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Recombinant human tag-free Tau-441 was co-expressed with PKAc alpha in E. coli cells. The Tau-441 protein was phosphorylated by PKAc alpha in vivo and in vitro prior to the final chromatography purification.
Catalog No. T08-50LN
| Catalog No. | Pack Size | Price (USD) | |
|---|---|---|---|
| T08-50LN-20 | 20 ug | $215 | |
| T08-50LN-50 | 50 ug | $435 | |
| T08-50LN-BULK | BULK | Contact Us |
Overview:
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, (2N4R), Tau-4, MAPT, MSTD; PPND; DDPAC; MAPTL; MTBT1; MTBT2; FTDP-17; FLJ31424; MGC138549
Genbank Number:
References:
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
Purity:
SDS-PAGE image of purified Tau Proteins. Lane 1, Tau-441, PKA-phosphorylated. Lane 2, Tau-441 Protein, Cat. # T08-54N.
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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 kDa
Fukuda Koichi et al., The Pseudoactive Site of ILK Is Essential for Its Binding to ?-Parvin and Localization to Focal Adhesions Molecular Cell December 2009 10.1016/j.molcel.2009.11.028
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
GiovannaDi Nardo,AndreaBandino,InesBarone RobertaBaravalle et al., Impact of R264C and R264H polymorphisms in human aromatase function J Steroid Biochem Mol Biol.? October 2001 10.1016/j.jsbmb.2016.09.022
Yamaguchi Fuminori et al., S100 Proteins Modulate Protein Phosphatase 5 FunctionA LINK BETWEEN CA2+ SIGNAL TRANSDUCTION AND PROTEIN DEPHOSPHORYLATION Journal of Biological Chemistry April 2012 10.1074/jbc.M111.329771
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
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
R Baravalle et al., Impact of R264C and R264H polymorphisms in human aromatase function. Journal of Steroid Biochemistry and Molecular Biology October 2016 10.1016/j.jsbmb.2016.09.022
Martic? Sanela et al., Electrochemical investigations into Tau protein phosphorylations Analyst March 2012 10.1039/c2an35097a
J. Coultrap Steven et al., Improving a Natural CaMKII Inhibitor by Random and Rational Design PLoS One October 2011 10.1371/journal.pone.0025245
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
Bhandaria Deepali et al., Cyclin-dependent kinase 5 activates guanine nucleotide exchange factor GIV/Girdin to orchestrate migration?proliferation dichotomy PNAS July 2015 10.1073/pnas.1514157112
Invasion/Metastasis, Neurobiology, p38 Pathway
Tau-441, BRSK1-phosphorylated, T08-50N
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Tau-441 Protein, T08-54N
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