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Phospho-Tau (Ser202/Thr205) (E6S2W) Rabbit mAb #30505
Filter:
- WB
Western blot analysis of extracts from mouse brain, Tau KO (-/-) mouse brain, and mouse liver, untreated (-) or λ phosphatase-treated (+), using Phospho-Tau (Ser202/Thr205) (E6S2W) Rabbit mAb (upper), Tau (D1M9X) XP® Rabbit mAb #46687 (middle), and α-Actinin (D6F6) XP® Rabbit mAb #6487 (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) | 55-80 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Related Products
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
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.
Protocol
Specificity / Sensitivity
Phospho-Tau (Ser202/Thr205) (E6S2W) Rabbit mAb recognizes endogenous levels of tau protein only when both sites are phosphorylated at Ser202 and Thr205. The antibody does not detetct single phosphorylation at Ser202 or Thr205. Human reactivity was done using the Tau Tg2508 mouse model.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser202 and Thr205 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).
A number of kinases have been shown to phosphorylate tau at Ser202 and Thr205 (aka AT8) including GSK-3β and CDK5. Tau is known to form paired helical filaments when phosphorylated at these residues (4).
A number of kinases have been shown to phosphorylate tau at Ser202 and Thr205 (aka AT8) including GSK-3β and CDK5. Tau is known to form paired helical filaments when phosphorylated at these residues (4).
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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