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Phospho-Tau (Ser404) (D2Z4G) Rabbit mAb #35834
Filter:
- WB
- IHC
Western blot analysis of normal mouse brain and Tau KO (-/-) mouse brain with Phospho-Tau (Ser404) (D2Z4G) Rabbit mAb (upper) and β-Actin (D6A8) Rabbit mAb #8457 (lower). Tau-KO mouse brain tissue was kindly provided by Dr. Dominic Walsh at Brigham and Women's Hospital and Harvard Medical School.
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 50-80 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Related Products
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunohistochemistry (Paraffin) | 1:400 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
For a carrier-free (BSA and azide free) version of this product see product #49562.
For a carrier-free (BSA and azide free) version of this product see product #49562.
Protocol
Specificity / Sensitivity
Phospho-Tau (Ser404) (D2Z4G) Rabbit mAb recognizes endogenous levels of tau protein when phosphorylated at Ser404. This antibody detects single phosphorylation at Ser404, dual phosphorylation at Ser400/Ser404 or Thr403/Ser404, and triple phosphorylation at Ser400/Thr403/Ser404. This antibody does not detect peptides with single phosphorylation at Ser400 or Thr403, and dual phosphorylation at Ser400/Thr403.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser400/Thr403/Ser404 of human tau protein.
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, glycogen synthase kinase-3 (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 (AD); these tangles are bundles of paired helical filaments (PHFs) 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 (2,4-6).
Investigators have shown that tau phosphorylation at Ser404 destabilizes microtubules and that tau is hyperphosphorylated at Ser404 in Alzheimer's disease (2,4-6).
- Johnson, G.V. and Stoothoff, W.H. (2004) J Cell Sci 117, 5721-9.
- Hanger, D.P. et al. (1998) J Neurochem 71, 2465-76.
- Bramblett, G.T. et al. (1993) Neuron 10, 1089-99.
- Shiurba, R.A. et al. (1996) Brain Res 737, 119-32.
- Evans, D.B. et al. (2000) J Biol Chem 275, 24977-83.
- Bertrand, J. et al. (2010) Neuroscience 168, 323-34.
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