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Neurotrophins are growth factors that modulate growth, differentiation, and survival of neurons. These structurally related proteins include neuron growth factor (NGF/β-NGF), brain derived neurogenic factor (BDNF), neurotrophin-3, and neurotrophin-4/5. They are highly homologous and share a similar structure of a tertiary folded, cysteine rich "knot". Neurotrophins are critical to the development of the central and peripheral nervous systems, and they play important roles in injury-induced neuron regeneration. β-NGF is a member of the neurotrophin family which controls growth, survival, and maturation of neurons. In peripheral and central neurons, neurotrophins are important regulators for survival, differentiation, and maintenance of nerve cells. They are detectable throughout embryogenesis and into the adult stage in the central and peripheral nervous systems. In animal models, β-NGF prevents neuronal degeneration and has become a therapeutical target in neuron regeneration studies. β-NGF is also critical for the survival and maintenance of sympathetic and sensory neurons. It is the main neurotrophin that maintains homeostasis of neurogenesis. It prevents neurons from undergoing apoptosis and promotes maturation while supporting axonal branching. Two receptors are known to interact with NGF, p75NTR and TrkA. The NGF-TrkA signaling pathway induces two pathways through activation of PI3K-Akt or Ras-MAPK. Either one of the pathways leads to CREB phosphorylation and increases expression of anti-apoptosis genes to keep neurons alive. Animal models of neurodegenerative diseases suggest that NGF can promote myelin repair of neurons in the peripheral nervous system. Clinical studies indicate that dysregulation of NGF signaling is related to Alzheimer's disease.Product Details
- Human β-NGF, amino acids (Ser122 — Ala241) (Accession# NM_002506.2) was expressed in E. coli.
- Molecular Mass
- The 120 amino acid recombinant protein has a predicted molecular mass of approximately 13.4 kD. The predicted N-terminal amino acid is Ser.
- >98% as determined by Coomassie stained SDS-PAGE.
- Lyophilized, carrier-free.
- Endotoxin Level
- Less than 0.1 ng per µg of protein (<1.0 EU/µg), as determined by the LAL method.
- 10 and 25 µg sizes are bottled at 200 µg/mL. 100 µg size and larger sizes are lot-specific and bottled at the concentration indicated on the vial (please contact technical support for concentration, or use our Lookup tool if you have a lot number.) Please note, new lots of the 100 µg size will be lot-specific and may differ from previous lots that had a fixed concentration.
- Storage & Handling
- Unopened vial can be stored at -20°C or -70°C for twelve months. 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, such as 5% Trehalose, and store in working aliquots at -20°C to -70°C for three months. Avoid repeated freeze/thaw cycles.
- Human β-NGF induces the proliferation of TF-1 cells. The ED50 ≤ 1.0 ng/ml.
- Recommended Usage
- Hypothalamus, pituitary, thyroid gland, testes, epididymis, vascular smooth muscle cells, fibroblasts, myofibroblasts, mast cells, eosinophils.
- β-NGF is important for maintaining neuron homeostasis.
- Neurons, astrocytes, eosinophils, B, T, and mast cells.
- Ligand Receptor
- Low-affinity NGF receptor (p75NTR); high-affinity NGF receptor (TrkA).
- Human β-NGF induces the proliferation of TF-1 cells.
- Biology Area
- Cell Biology, Neuroscience, Synaptic Biology
- Molecular Family
- Growth Factors, Cytokines/Chemokines
- Antigen References
1. Ullrich A, et al. 1983. Nature. 303:821.
2. Klein R, et al. 1991. Cell. 65:189.
3. Welker P, et al. 2000. Immunology 99:418.
4. Fahnestock M, et al. 2004. Prog. Brain Res. 146:101.
5. Bruno MA. Cuello AC. 2006. Proc. Natl. Acad. Sci. USA 103:6735.
6. Aloe L, et al. 2015. Curr. Neuropharmacol. 13:294.
- Gene ID
- 4803 View all products for this Gene ID
- View information about beta-NGF on UniProt.org
- Does specific activity of a recombinant protein vary between lots?
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.
- 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.
- 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)
- 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.