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AnaSpec Introduces Expanded Selection of Anti-Tau Antibodies
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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 announced the release of 4 additional new phosphospecific anti-Tau antibodies.
Tau is a collection of microtubule-associated proteins that is involved in microtubule assembly and stabilization.3 In adult human brain, 6 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 fetal 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 52 kDa 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.
Tau is a collection of microtubule-associated proteins that is involved in microtubule assembly and stabilization.3 In adult human brain, 6 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 fetal 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 52 kDa 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.
