Western blot analysis of tau and a-syn polymerization with all six major CNS isoforms of tau (T40, T39, T43, T44, T37, and T34) employed polyclonal rabbit 17026 (1:10,000) antibody to tau, and the mouse Syn 102 antibody to a-syn, which reacts equally with a-and b-syn, to detect these proteins.
For Immuno EM of tau and a-syn fibrils the following combinations of antibodies were used: mouse antibody to a-syn 505 (1:5000) and rabbit antibody to tau 17026; mouse antibody to a-syn 506 (1:5000) and rabbit 17026; rabbit antibody to a-syn SNL-4 and mouse antibody to tau Tau-1; mouse a-Syn 505 and rabbit 17026; rabbit SNL-4 (1:200) and mouse antibody to tau 24E12.
Brain sections from a transgenic mouse model of a-synucleinopathy that overexpresses human A53T a-syn were studied. These mice develop severe motor impairments that coincide with the formation of abundant a-syn inclusions. To examine whether a-syn and tau synergistically promote the fibrillization of each other, we examined bigenic mice that express both wild-type human a-syn and P301L mutant tau. In the single transgenic mouse lines, tauP301L (line 6) and human a-syn (line M2) expression was observed in oligodendrocytes.
IHC of a-syn and tau inclusions in a patient with A53T a-syn mutation antibodies used monoclonal antia-syn 303 and monoclonal anti-tau PHF1 (gift of Peter Davies).