Render Target: STATIC
Render Timestamp: 2024-10-14T09:51:48.284Z
Commit: 56767fe525c928647c8401233a175d0d607d385d
XML generation date: 2024-09-30 01:58:48.374
Product last modified at: 2024-10-11T20:45:07.642Z
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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 (Thr217) (E9Y4S) Rabbit mAb #51625

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 50-80
    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
    Simple Western™ 1:10 - 1:50
    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 (Thr217) (E9Y4S) Rabbit mAb recognizes endogenous levels of tau protein only when phosphorylated at Thr217 and Ser214/Thr217. This antibody does not detect phosphorylation at Ser214 alone.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr217 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).

    Tau phosphorylation at Thr217 has been identified as a highly specific biomarker of AD. Phosphorylated tau at Thr217 can be detected in cerebrospinal fluid in both preclinical and advanced stages of AD and has been shown to successfully differentiate between AD and non-AD neurodegenerative diseases (4,5).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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