Anaspec has brought out four more phosphospecific anti-Tau antibodies, meaning the company now has 17 phosphospecific and nine non-phosphospecific anti-Tau antibodies.
Anaspec has produced an anti-Tau to phosphoserine at position 235 (catalogue no.
55315) clearly delineated from one at phosphoserine position 238 (catalogue no.
55323).
Anaspec's phosphospecific antibodies do not cross-react with each other.
Tau is a collection of microtubule-associated proteins involved in microtubule assembly and stabilisation.
In an adult human brain, six isoforms, 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 phosphorylated in Tau from normal brains and Alzheimer's brains.
The Tau proteins 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.