Render Target: STATIC
Render Timestamp: 2024-12-20T11:21:18.560Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-10-16 18:03:08.219
Product last modified at: 2024-12-17T18:50:14.723Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Phospho-Tau (Thr231/Ser235) (E7G5W) Rabbit mAb #20473

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 55-80
    Source/Isotype Rabbit IgG
    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, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-Tau (Thr231/Ser235) (E7G5W) Rabbit mAb recognizes endogenous levels of tau protein only when phosphorylated at Thr231 and Thr231/Ser235. This antibody does not detect phosphorylation at Ser235 alone.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr231 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).

    It has been shown that phosphorylation of tau at Thr231/Ser235 is elevated in AD brain and human tau-transgenic mouse models of AD, where it may be involved in increasing tau seeding efficiency (4,5). Tau phosphorylation at Thr231 can be detected in cerebrospinal fluid and plasma and shows potential as a biomarker of neurofibrillary pathology in AD (6,7).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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