This product is freeze dried. All water molecules have been removed.
Every lot is tried & tested in a relevant biological assay.
0.1 EU per 1 µg of the protein by the LAL method & lyophilized from a 0.2 µm filtered solution.
Tolkovsky, A. (1997) Trends Neurosci. 20, 1.
Jing, S. et al. (1992) Neuron 9, 1067.
Acheson, A. et al. (1995) Nature 374, 450.
Morse, J.K. et al. (1993) J. Neurosci. 13, 4146.
Hyman, C. et al. (1991) Nature 350, 230.
Friedman, B. et al. (1995) J. Neurosci. 15, 1044.
Meyer, M. et al. (1992) J. Cell Biol. 119, 45.
Koliatsos, V.E. et al. (1993) Neuron 10, 359.
Teng, H.K. et al. (2005) J. Neurosci. 25, 5455.
Woo, N.H. et al. (2005) Nat. Neurosci. 8, 1069.
Centrifuge all product preparations before use (10000 x g 5 min). Repeated freezing/thawing might result in loss of activity.
Western blot analysis of purified proteins:
Recombinant human proBDNF protein (#B-257), (lanes 1 and 4)
Recombinant human BDNF proDomain protein (#B-245), (lanes 2 and 5)
Recombinant human BDNF protein (#B-250), (lanes 3 and 6)1-3. Guinea pig Anti-proBDNF Antibody (#AGP-032), (1:280)
4-6. Guinea pig Anti-BDNF Antibody (#AGP-021), (1:280)
proBDNF is recognized both by Anti-proBDNF and Anti-BDNF antibodies as a monomer at ~ 26 kDa.
BDNF proDomain is recognized by Anti-proBDNF, but not by Anti-BDNF antibody, at ~ 12.4 kDa.
BDNF is recognized by Anti-BDNF, but not by Anti-proBDNF antibody, as a monomer at ~ 13.5 kDa.
- Segal, R. (2001) Sci. STKE. 2001, pe1.
- Hariri, A.R. et al. (2003) J. Neurosci. 23, 6690.
- Fahnestock, M. et al. (2001) Mol. Cell. Neurosci. 18, 210.
- Dechant, G. et al. (1993) Development 119, 545.
- Mowla, S.J. et al. (2001) J. Biol. Chem. 276, 12660.
- Teng, H.K. et al. (2005) J. Neurosci. 25, 5455.
- Gray, A.M. and Mason, A.J. (1990) Science 247, 1328.
- Gregory, K.E. et al. (2005) J. Biol. Chem. 280, 27970.
- Egan, M. et al. (2003) Cell 112, 257.
- Quistgaard, E.M. et al. (2008) Nat. Struct. Mol. Biol. 16, 96.
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.1 Like 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.7,8 The 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
Recombinant human BDNF proDomain protein (#B-245) is a highly pure, recombinant, and biologically active protein.