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When human Neurturin is immobilized at 0.5 µg/mL, human GFRα2 binds with EC50 of 20 - 80 ng/mL in a functional ELISA.
| Cat # | Size | Price | Quantity Check Availability | Save | ||
|---|---|---|---|---|---|---|
| 760302 | 5 µg | 67€ | ||||
| 760304 | 20 µg | 168€ | ||||
Neurturin belongs to the GDNF family of ligands, which consists of 4 members: GDNF, Neurturin, Artemin, and Persephin. GDNF family members orchestrate multiple aspects of the development and maintenance of the central and peripheral nervous systems. These GDNF family ligands signal through a multicomponent receptor system composed of a common signaling component RET (receptor tyrosine kinase) and one of the high affinity binding coreceptor GFRα (α1-α4). Neurturin is a GDNF family member that functions as a ligand for the GFRα2 and RET complex. Neurturin is a potent neurotrophic factor that can promote the survival of numerous neuronal populations, which include the sympathetic, nodose, and dorsal root ganglion sensory neurons. Neurturin is synthesized as a precursor protein that is cleaved to release the carboxy-terminal domain. The carboxy-terminal domain contains seven conserved cysteine residues that are necessary for the formation of the cysteine-knot and the single interchain disulfide bond. The functional form of human Neurturin is a disulfide-linked homodimer of the carboxy-terminal 102 amino acid residues. Studies have shown positive results for Neurturin in protecting and repairing dopaminergic neurons in various models of Parkinson's disease. In association with mutations of RET gene, genetic variations in Neurturin may contribute to Hirschsprung's disease.
Product DetailsProduct Details
- Source
- Human Neurturin, amino acids (Ala96-Val197) (Accession# Q99748), was expressed in E. coli.
- Molecular Mass
- The 102 amino acid recombinant protein has a predicted molecular mass of approximately 11.7 kD. The predicted N-terminal amino acid is Ala.
- Purity
- >98%, as determined by SDS PAGE gel and HPLC analysis.
- Formulation
- Lyophilized from 0.2 µm filtered protein solution in 10 mM Sodium Citrate, pH 4.0.
- Endotoxin Level
- Less than 1.0 EU per µg protein as determined by the LAL method.
- Storage & Handling
- Unopened vial can be stored at -20°C or -70°C. For maximum results, quick spin vial prior to opening. Reconstitute in water to a concentration of 0.1-0.5 mg/ml. Do not vortex. It is recommended to further dilute in a buffer containing a carrier protein such as 0.1% BSA and store working aliquots at -20°C to -80°C. Avoid repeated freeze/thaw cycles.
- Activity
- EC50 = 20 - 80 ng/mL as measured by the ability for the immobilized protein to bind GFRα2 in a functional ELISA.
- Application
-
Bioassay
Antigen Details
- Structure
- Disulfide-linked homodimer.
- Distribution
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Neurturin is a secreted protein that is expressed in both neuronal tissues and non-neuronal tissues such as the pancreas, heart, and hair follicles.
- Function
- It is a neurotrophic factor and promotes the survival of sympathetic, nordose, and dorsal root ganglion sensory neurons.
- Interaction
- Neurturin targets multiple central and peripheral neurons including the midbrain dopaminergic, sympathetic, and sensory neurons.
- Ligand/Receptor
- Interacts with GDNF family receptor α-2(GFRα2). Has a lower affinity with GFRα1.
- Bioactivity
- Measured by the ability of immobilized human Neurturin to bind GFRα2 in a functional ELISA.
- Cell Type
- Embryonic Stem Cells, Neural Stem Cells
- Biology Area
- Cell Biology, Neuroscience, Stem Cells, Synaptic Biology
- Molecular Family
- Growth Factors
- Antigen References
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1. Kotzbauer PT, et al. 1996. Nature 6608:467-70.
2. Doray B, et al. 1998. Hum. Mol. Genet. 7:1449-1452.
3. Milbrandt J, et al. 1998. Neuron 20:245-253.
4. Baloh RH, et al. 1998. Neuron. 21:1291-1302.
5. Sariola H, Saarma M. 2003. 116:3855-3862.
6. Ruiz-Ferrer M, et al. 2011. J. Mol. Med. (Berl) 5:471-480.
7. Lindholm D, et al. 2016. Cell Mol. Life Sci. 7:1365-79. - Gene ID
- 4902 View all products for this Gene ID
- UniProt
- View information about Neurturin on UniProt.org
Related FAQs
- Why choose BioLegend recombinant proteins?
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• Each lot of product is quality-tested for bioactivity as indicated on the data sheet.
• Greater than 95% Purity or higher, tested on every lot of product.
• 100% Satisfaction Guarantee for quality performance, stability, and consistency.
• Ready-to-use liquid format saves time and reduces challenges associated with reconstitution.
• Bulk and customization available. Contact us.
• Learn more about our Recombinant Proteins. - How does the activity of your recombinant proteins compare to competitors?
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We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!
- What is the specific activity or ED50 of my recombinant protein?
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The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.
- Have your recombinants been tested for stability?
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Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.
- Does specific activity of a recombinant protein vary between lots?
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Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.
- How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
- Use formula Specific activity (Units/mg) = 10e6/ ED50 (ng/mL)
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