Tau is a heterogeneous microtubule-associated protein that promotes and stabilizes microtubule assembly, especially in axons. Six isoforms with different amino-terminal inserts and different numbers of tandem repeats near the carboxy-terminus have been identified, and tau is hyperphosphorylated at approximately 25 sites by ERK, GSK-3 and CDK5 (1-2). Phosphorylation decreases the ability of tau to bind to microtubules. Neurofibrillary tangles are a major hallmark of Alzheimer's disease and these tangles are bundles of paired helical filaments composed of hyperphosphorylated tau. In particular, phosphorylation of Ser396 by GSK-3 or CDK5 destabilizes microtubules in Alzheimer's disease. Furthermore, inclusions of tau are found in a number of other neurodegenerative diseases, collectively known as tauopathies (1, 3).1) Johnson, G. V. and Stoothoff, W. H. (2004) J. Cell Sci. 117, 5721-5729. Hanger, D. P. et al. (1998) J. Neurochem. 71, 2465-2476. Bramblett, G. T. et al. (1993) Neuron 10, 1089-1099. More
Tau (phospho-Ser416) antibody was raised against a peptide sequence around phosphorylation site of serine 416 (T-G-S (p) -I-D) derived from Rat Tau.
WB
Rat
Western blot analysis of extract from rat brain, rat hippocampus and mouse brain using Tau (phospho-Ser416).
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