Confocal immunofluorescent analysis of normal mouse cerebellar peduncle, untreated (left) or treated with λ-phosphatase (right), using Phospho-Tau (Ser404) (D2Z4G) Rabbit mAb (Alexa Fluor® 488 Conjugate) (green). Sections were mounted in ProLong® Gold Antifade Reagent with DAPI #8961.
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This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct immunofluorescent analysis in mouse tissue. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-Tau (Ser404) (D2Z4G) Rabbit mAb #20194.
Supplied in PBS (pH 7.2), less than 0.1% sodium azide and 2 mg/ml BSA. Store at 4°C. Do not aliquot the antibody. Protect from light. Do not freeze.
NOTE: Prepare solutions with reverse osmosis deionized (RODI) or equivalent grade water.
Cover sections with 4% formaldehyde dilute in 1X PBS.
NOTE: Formaldehyde is toxic, use only in fume hood.
NOTE: All subsequent incubations should be carried out at room temperature unless otherwise noted in a humid light-tight box or covered dish/plate to prevent drying and fluorochrome fading.
posted November 2006
revised November 2013
Protocol Id: 222
Phospho-Tau (Ser404) (D2Z4G) Rabbit mAb (Alexa Fluor® 488 Conjugate) 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.
Human, Mouse, Rat
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser400/Thr403/Ser404 of human Tau protein.
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).
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