||Recombinant murine Persephin produced inE.coliis a disulfide-linked homodimer, composed of two 10.3 kDa polypeptide chains (96 total amino acid residues). Each chain contains seven conserved cysteine residues, one of which (Cys 63) is used for inter-chain disulfide bridging and the others are involved in intramolecular ring formation known as the cysteine knot configuration.
||Persephin is a disulfide-linked homodimer neurotrophic factor structurally related to GDNF, Artemin, and Neurturin. These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. Persephin signals through a multicomponent receptor system, composed of RET and one of four GFRα (α1-α4) receptors. The GFRα4 was first identified in chicken and was later shown to be the preferential binding subunit for Persephin. Persephin promotes the survival of ventral midbrain dompaminergic neurons and motor neurons after sciatic nerve oxotomy, and like GNDF, promotes ureteric bud branching. However, in contrast to GDNF and Neurturin, Persephin does not support survival of peripheral neurons.
||> 98% by SDS-PAGE.
||< 0.1 ng per μg of Persephin.
||The ED50 was determined by its ability to stimulate proliferation of human thyroid carcinoma cells (TT cells) is < 0.1 ng/ml, corresponding to a specific activity of > 1 x 107 units/mg.
||The lyophilized protein is stable for at least 2 years from date of receipt at -20°C. Reconstituted Persephin is stable for at least 3 months when stored in working aliquots with a carrier protein at -20°C. Avoid repeated freeze-thaw cycles.