NRTN Human
Description
Product Specs
To reconstitute the lyophilized NRTN, it is recommended to dissolve it in sterile 18 MΩ-cm H2O to a concentration of at least 0.5 mg/ml. The reconstituted solution can be further diluted in other aqueous solutions as needed.
Product Science Overview
Neurturin is synthesized as a precursor protein that is cleaved at a dibasic cleavage site to release the carboxy-terminal domain . The carboxy-terminal domain contains seven conserved cysteine residues necessary for forming the cysteine-knot and the single interchain disulfide bond . Biologically active human Neurturin is a disulfide-linked homodimer of the carboxy-terminal 102 amino acid residues .
Neurturin is expressed in both neuronal and non-neuronal tissues . It plays a crucial role in regulating the development and maintenance of the central and peripheral nervous systems, as well as non-neuronal systems . Neurturin preferentially binds to GFRα-2 but can also bind GFRα-1 at higher concentrations . The bioactivities of all GDNF family ligands are mediated through a unique multicomponent receptor complex composed of high-affinity ligand-binding components (GFRα-1 to GFRα-4) and a common signaling component (cRET receptor tyrosine kinase) .
Recombinant human Neurturin is typically produced in E. coli and has a predicted molecular mass of approximately 11.8 kDa (monomer) . It is often used in research to study its effects on cell proliferation, particularly in neuroblastoma cells . The recombinant protein is available in both carrier-free and carrier-containing formulations, with the carrier protein usually being Bovine Serum Albumin (BSA) .
Recombinant human Neurturin is used in various research applications, including cell culture and ELISA standards . It is also utilized to study its binding ability in functional assays, such as ELISA . The protein’s stability and storage conditions are crucial for maintaining its biological activity, with recommendations to store it at -20 to -70°C and avoid repeated freeze-thaw cycles .
