Neurturin is a disulfide-linked homodimer neurotrophic factor structurally related to GDNF, artemin, and persephin. These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. Neurturin signals through a multicomponent receptor system, composed of RET and one of four GFRα (α1-α4) receptors. Neurturin promotes the development and survival of sympathetic and sensory neurons by signaling through a receptor system composed of RET and GFRα2. The functional form of human neurturin is a disulfide-linked homodimer, of two 11.8 kDa polypeptide monomers (204 total amino acid residues). Each monomer contains seven conserved cysteine residues, one of which (Cys 69) is used for inter-chain disulfide bridging, and the others are involved in the intramolecular ring formation known as the cysteine knot configuration.
- Species: Human
- Expression: E. coli Cell Expressed
- Activity: Typically ≤0.1 ng/mL ED50
- Purity: ≥98%
- Endotoxin: <1.0 EU/μg
- Molecular Mass: 11.8 kDa, homodimer
- Formulation: 10 mM Sodium Citrate, pH 4.0.
- Country of Origin: USA
This was determined by SDS-PAGE gel and HPLC analysis.
Human Neurturin at a concentration of 100 ng/ml will support the survival of 65% of newborn rat sympathetic neurons.
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex.
For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% HSA) and store in working aliquots at -20°C to -80°C.