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- Regulatory Status
- RUO
- Other Names
- Neurotrophin 4 (NT-4), Neurotrophin 5 (NT-5)
- Ave. Rating
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- Product Citations
- publications
| Cat # | Size | Price | Save |
|---|---|---|---|
| 598302 | 10 µg | ¥43,390 |
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Neurotrophins are growth factors that modulate growth, differentiation, and survival of neurons. Structure related proteins include neuron growth factor (NGF), brain derived neurogenic factor (BDNF), neurotrophin-3 (NT-3), and neurotrophin-4/5 (NT-4). They are highly homologous and share a similar structure with a tertiary folded, cysteine rich "knot". Neurotrophins are critical to the development of the central and peripheral nervous systems and play important roles in injury induced neuron regeneration. NT-4 is encoded by the NTF4 gene. The name NT-4/5 arose from the uncertainties between neurotrophin-5 found in humans and neurotrophin-4 identified in Xenopus. Although NT-4 is structurally the most divergent neurotrophin, like BNDF NT-4 binds to receptor TrkB with high affinity and mediates similar functions with BDNF in neurogenesis. However, similar to NGF and NT-3 gene-knockouts, the disruption of BDNF function severely affects neuron development. However, NT-4 knockout mice show minor deficits, with nearly 50% neuron loss in nodose-petrosal and geniculate ganglia. The double knockouts of BDNF and NT-4 present additive deficit phenotype compared to NT-4 knockout mice. It is thus suggested that there are two groups of downstream target cells through multiple coreceptors interaction of BDNF/TrkB and NT-4/TrkB signaling. There are also some exceptions of biological actions of NT-4 that are not parallel with BDNF function. NT-4, but not BDNF, is reported to promote survival of striatal neurons and is able to overturn spatial memory impairments in aged rats. NT-4 is also suggested to participate in stem cell differentiation toward oligodendrocyte progenitor cells in the brain.
Product DetailsProduct Details
- Source
- Human NT-4, amino acids Gly81-Ala210, (Accession# NM_006179.4), was expressed in E. coli.
- Molecular Mass
- NT-4 recombinant protein is a noncovalent linked homodimer. The 130 amino acid recombinant protein has a predicted molecular mass of approximately 14 kD as monomer, 28 kD as dimer. The predicted N-terminal Amino acid is Gly.
- Purity
- >98%, as determined by SDS-PAGE and HPLC analysis.
- Formulation
- Lyophilized
- Endotoxin Level
- Less than 0.1 ng per µg of protein.
- 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 0.1-1.0 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
- The ED50, determined by the dose-dependent induction of choline acetyl transferase activity in rat basal forbrain primary septal cell cultures, was found to be in the range of 20-50 ng/ml, corresponding to a specific activity of 2-5 x 104 units/mg.
- Application
-
Bioassay
- Application Notes
-
This product is reactive with human, rat, frog, and mouse.
Antigen Details
- Structure
- Dimeric growth factor.
- Distribution
-
NT-4 is expressed in the prostate and at lower levels in the thymus, placenta, and skeletal muscle.
- Function
- NT-4 promotes cell survival of peripheral sensory sympathetic neurons.
- Interaction
- Neuroblasts and sensory sympathetic neurons.
- Ligand/Receptor
- p75NTR, TrkA, TrkB.
- Cell Type
- Neural Stem Cells
- Biology Area
- Cell Biology, Neuroscience, Stem Cells, Synaptic Biology
- Molecular Family
- Cytokines/Chemokines, Growth Factors
- Antigen References
-
1. Roosen A, et al. 2001. J. Neurosci. 21:3073.
2. Skaper SD. 2008. CNS Neurol. Disord. Drug Targets 7:46.
3. Ibáñez CF, et al. 1996. Neurochem. Res. 21:787.
4. Lai KO, et al. 1998. Mol. Cell. Neurosci. 11:64.
5. Eide FF, et al. 1993. Exp. Neurol. 121:200. - Gene ID
- 4909 View all products for this Gene ID
- UniProt
- View information about NT-4 on UniProt.org
Related Pages & Pathways
Pathways
Related FAQs
- Why choose BioLegend recombinant proteins?
-
• 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?
-
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?
-
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?
-
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?
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Use formula Specific activity (Units/mg) = 10^6/ ED50 (ng/mL)
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