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Tau-441, GSK3beta-phosphorylated

Recombinant human tag-free Tau-441 was co-expressed with GSK3beta in E. coli cells. The Tau-441 protein was phosphorylated by GSK3beta in vivo and in vitro prior to the final chromatography purification.
Catalog No. T08-50FN

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T08-50FN-20 20 ug $215
T08-50FN-50 50 ug $435
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Tau-441 or Tau-F is a member of the Tau family of proteins which function to stabilize the microtubules by binding to them. Tau proteins are subject to phosphorylation and this phenomenon regulates the association of the Tau protein with the microtubules (1). Deposits of Alzheimer's disease AD-associated proteins, such as hyperphosphorylated Tau, as well as other shared misfolded proteins, such as, beta-amyloid precursor protein (betaAPP), ubiquitin, and various chaperones and protein kinases are thought to play a pathologic role in the cognitive decline and muscular failure. Malfunctioning of Tau proteins is associated with microtubules disintegration and collapsing of the neuronal transport system (2).

Gene Aliases:

Tau-F, (N2R4), Tau-4, MAPT, MSTD, PPND, DDPAC, MAPTL, MTBT1, MTBT2, FTDP-17, FLJ31424, MGC138549

Genbank Number:


1. Zilka, N., et al. Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo. FEBS Lett. 2006; 508: 3582-3588.

2. Rial, A. et al: Calcium Dyshomeostasis in beta-Amyloid and Tau-bearing Skeletal Myotubes. J. Biol. Chem., 2004; 279: 3524-53532


SDS-PAGE image of purified Tau Proteins. Lane 1, Tau-441, GSK3beta -phosphorylated. Lane 2, Tau-441 Protein, Cat. # T08-54N.

Tau Proteins:

Representation of seven Tau proteins, from top to bottom: Tau-441, Tau-410, Tau-412, Tau-381, Tau-383, Tau-352 and Tau-316 (Tau Protein Marker; Cat # T08-07N).

Storage, Stability and Shipping:

Store product at –70oC. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.

Molecular Weight:

~64-68 kDa

 Ishizuka Koko et al., DISC1-dependent switch from progenitor proliferation to migration in the developing cortex Nature April 2011 10.1038/nature09859

 Wang K et al., Identification and characterization of DNA aptamers specific for phosphorylation epitopes of Tau protein Journal of American Chemical Society October 2018 10.1021/jacs.8b08645

 SH Lee et al., Antibody-Mediated Targeting of Tau In Vivo Does Not Require Effector Function and Microglial Engagement. Cell Reports August 2016 10.1016/j.celrep.2016.06.099

 A Chakraborty et al., Inositol hexakisphosphate kinase-1 regulates behavioral responses via GSK3 signaling pathways. Molecular Psychiatry March 2014 10.1038/mp.2013.21

 I Pronobis Mira et al., A novel GSK3-regulated APC:Axin interaction regulates Wnt signaling by driving a catalytic cycle of efficient ?catenin destruction Elife September 2015 10.7554/eLife.08022

 Absalon Sabrina et al., MiR-26b, Upregulated in Alzheimer's Disease, Activates Cell Cycle Entry, Tau-Phosphorylation, and Apoptosis in Postmitotic Neurons Journal of Neuroscience September 2013 10.1523/JNEUROSCI.1327-13.2013

 Richard Rubenstein et al., A novel, ultrasensitive assay for tau: potential for assessing traumatic brain injury in tissues and biofluids Journal of Neurotrauma March 2016 10.1089/neu.2014.3548

 JN Kong et al., Regulation of Chlamydomonas flagella and ependymal cell motile cilia by ceramide-mediated translocation of GSK3. Molecular Biology of the Cell December 2015 10.1091/mbc.E15-06-0371

 Kawakami Fumitaka et al., Leucine-rich repeat kinase 2 regulates tau phosphorylation through direct activation of glycogen synthase kinase-3β FEBS Journal November 2013 10.1111/febs.12579

 D Xu et al., Obg-like ATPase 1 regulates global protein serine/threonine phosphorylation in cancer cells by suppressing the GSK3β-inhibitor 2-PP1 positive feedback loop. Oncotarget January 2016 10.18632/oncotarget.6496

 Douglass Jacqueline et al., Identifying Protein Kinase Target Preferences Using Mass Spectrometry American Journal of Physiology - Cell Physiology June 2012 10.1152/ajpcell.00166.2012

 CJ Dunning et al., Direct High Affinity Interaction between Aβ42 and GSK3α Stimulates Hyperphosphorylation of Tau. A New Molecular Link in Alzheimer's Disease? ACS Chemical Neuroscience February 2016 10.1021/acschemneuro.5b00262

 Martic Sanela et al., Electrochemical Investigations of Tau Protein Phosphorylations and Interactions with Pin1 Chemistry & Biodiversity September 2012 10.1002/cbdv.201100418

 Martic? Sanela et al., Electrochemical investigations into Tau protein phosphorylations Analyst March 2012 10.1039/c2an35097a

 Frost Danielle et al., β-Carboline Compounds, Including Harmine, Inhibit DYRK1A and Tau Phosphorylation at Multiple Alzheimer's Disease-Related Sites PLoS One May 2011 10.1371/journal.pone.0019264

 Gao Feng et al., The Roles of GSK-3? and APC in Cytoplasmic Dynein Regulation Thesis PhD; University of South Carolina December 2014 10.1038/35041020


Invasion/Metastasis, Neurobiology, p38 Pathway


  Tau-381 Protein, T04-54N

  Tau-441, PHKG2-phosphorylated, T08-50KN

  Tau-441, PKA-phosphorylated, T08-50LN

  Tau-412, GSK3beta-phosphorylated, T07-50CN



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