Overview
- Milbrandt, J. et al. (1998) Neuron 20, 245.
- Bilak, M.M. (1999) Mol. Cell Neurosci. 13, 326.
- Enokido, Y. et al. (1998) Curr. Biol. 8, 1019.
- Masure, S. et al. (2000) J. Biol. Chem. 275, 39427.
BSA (0.1 mg/ml) should be added for more diluted solutions. Centrifuge all product preparations before use (10000 x g 5 min). Repeated freezing/thawing might result in loss of activity.
- Milbrandt, J. et al. (1998) Neuron 20, 245.
- Jaszai, J. et al. (1998) J. Neurosci. Res. 53, 494.
- Bilak, M.M. (1999) Mol. Cell Neurosci. 13, 326.
- Enokido, Y. et al. (1998) Curr. Biol. 8, 1019.
- Masure, S. et al. (2000) J. Biol. Chem. 275, 39427.
- Akerud, P. et al. (2002) Mol. Cell. Neurosci. 21, 205.
Persephin is a novel neurotrophic factor related to GDNF and Neurturin in the GDNF subfamily.1 Persephin is ubiquitously expressed, although at very low levels.2
In sharp contrast to GDNF and Neurturin, Persephin does not support the survival of neurons from peripheral ganglia including sympathetic and parasympathetic neurons, sensory neurons and enteric neurons.1,3 Persephin does promote the survival of midbrain dopaminergic neurons after neurotoxic injury and the survival of spinal motor neurons in vitro and in vivo animal models.
The receptor for Persephin is a multi-component complex composed of RET tyrosine kinase and the glycosyl-phosphatidylinositol (GPI)-anchored co-receptor GFRalpha1-alpha4.4,5
Persephin induces, in vitro, branching of the ureteric bud of the kidney, an activity shared by Neurturin and GDNF.1 Both in vitro and in vivo experiments using animal models suggest that Persephin could be useful in the treatment of neurodegenerative diseases including Parkinson's disease and Amyotrophic Lateral Sclerosis (ALS).6
Recombinant human Persephin protein (#P-320) is a highly pure, recombinant, and biologically active protein.
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