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. Recombinant murine Persephin is 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
Mouse Pspn expressed in E.coli
CAT# CSC-CTK0760-20 (20 μg); CAT# CSC-CTK0760-100 (100 μg)
Greater than 98% as determined by SDS-PAGE and HPLC analysis.
The ED50 was determined by its ability to stimulate proliferation of human thyroid carcinoma cells (TT cells) is 1 x 10^7 units/mg.
Less than 1 EU/μg.
Lyophilized from a sterile-filtered solution with no additives.
Please centrifuge product before opening vial. The lyophilized protein should be reconstituted with distilled, sterile water to a concentration of 0.1-1.0 mg/ml. For further dilution, carrier protein (0.1% BSA or HSA) should be added to avoid loss of bioactivity.
Storage & Stability
The lyophilized protein, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted protein should be used immediately or stored long-term in undiluted working aliquots at -20°C. For long-term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
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