Recombinant human tag-free Tau-441 was co-expressed with TTBK1 in E. coli cells. The Tau-441 was phosphorylated by TTBK1 in vivo and in vitro prior to the final chromatography purification.
Catalog No. T08-50ON
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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, β-amyloid precursor protein (βAPP), 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).
Tau-F, (N2R4), Tau-4, MAPT, MSTD, PPND, DDPAC, MAPTL, MTBT1, MTBT2, FTDP-17, FLJ31424, MGC138549
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 β-Amyloid and Tau-bearing Skeletal Myotubes. J. Biol. Chem., 2004; 279: 3524-53532
SDS-PAGE image of purified Tau Proteins. Lane 1, Tau-441, TTBK1-phosphorylated. Lane 2, Tau-441 Protein, Cat. # T08-54N.
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.
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
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F. Liachko Nicole et al., CDC7 inhibition blocks pathological TDP-43 phosphorylation and neurodegeneration Annals of Neurology February 2013 10.1002/ana.23870
F. Liachko Nicole et al., The Tau Tubulin Kinases TTBK1/2 Promote Accumulation of Pathological TDP-43 PLoS Genetics December 2014 10.1371/journal.pgen.1004803
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
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
R Rubenstein et al., A Novel, Ultrasensitive Assay for Tau: Potential for Assessing Traumatic Brain Injury in Tissues and Biofluids Journal of Neurotrauma March 2015 10.1089/neu.2014.3548
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
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
Invasion/Metastasis, Neurobiology, p38 Pathway