The hallmark of Alzheimer's disease (AD) pathology includes b-sheet aggregates of b-amyloid peptides in senile plaques and hyperphosphorylated Tau protein in neurofibrillary tangles (NFT).
Anaspec has brought out four new phosphospecific anti-Tau antibodies.
These antibodies have been validated in dot blots and IHC.
Tau is a collection of microtubule-associated proteins involved in microtubule assembly and stabilisation.
In an adult human brain, six isoforms, ranging between 352 and 441 amino acids in length, are produced as a result of alternative RNA splicing.
The expression of Tau isoforms is developmentally regulated, as only the smallest Tau polypeptide is expressed in the foetal brain.
Hyperphosphorylated Tau is the major component of the paired helical filament of Alzheimer's disease.
Anti-phospho-Tau antibodies are used to identify specific amino acids that are phosphorylated in Tau from normal brains and Alzheimer's-disease brains.
The Tau proteins, especially in developing brains and in Alzheimer brains, are phosphorylated in vivo at many different sites such as Thr181, Ser198, Ser199, Ser202, Thr205, Thr212, Ser214, Thr217, Thr231, Ser235, Ser262, Ser356, Ser396, Ser400, Ser404 and Ser413.
Rabbit anti-phospho-Tau antibodies were raised against synthetic phosphopeptides.
These antibodies were evaluated for specificity with Elisa and/or Western blot.
By Western blot, an immunoreactive band around 52kDa was observed in the mouse whole brain lysate.
Species reactivity includes human, mouse and rat.
Some antibodies have also shown reactivity with bovine, chicken and zebrafish.
