Tau is a family of six isoforms, derived from a single gene by alternative mRNA splicing1. They vary in size from 352 to 441 amino acids (36.8 to 45.9 kDa), and differ from one another in having three or four microtubule binding repeats (R) of 31-32 amino acids each, and two, one or none amino terminal inserts (N) of 29 amino acids each2.
Tau promotes the assembly and maintains the structure of microtubules in neuronal cells3,4,5. While the fetal brain contains a single isoform of tau (Tau-352) the adult brain has several isoforms. Tau is both phosphorylated and O-GlcNAcylated6. The normal brain tau contains 2-3 moles of phosphate/mole of the protein. In Alzheimer disease tau is hyperphosphorylated, containing 3-4-fold more phosphate/mole of the protein than the normal tau7,8 and is the major protein subunit of paired helical filaments (PHF) that form the neurofibrillary tangles (NFT). NFT accumulation correlates with the clinical progression of Alzheimer’s disease. Tau-1A6 (TA-1002; Patent Pending) is a proprietary rPeptide Tau Monoclonal Antibody that binds all 6 Tau isoforms.
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- Goedert, M., et. al. 1989, Neuron. 3, 519.
- Avila J. et. al., 2004, Physiol Rev. 84, 361.
- Goedert, M., 1993, Trends Neurosci. 16, 460.
- Mandelkow, E. et al. 1996, Ann N Y Acad Sci. 777, 96.
- Liu, F., et. al., 2004, Proc. Natl. Acad. Sci. U.S.A. 101, 10804.
- Iqbal, K., et. al., 1986, Lancet 2, 421.
- Kopke, et. al., 1993, J. Biol. Chem. 268, 2437
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