Nerve Growth Factor 2.5S
Purified Mouse Nerve Growth Factor 2.5S has been used to demonstrate the importance of NGF in regulation of neuronal function through the up-regulation of the transcription factor NFAT (Nuclear Factor of Activated T-cells) via activation of the PI3K/Akt pathway (Kim et al. 2014).
- Target Species
- Species Cross-Reactivity
Target Species Cross Reactivity Rat
- N.B. Antibody reactivity and working conditions may vary between species.
- Product Form
- Purified natural murine nerve growth factor - lyophilized
- Reconstitute with 1.0 ml distilled water. Care should be taken during reconstitution as the protein may appear as a film at the bottom of the vial. Bio-Rad recommend that the vial is gently mixed after reconstitution.
- Murine nerve growth factor is prepared from the submaxillary glands of mice by sephadex and subsequent cellulose chromatography (Bocchini and Angeletti 1969).
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
- None present
- >98% by SDS PAGE
- Approx. Protein Concentrations
- Protein Molecular Weight
- Approximately 30 kDa
- Prior to reconstitution store at +4oC. Following reconstitution store at -20oC.
This product should be stored undiluted.
Storage in frost-free freezers is not recommended. Avoid repeated freezing and thawing as this may denature the protein. Should this product contain a precipitate we recommend microcentrifugation before use.
- 3 months from date of reconstitution
- Entrez Gene
- GO Terms
- GO:0005057 receptor signaling protein activity
- GO:0005788 endoplasmic reticulum lumen
- GO:0007422 peripheral nervous system development
- GO:0008083 growth factor activity
- GO:0019233 sensory perception of pain
- GO:0043524 negative regulation of neuron apoptosis
- GO:0045773 positive regulation of axon extension
- GO:0046928 regulation of neurotransmitter secretion
- For research purposes only
Applications of Nerve Growth Factor 2.5S
|Application Name||Verified||Min Dilution||Max Dilution|
Product Specific References
References for Nerve Growth Factor 2.5S
Rohn, T.A. et al. (2011) A Virus-Like Particle-Based Anti-Nerve Growth Factor Vaccine Reduces Inflammatory Hyperalgesia: Potential Long-Term Therapy for Chronic Pain.
J Immunol. 186: 1769-80.
Laursen, L.S. et al. (2011) Translation of myelin basic protein mRNA in oligodendrocytes is regulated by integrin activation and hnRNP-K.
J Cell Biol. 192: 797-811.
Colbert, R.A. et al. (1994) Vasoactive intestinal peptide stimulates neuropeptide Y gene expression and causes neurite extension in PC12 cells through independent mechanisms.
J Neurosci. 14: 7141-7.
Smith-Thomas, L.C. et al. (1995) Increased axon regeneration in astrocytes grown in the presence of proteoglycan synthesis inhibitors.
J Cell Sci. 108: 1307-15.
Barrie, A.P. et al. (1997) Pituitary adenylyl cyclase-activating peptide stimulates extracellular signal-regulated kinase 1 or 2 (ERK1/2) activity in a Ras-independent, mitogen-activated protein Kinase/ERK kinase 1 or 2-dependent manner in PC12 cells.
J Biol Chem. 272: 19666-71.
Liu, N. et al. (2005) Enhancement of Schwann cell myelin formation by K252a in the Trembler-J mouse dorsal root ganglion explant culture.
J Neurosci Res. 79: 310-7.
Eibl, J.K. et al. (2010) Multipotent neurotrophin antagonist targets brain-derived neurotrophic factor and nerve growth factor.
J Pharmacol Exp Ther. 332: 446-54.
Vogelezang, M. et al. (2007) Neurite outgrowth on a fibronectin isoform expressed during peripheral nerve regeneration is mediated by the interaction of paxillin with alpha4beta1 integrins.
BMC Neurosci. 8: 44.
Seiberlich, V. et al. (2015) Downregulation of the microtubule associated protein Tau impairs process outgrowth and myelin basic protein mRNA transport in oligodendrocytes.
Glia. 63 (9): 1621-35.
von Büdingen, H.C. et al. (2015) The myelin oligodendrocyte glycoprotein directly binds nerve growth factor to modulate central axon circuitry.
J Cell Biol. 210 (6): 891-8.
Miyamoto, Y. et al. (2015) Involvement of the Tyro3 receptor and its intracellular partner Fyn signaling in Schwann cell myelination.
Mol Biol Cell. 26 (19): 3489-503.
Bocchini V & Angeletti PU (1969) The nerve growth factor: purification as a 30,000-molecular-weight protein.
Proc Natl Acad Sci U S A. 64 (2): 787-94.