Persephin is a disulfide-linked, homodimeric, 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 GFR α (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 dopaminergic neurons and motor neurons
after sciatic nerve oxotomy, and, like GDNF, promotes ureteric bud
branching. However, in contrast to GDNF and neurturin, persephin does
not support the survival of peripheral neurons. Recombinant Murine Persephin is a disulfide-linked homodimer, composed of two 10.3 kDa polypeptide chains (192 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 the intramolecular ring formation known as the cysteine knot configuration.
ALAGSCRLWS LTLPVAELGL GYASEEKVIF RYCAGSCPQE ARTQHSLVLA RLRGRGRAHG RPCCQPTSYA DVTFLDDQHH WQQLPQLSAA ACGCGG
Greater than 98% by SDS-PAGE gel and HPLC analyses.
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.
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