| Field | Specification |
|---|---|
| Mfr No | |
| Accession Number | |
| Activity | |
| Alternative Names | PSP |
| Form | Lyophilized |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
| Product Type | |
| Purity | |
| Reconstitution | |
| Solubility | Centrifuge the vial before adding solvent (10,000 x g for 5 minutes) to spin down all the powder to the bottom of the vial. The lyophilized product may be difficult to visualize. Add solvent directly to the centrifuged vial. Tap the vial to aid in dissolving the lyophilized product. Tilt and gently roll the liquid over the walls of the vial. Avoid vigorous vortexing. Light vortexing for up to 3 seconds is acceptable if needed. For long-term storage in solution, we recommend preparing a stock solution by dissolving the product in sterile water at a concentration of at least 0.1 mg/mL. Divide the stock solution into small aliquots and store at -20°C. Before use, thaw the relevant vial(s) and dilute to the desired working concentration in your working buffer. It is recommended to prepare fresh solutions in working buffers just before use. For long-term storage of diluted solutions, we recommend adding 0.1% BSA. Repeat freeze-thawing may result in loss of activity. |
| Source | Recombinant, E. coli |
| Storage | |
| Target |
Overview
Recombinant human Persephin protein is a research-grade protein/peptide reagent used in research settings. It is commonly applied as a tool reagent related to GFRa4 biology and/or assay development. It is supplied in Lyophilized format to support flexible downstream use in RUO workflows.
Key elements and design rationale
- Molecular identity: MW: 20.6 kDa (dimer).
- Source / origin: Recombinant, E. coli.
- Quality attributes: Purity: ≥98% (HPLC); Bioassay tested: Yes; Sterile / endotoxin-free: No.
When used as a biochemical or pharmacological tool, results are best interpreted relative to the experimental system (species, expression level, and assay readout) and with appropriate negative and competition-style controls where relevant. This product is intended for research use only.
Biological background
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.2In 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-alpha4.4,5Persephin 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
Research relevance and current trends
- Using high-specificity ligands, toxins, and engineered peptides to dissect closely related receptor/channel subtypes and signaling microdomains.
- Pairing labeled (e.g., fluorescent) proteins/peptides with advanced imaging to map surface expression, trafficking, and nanoscale organization.
- Increasing emphasis on reproducibility through standardized characterization (identity, purity, and lot QC) and transparent reporting of reagent attributes.
Common research applications
- Assay development and optimization: used as a reference material or tool reagent in RUO workflows.
- Reagent validation: supports conceptual controls such as competition/neutralization, when relevant.
Across these use cases, changes in signal or functional readout are generally interpreted as evidence of differences in target abundance, accessibility, or engagement, but alternative explanations (matrix effects, off-target interactions, or assay artifacts) should be considered.
Notes for experimental interpretation
- Assay context matters: binding assays, functional modulation, and detection workflows can yield different readouts even for the same target system.
- Target complexity: closely related family members, splice variants, and post-translational modifications can influence apparent specificity and potency.
- Matrix and sample effects: buffer composition, detergents, and biological matrices may alter stability or apparent activity; interpret with appropriate controls.
- Control concepts: include negative controls and orthogonal validation (e.g., genetic perturbation or alternative reagents) to support robust interpretation.
Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.
Jones, H.M.
et al. (2016) Clin Pharmacokinet. 55, 875.
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.
Akerud, P.
et al. (2002) Mol. Cell. Neurosci. 21, 205.
Milbrandt, J.
et al. (1998) Neuron20, 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.
Masure, S.
et al. (2000) J. Biol. Chem. 275, 39427.
