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Amino Acid Sequence: YAEHKSHRGEYSVCDSESLWVTDKSSAIDIRGHQVTVLGEIKTGNSPVKQYFYETRCKEARPVKNGCRGIDDKHWNSQCKTSQTYVRALTSENNKLVGWRWIRIDTSCVCALSRKIGRT
Background: NT-3 is found in neurons of the central nervous system. NT-3 is expressed also in muscles and its expression is down-regulated in denervated muscles. Many human gliomas express and secrete NT-3 into the conditioned medium. Some protein domains of NT-3 are identical with those of NGF and BDNF. NT-3 selectively supports the survival of neuronal cell populations, and prevents the death of cultured embryonic rat spinal motor neurons at picomolar concentrations. NT-3 has been shown to enhance sprouting of corticospinal tract during development and after adult spinal cord lesion. The activities of NT-3 and BDNF are additive in some systems. The biological activities of NT- 3 are mediated by a receptor belonging to the trk family of receptors with intrinsic tyrosine-specific protein kinase activity. NT-3 only binds weakly to the trk receptor which is a high-affinity receptor for NGF.
Biological Activity: The ED50 was determined by the dose-dependent induction of choline acetyl transferase activity in rat basal forebrain primary septal cell cultures was found to be in the range of 10-50 ng/ml.
Description: Recombinant NT-3 is a disulfide-linked homodimer protein consisting of two 120 amino acid residue subunits, and migrates as an approximately 27 kDa protein under non-reducing and as 14 kDa under reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human Neurotrophin-3 mature chain was expressed in E. coli.
Endotoxin Level: <0.1 ng/µg (1 EU/µg), using the LAL gel clot method.
Format: lyophilized protein
Formulation: Lyophilized from a 0.2 µm filtered PBS solution, pH 7.5.
Genbank: P20783
Purity: ≥97% by SDS-PAGE and HPLC
Reconstitution: Reconstitute at 0.1-1.0 mg/ml in distilled water. This solution can then be diluted into other buffers. To maximize product collection from vial surface, vortex briefly and then spin down to recollect the liquid.
Storage Stability: The lyophilized protein is stable for at least 2 years from date of receipt when stored at -20°C. Upon reconstitution, store in working aliquots at +4°C for up to one month, or at -20°C for up to six months, in the presence of a carrier protein. Avoid repeated freeze/thaw cycles.
Uniprot: P20783
Warnings: Avoid freeze/thaw cycles.
Biosafety Level: Not applicable (BSL-1)
References: 1. J. Immunol., Apr 2009, 182: 4705 - 4712.
2. J. Neurosci., Jan 2009, 29: 575 - 587.
3. J. Cell Biol., Dec 2006, 175: 1029 - 1042.
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