This antibody is raised against the corresponding amino-acid sequence of Tau proteins translated from exon 3. This sequence is the second amino-terminal insert. Such epitope is expressed in two of the six adult Tau isoforms and is developmentally regulated [1].
Source:
A New Zealand rabbit was immunized sub-cutaneously with a KLH coupled peptide (Neosystem, France).
Applications:
This antibody can be used for both immunohistochemistry and western blotting .
Specificity:
This antibody recognizes the second amino-terminal insert of normal Tau proteins.
1. Using western blotting, it detects the two recombinant Tau isoforms containing this insert [1]. In brain cortical homogenates from AD patients, this antibody recognizes the 69 and 74 kDa components of PHF-Tau proteins [2-4].
2. Using immunohistochemistry, this antibody reacted with PHF-Tau and revealed neurofibrillary tangles and neuritic plaques on frozen sections of cortical brain tissue.
Presentation:
This rabbit polyclonal antibody to human Tau proteins is in 50% glycerol. There is no other additive or preservative products. This antibody has not been purified by protein A chromatography. It is a total serum.
Instruction for use:
1. For Western-blot, a final dilution of 1/1000 in TBS-Tween buffer is suggested to detect Tau proteins from cortical brain homogenates (as described elsewhere [3]).
2. For immunohistochemistry, a final dilution of 1/200 is suggested for immunostaining on frozen sections of cortical brain tissue.
Note: The recommended dilutions are approximative values. For each application, a dose response assay should be performed to determine the optimal concentration.
FOR RESEARCH USE ONLY
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References:
[1] Goedert M. and Jakes R., EMBO J. 1990, 9, 4225-4230.
[2] Delacourte A et al., J Neuropathol Exp Neurol, 1996, 55, 159-168.
[3] Buée-Scherrer V et al. , Am J Pathol, 1995, 146, 924-932.
[4] Sergeant N, David JP, Lefranc D, Vermersch P, Wattez A, Delacourte A
FEBS Lett 1997 Aug 4;412(3):578-582
Different distribution of phosphorylated tau protein isoforms in Alzheimer's and Pick's diseases.
Tau proteins aggregate into different neuronal inclusions in several neurodegenerative disorders. In Alzheimer's disease (AD), hyperphosphorylated Tau from paired helical filaments (PHF) of neurofibrillary tangles, named PHF-Tau, have an electrophoretic profile with four main bands (Tau 55, 64, 69, 74 kDa). In Pick's disease, phosphorylated Tau from Pick bodies are made of two major components (Tau 55, 64 kDa) and a minor 69 kDa. Here we show, using specific antibodies against translated exon 2, 3 or 10 of Tau isoforms, that the set of Tau isoforms engaged in the most insoluble part of PHF in AD is made of Tau isoforms with exon 10 while they are lacking in phosphorylated Tau from Pick's disease. Our results suggest that specific sets of Tau isoforms distinguish between typical neuronal inclusions.
PMID: 9276470, UI: 97420485
