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 GFRalpha (alpha-1 - alpha-4) receptors. The GFR(-4 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 human Persephin is a disulfide-linked homodimer, composed of two 10.3 kDa polypeptide chains (192 total amino acid residues).
Human PSPN expressed in E.coli
CAT# CSC-CTK0485-20 (20 μg); CAT# CSC-CTK0485-100 (100 μg)
Greater than 98% as determined by SDS-PAGE and HPLC analysis.
Human Persephin induces RET phosphorylation using a concentration range of 0.1-1.0 ng/ml. Human Persephin binds to mammalian GFR(-4 with the Kd of 100 pM. Other members of the GDNF family (Artemin, GDNF and Neurturin) do not bind to mammalian GFR-4.
Less than 1 EU/μg.
Lyophilized from a sterile-filtered solution in 0.3x PBS (pH 7.2).
Please centrifuge product briefly before opening the vial. Reconstitute in sterile, ultra-pure water to a concentration of 0.1-1.0 mg/ml. This solution can be diluted into other aqueous buffers and stored at -20°C for future use.
Storage & Stability
The lyophilized powder, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted PSP should be used immediately or stored in undiluted working aliquots at -20°C. Avoid repeated freeze / thaw cycles.
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