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Pro-Nerve Growth Factor Human Recombinant ( ProNGF Human )
DescriptionPro NGF is the pro-form of the neurotrophin nerve growth factor. Like the mature protein pro NGF is characterized by the cysteine knot motif consisting of three cysteine bridges. The protein predominantly exists as a non-covalently linked
Data sheet
| Formulation | ProNGF was lyophilized from a 0.2 uM filtered solution of 20mM PB and 250mM NaCl pH 7.2. |
| Solubility | It is recommended to reconstitute the lyophilized ProNGF in 1xPBS to a concentration no less than 100 ug/ml, which can then be further diluted to other aqueous solutions. |
| Purity | Greater than 95.0% as determined by SDS-PAGE. |
| Description | Pro NGF is the pro-form of the neurotrophin nerve growth factor. Like the mature protein pro NGF is characterized by the cysteine knot motif consisting of three cysteine bridges. The protein predominantly exists as a non-covalently linked homodimer.Pro-Nerve Growth Factor Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 224 amino acids and having a molecular mass of 50KDa.The Pro NGF is purified by proprietary chromatographic techniques. |
| Expression host | Escherichia Coli. |
| Synonyms | Human Pro-NGF, ProNGF, NGFB. |
| Reagent Appearance | Sterile Filtered White lyophilized (freeze-dried) powder. |
| Stability | Lyophilized ProNGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ProNGF should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles. |
| Amino acid sequence | MEPHSESNVPAGHTIPQVHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNITVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRSSSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFETKCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTACVCVLSRKAVRRA. |
| References | Title: ProNGF inhibits NGF mediated TrkA activation in PC12 cells. Publication: Journal of neurochemistry 107.5 (2008): 1294-1303. Link: http://onlinelibrary.wiley.com/doi/10.1111/j.1471-4159.2008.05690.x/epdf |