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.
Sample Purity Data. For specific information on a given lot, see related technical data sheet.
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.
Peng Z et al., A droplet reactor on a super-hydrophobic surface allows control and characterization of amyloid fibril growth Communications Biology September 2020 10.1038/s42003-020-01187-7
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
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
Kawakami Fumitaka et al., Stimulatory effect of α-synuclein on the tau-phosphorylation by GSK-3β FEBS Journal October 2011 10.1111/j.1742-4658.2011.08389.x
Coutadeur Severine et al., A novel DYRK1A (Dual specificity tyrosine phosphorylation-regulated kinase 1A) inhibitor for the treatment of Alzheimer's disease: effect on Tau and amyloid pathologies in vitro Journal of Neurochemistry May 2015 10.1111/jnc.13018
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
Kawakami Fumitaka et al., LRRK2 Phosphorylates Tubulin-Associated Tau but Not the Free Molecule: LRRK2-Mediated Regulation of the Tau-Tubulin Association and Neurite Outgrowth PLoS One January 2012 10.1371/journal.pone.0030834
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