Cell Signaling Technology

Product Pathways - Neuroscience

Phospho-Tau (Ser400/Thr403/Ser404) Antibody #11837

Applications Reactivity Sensitivity MW (kDa) Source
W H M R Endogenous 50-80 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Phospho-Tau (Ser400/Thr403/Ser404) Antibody recognizes endogenous levels of tau protein when phosphorylated at Ser400 or Thr403 or Ser404. This antibody also detects dual phosphorylation at Ser400/Thr403, Ser400/Ser404, or Thr403/Ser404, and triple phosphorylation at Ser400/Thr403/Ser404.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser400/Thr403/Ser404 of human tau protein. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from adult and neonatal mouse brain using Phospho-Tau (Ser400/Thr403/Ser404) Antibody. The phospho-specificity of the antibody was verified by blocking with a Ser400/Thr403/Ser404 phosphopeptide (middle panel) or a nonphosphopeptide (right panel).

Background

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; these tangles are bundles of paired helical filaments composed of hyperphosphorylated tau. In particular, phosphorylation at Ser396 by GSK-3 or CDK5 destabilizes microtubules. Furthermore, research studies have shown that inclusions of tau are found in a number of other neurodegenerative diseases, collectively known as tauopathies (1,3).

Investigators have shown that tau phosphorylation at Ser404 destabilizes microtubules and that tau is hyperphosphorylated at Ser404 in Alzheimer's disease (4-7).

  1. Johnson , G.V. and Stoothoff , W.H. (2004) J. Cell Sci. 117, 5721-5729.
  2. Hanger, D. P. et al. (1998) J. Neurochem. 71, 2465-2476.
  3. Bramblett, G. T. et al. (1993) Neuron 10, 1089-1099.
  4. Shiurba, R.A. et al. (1996) Brain Res 737, 119-32.
  5. Hanger, D.P. et al. (1998) J Neurochem 71, 2465-76.
  6. Evans, D.B. et al. (2000) J Biol Chem 275, 24977-83.
  7. Bertrand, J. et al. (2010) Neuroscience 168, 323-34.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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