Amyloid Precursor Protein α (444-612), Secreted human 

Expressed as a soluble protein and purified under non-denaturing conditions.

Solution in phosphate buffered saline, pH 7.4, 0.2 μm filtered.

This fragment enables study of biological effects without the interference of the sAPPα N-terminal cysteine rich domain and the RERMS peptide domain activities (e.g. activation of pro-inflammatory effects of microglial cells, binding to heparan sulfate proteoglycan, binding ApoE proteins and inducing fibroblast proliferation, and neurite outgrowth in neuroblastoma cells).

Secreted amyloid precursor protein α (sAPPα) is a 612 amino acid protein produced from the ubiquitously expressed β-Amyloid precursor protein (βAPP), 695 isoform, by α-secretase cleavage. The sAPPα (444-612) fragment was designed to contain a sequence that is linked to the attenuation of glutamate exocitotoxicity and to the promotion of neurite outgrowth. In addition, it contains the C-terminal domain corresponding to sAPPα (597-612) that acts as a heparin-binding domain.

expressed in Escherichia coli (N-terminal histidine tagged)

>90% (SDS-PAGE)

buffered aqueous solution

apparent mol wt 33 kDa by SDS-PAGE

human ... APP(351)

dry ice

−70°C

Selkoe, D.J. Annu. Rev. Cell Biol. 10, 373, (1994)

Jin, L-W., et al. J. Neurosci. 14, 5461, (1994)

Mattson, M.P. J. Neurobiol. 25, 439, (1994)

Greenfield, J.P. Front. Biosci. 5, (2000)

Mattson, M.P. Physiol. Rev. 77, 1081, (1997)

Small, D.H., et al. J. Neurosci. 14, 2117, (1994)

Barger, S.W., Harmon, A.D. Nature 388, 878, (1997)

3