AnaSpec Introduces Two (2) Anti-Tau Antibody (GlcNAc Ser400 & Ser400) & Five (5) Tau Peptides

AnaSpec is pleased to announce the recent release of two rabbit polyclonal antibodies. Anti-Tau antibody (GlcNAc Ser 400) recognizes the glycosylated [N-acetyl-D-glucosamine (GlcNAc)] Serine400 residue. This antibody was raised against a synthetic peptide derived from amino acids surrounding the Tau Ser400 sequence. As confirmed by Western and dot blots, this antibody only recognizes Tau glycosylated Ser400 and not the non-glycosylated Tau. Species reactivity includes human, monkey, mouse, rat, and other mammalian species. As well, Anti-Tau antibody (Ser 400) that recognizes long variants of Tau (1N4R, 2N3R, and 2N4R) in human, monkey, mouse, rat, and other mammalian species was also introduced. The specificity of this antibody was confirmed by Western blot. This antibody recognizes all Tau modifications including phosphorylation and glycosylation.

In addition to the new antibodies, five new Tau peptides were also released. These peptides, 29 to 32 amino acids long are from Inserts1, 2 (from N-terminus) or the Repeat domains (C-terminus) of Tau isoforms found in human brain.

Tau is a microtubule-associated protein that stabilizes and promotes microtubule assembly. In the human brain, it is present in six isoforms that are 352, 381, 383, 410, 412, and 441 amino acids in length (1-5). When Tau is hyperphosphorylated, it can detach and form paired helical filament (PHF) aggregates (2-5). PHFs were found in neurofibrillary tangles in Alzheimer’s disease (AD) patients. As such, hyperphosphorylation of Tau has been linked to AD. In addition to being modified with phosphate groups, Tau can also undergo glycosylation on the same regions where phosphorylation takes place (5). Discovery of this phenomenon has led to the hypothesis that glycosylation of Tau may help stabilize microtubule-Tau connection and prevent free Tau aggregation.