Supplementary Table S1: Antibodies
Antibody
Specificity
Source
Dilution
References
Mouse-anti-
Amino acid sequence
Dakocytomation (Hamburg,
1:2001
S2
Aβ8-17
8-17 of Aβ
Germany)
Rabbit-anti-
Amino acid sequence
Synaptic Systems
1:2002
S3
Aβx-38-40-42-43
13-29 of Aβ
(Göttingen, Germany)
Monoclonal
Pyroglutamyl residue
Synaptic Systems
1:5001
S3
mouse-anti-
at position 3 of Aβ
(Göttingen, Germany)
Digoxigenyla
Pyroglutamyl desidue
Synaptic Systems
1:1002
(27)
-ted-anti-
at position 3 of Aβ
designation
(clone 6F3D)
pE3Aβ
(clone 2-48)
(20 µg/ml)
pE3Aβ
1:10001
S4
Thermo Scientific
1:1002
S5
1:10001
S6
1:20001
S7
1:5001
S8
Monoclonal
Phosphorylated serine
Thermo Scientific (Bonn,
mouse-anti-
202 and threonine 205
Germany)
AT8
of human tau
Biotinylated
Phosphorylated serine
AT8
202 and threonine 205
of human tau
Rabbit-anti-
Phosphorylated
Invitrogen (Karlsruhe,
pT205
threonine 205 of
Germany)
human tau
Rabbit-anti-
Phosphorylated serine
Christian Czech (Hoffmann-
pS422
422 of human tau
La-Roche, Basel,
Switzerland)
Monoclonal
Conformation-
mouse-anti-
dependent threonine
AT100
212 and serine 214 of
Thermo Scientific
human tau
Dr. Peter Davies (New York)
1:5001
S9
Dr. Peter Davies (New York)
1:4001
S10
Ionized calcium-
Wako Chemicals (Neuss,
1:10001
S11
binding adapter
DE)
1:4002
Monoclonal
Phosphorylated serine
mouse-anti-
396 and 404 of human
PHF-1
tau
Monoclonal
Aberrantly folded,
mouse-anti-
conformationally
MC-1
changed human tau
Rabbit-antiIba-1
1:2003
molecule 1
Guinea pig-
Recombinant human
anti-GFAP
GFAP
Synaptic Systems
1:2003
S12
1dilution
for avidin/biotinyl-peroxidase method with nickel-enhanced DAB as chromogen.
2dilution
for Cy3-immunolabelling.
3dilution
for Cy2- or Cy5-immunolabelling.
Supplemental References
S2.
Czasch S, Paul S, Baumgärtner W. A comparison of immunohistochemical
and silver staining methods for the detection of diffuse plaques in the aged
canine brain. Neurobiol Aging 2006;27:293--305
S3.
Hartlage-Rübsamen M, Morawski M, Waniek A, et al. Glutaminyl cyclase
contributes to the formation of focal and diffuse pyroglutamate (pGlu)-Aβ
deposits in hippocampus via distinct cellular mechanisms. Acta Neuropathol
2011;121:705--19
S4.
Goedert M, Jakes R, Vanmechelen E. Monoclonal antibody AT8 recognises
tau protein phosphorylated at both serine 202 and threonine 205. Neurosci
Lett 1995;189:167--9
S5.
Härtig W, Lehmann J, Stieler J, et al. Simultaneous detection of tau
phospho-epitopes with haptenylated antibodies. Neuroreport. 2006; 17:869-74
S6.
Yu Y, Run X, Liang Z, et al. Developmental regulation of tau
phosphorylation, tau kinases, and tau phosphatases. J Neurochem
2009;108:1480--94
S7.
Grueninger F, Bohrmann B, Czech C, et al. Phosphorylation of Tau at S422
is enhanced by Abeta in TauPS2APP triple transgenic mice. Neurobiol Dis
2010;37:294--306
S8.
Yoshida H, Goedert M. Sequential phosphorylation of tau protein by cAMPdependent protein kinase and SAPK4/p38delta or JNK2 in the presence of
heparin generates the AT100 epitope. J Neurochem 2006;99:154--64
S9.
Greenberg SG, Davies P, Schein JD, et al. Hydrofluoric acid-treated tau
PHF proteins display the same biochemical properties as normal tau. J Biol
Chem 1992;267:564--9
S10. Jicha GA, Bowser R, Kazam IG, et al. Alz-50 and MC-1, a new monoclonal
antibody raised to paired helical filaments, recognize conformational
epitopes on recombinant tau. J Neurosci Res 1997;48:128--32
S11. Imai Y, Ibata I, Ito D, et al. A novel gene iba1 in the major histocompatibility
complex class III region encoding an EF hand protein expressed in a
monocytic lineage. Biochem Biophys Res Commun 1996;224:855--62
S12. Michalski D, Heindl M, Kacza J, et al. Spatio-temporal course of
macrophage-like cell accumulation after experimental embolic stroke
depending on treatment with tissue plasminogen activator and its
combination with hyperbaric oxygenation. Eur J Histochem. 2012;56:e14