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Product last modified at: 2024-09-13T07:01:21.354Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-Tau (Thr181) Antibody #5383

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Filter:
  • WB
  • IP
Western Blotting Image 1: Phospho-Tau (Thr181) Antibody
Western blot analysis of extracts from mouse and rat brain using Tau (Tau46) Mouse mAb #4019 (red) and Phospho-Tau (Thr181) Antibody (green). The phospho-specificity of Phospho-Tau (Thr181) Antibody was verified by peptide blocking using a phosphopeptide or non-phosphopeptide. Western blot image was obtained using the Odyssey® Infrared Imaging System (LI-COR® Biotechnology).
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Inquiry Info. # 5383

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Supporting Data

REACTIVITY H M R
SENSITIVITY Endogenous
MW (kDa) 50-80
SOURCE Rabbit
Application Key:
  • WB-Western Blotting 
  • IP-Immunoprecipitation 
Species Cross-Reactivity Key:
  • H-Human 
  • M-Mouse 
  • R-Rat 

Product Information

Product Usage Information

Application Dilution
Western Blotting 1:1000
Immunoprecipitation 1:50

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

Protocol

Specificity / Sensitivity

Phospho-Tau (Thr181) Antibody recognizes endogenous levels of Tau protein only when phosphorylated at Thr181.

Species Reactivity:

Human, Mouse, Rat

The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

Species predicted to react based on 100% sequence homology:

Monkey

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr181 of human Tau protein. Antibodies are purified by protein A and peptide affinity chromatography.

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).

The cerebrospinal fluid concentration of Tau phosphorylated at Thr181 has been proposed to be a biomarker for the study of neurodegenerative disorders (4).
For Research Use Only. Not For Use In Diagnostic Procedures.
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