thalamus, neocortex, hippocampus, and striatum regions. Other tissues express α-Synuclein at very low levels. The physiological role of α-synuclein is not yet well understood. However, the presence of imperfect KTKEGV lipid interacting repeats suggests that it may be involved in synaptic vesicle homeostasis.