Render Target: STATIC
Render Timestamp:
4/1/2025, 6:01:11 AM EDT
4/1/2025, 10:01:11 AM UTC
Commit: 461ca8d8fe5b1efd4c01fc87e5b5eb592e2d154a
XML generation date: 2025-03-25 22:05:21.738
Product last modified at: 2025-03-27T08:00:10.782Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
  1. Products /
  2. Primary Antibodies /
  3. Phospho-Tau (Thr212/Ser214) (F2A4N) Rabbit mAb
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Phospho-Tau (Thr212/Ser214) (F2A4N) Rabbit mAb #16075

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 50-80
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    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 (Thr212/Ser214) (F2A4N) Rabbit mAb recognizes endogenous levels of tau protein only when phosphorylated at Thr212/Ser214. This antibody does not detect phosphorylation at Thr212 or Ser214 alone.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr212/Ser214 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 is phosphorylated at Thr212 by the kinases DYRK1A, AKT, and GSK3β (4-7). Numerous kinases, including PKA, CDK5, GSK3β, and SGK1, have been shown to phosphorylate tau at Ser214 (8-12). Phosphorylation of these sites occurs in AD and dementia with Lewy bodies (13,14). Investigators have shown that tau phosphorylation at Ser214 detaches tau protein from microtubules, protecting it against aggregation into Alzheimer PHFs (15). However, dual phosphorylation at Thr212 and Ser214 promotes tau aggregation and PHF formation (5,13).
    1. Johnson, G.V. and Stoothoff, W.H. (2004) J Cell Sci 117, 5721-9.
    2. Hanger, D.P. et al. (1998) J Neurochem 71, 2465-76.
    3. Bramblett, G.T. et al. (1993) Neuron 10, 1089-99.
    4. Di, J. et al. (2016) Sci Rep 6, 20833.
    5. Ksiezak-Reding, H. et al. (2003) Biochim Biophys Acta 1639, 159-68.
    6. Götz, J. et al. (2010) Biochim Biophys Acta 1802, 860-71.
    7. Miao, J. et al. (2019) Front Aging Neurosci 11, 34.
    8. Illenberger, S. et al. (1998) Mol Biol Cell 9, 1495-512.
    9. Götz, J. et al. (2001) Science 293, 1491-5.
    10. Yang, Y.C. et al. (2006) Mol Cell Biol 26, 8357-70.
    11. Liu, F. et al. (2006) FEBS Lett 580, 6269-74.
    12. Zhu, B. et al. (2010) Am J Physiol Lung Cell Mol Physiol 299, L493-501.
    13. Zheng-Fischhöfer, Q. et al. (1998) Eur J Biochem 252, 542-52.
    14. Duka, V. et al. (2013) PLoS One 8, e75025.
    15. Schneider, A. et al. (1999) Biochemistry 38, 3549-58.

    Database Links

    UniProt ID: P10636-8


    Entrez-Gene Id: 4137


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    For Research Use Only. Not For Use In Diagnostic Procedures.
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