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BDNF proDomain Protein (WT-human)
Brain-Derived Neurotrophic Factor proDomain (WT-human), Recombinant, E. coli
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Storage | -20°C |
|---|---|
| Precautions | BDNF proDomain Protein (WT-human) is for research use only and not for use in diagnostic or therapeutic procedures. |
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Provided below are standard protocols that you may find useful for product applications.
Background
BDNF regulates neuronal survival, differentiation, and synaptic plasticity. It affects the release of excitatory neurotransmitters and has been found to affect cardiovascular development and function.1Like many other neurotrophins, BDNF is a cleavage product of the BDNF precursor proBDNF. This precursor may be cleaved by various proteases, intracellularly by furin and extracellularly by several proteases including prohormone convertases, plasminogen activator, MMP-3 and MMP-7 in vitro.2,3
Two different trans-membrane receptor proteins mediate BDNF and proBDNF signal transduction: the TrkB, and the pan-neurotrophic receptor p75NTR.4 ProBDNF has been demonstrated to induce TrkB phosphorylation in vitro and to bind p75NTR and sortilin to promote apoptosis.5,6
In many cases, the full prodomain region derived from the protein precursor has biological functions, for instance; the prodomain of the transforming growth factor β (TGFβ) affects the dimerization and folding as well as the activity of the mature proteins via non-covalent association. The propeptide of the bone morphogenetic proteins BMP-4 and BMP-7 regulates the diffusion and distribution of these growth factors within the extracellular matrix.7,8The prodomain region of the BDNF precursor plays an important role in regulating its intracellular trafficking to secretory pathways.9 However, the role of the full BDNF-prodomain, which is a product of proteolytic cleavage of proBDNF, is not clearly understood. Furthermore, binding competition studies suggest that binding sites for BDNF prodomain are located in the tunnel of the ten-bladed b-propeller domain of sortilin. 10
References
1 . Segal, R. (2001)Sci. STKE,2001, pe1.
2 . Hariri, A.R.et al.(2003)J. Neurosci.23, 6690.
3 . Fahnestock, M.et al. (2001) Mol. Cell. Neurosci., 18, 210.
4 . Dechant, G.et al.(1993)Development119,545
5 . Mowla, S.J.et al. (2001) J. Biol. Chem.276, 12660.
6 . Teng, H.K.et al. (2005). J. Neurosci.25, 5455.
7 . Gray, A. M. and Mason, A.J. (1990) Science.247, 1328
8 . Gregory, K. E.et al. (2005) J. Biol. Chem.280, 27970.
9 . Egan, M.et al. (2003) Cell,112, 257
10 . Quistgaard, E. M.et al.(2008)Nature Structural & Molecular Biology,16, 96.
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