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Thioflavin T acid

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Physical properties
Molecular weight496.55
SolventDMSO
Spectral properties
Absorbance (nm)199
Excitation (nm)349
Emission (nm)454
Storage, safety and handling
H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22
StorageFreeze (< -15 °C); Minimize light exposure
UNSPSC12352200

OverviewpdfSDSpdfProtocol


Molecular weight
496.55
Absorbance (nm)
199
Excitation (nm)
349
Emission (nm)
454
Thioflavin T (ThT), also called Basic Yellow 1 or CI 49005, is a benzothiazole salt. The dye is used to visualize plaques composed of beta-amyloid found in the brains of Alzheimer's disease patients. When it binds to beta sheets, such as those in amyloid oligomers, the dye undergoes a characteristic 120 nm red shift of its excitation spectrum that may be selectively excited at 450 nm, resulting in a fluorescence signal at 482 nm. ThT binds rapidly and specifically to the anti-parallel beta-sheet fibrils formed from synthetic beta-amyloid (1-40), but does not bind to monomer or oligomeric intermediates. The binding of ThT does not interfere with the aggregation of beta-amyloid peptide into amyloid fibrils. Thioflavin T acid is a valuble tool for making various bioconjugates of Thioflavin T that can direct Thioflavin T to a desired target. It is an essential reagent to make the peptides and other conjugates of Thioflavin T.

Calculators


Common stock solution preparation

Table 1. Volume of DMSO needed to reconstitute specific mass of Thioflavin T acid to given concentration. Note that volume is only for preparing stock solution. Refer to sample experimental protocol for appropriate experimental/physiological buffers.

0.1 mg0.5 mg1 mg5 mg10 mg
1 mM201.39 µL1.007 mL2.014 mL10.069 mL20.139 mL
5 mM40.278 µL201.39 µL402.779 µL2.014 mL4.028 mL
10 mM20.139 µL100.695 µL201.39 µL1.007 mL2.014 mL

Molarity calculator

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Spectrum


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spectrum

Spectral properties

Absorbance (nm)199
Excitation (nm)349
Emission (nm)454

Images


Citations


View all 9 citations: Citation Explorer
Human Telomeric Hybrid-2-over-Hybrid-1 G-quadruplex Targeting and a Selective Hypersaline-Tolerant Sensor Using Abasic Site-Engineered Monomorphism
Authors: Wu, Tao and Ye, Meiyun and Mao, Tianyi and Lin, Fan and Hu, Yuehua and Gan, Ning and Shao, Yong
Journal: Analytica Chimica Acta (2017)
Fluorescent dyes in the context of DNA-binding: The case of Thioflavin T
Authors: Biancardi, Aless and ro , undefined and Biver, Tarita and Mennucci, Benedetta
Journal: International Journal of Quantum Chemistry (2017)
Thioflavin T as a fluorescence probe for monitoring RNA metabolism at molecular and cellular levels
Authors: Sugimoto, Shinya and Arita-Morioka, Ken-ichi and Mizunoe, Yoshimitsu and Yamanaka, Kunitoshi and Ogura, Teru
Journal: Nucleic acids research (2015): gkv338
Determinants of amyloid fibril degradation by the PDZ protease HTRA1
Authors: Poepsel, Simon and Sprengel, Andreas and Sacca, Barbara and Kaschani, Farnusch and Kaiser, Markus and Gatsogiannis, Christos and Raunser, Stefan and Clausen, Tim and Ehrmann, Michael
Journal: Nature chemical biology (2015): 862--869
Mechanistic aspects of thioflavin-T self-aggregation and DNA binding: evidence for dimer attack on DNA grooves
Authors: Biancardi, A and Biver, T and Burgalassi, A and Mattonai, M and Secco, F and Venturini, M
Journal: Physical Chemistry Chemical Physics (2014): 20061--20072
Molecular rotor-based fluorescent probe for selective recognition of hybrid G-quadruplex and as a K+ sensor
Authors: Liu, Lingling and Shao, Yong and Peng, Jian and Huang, Chaobiao and Liu, Hua and Zhang, Lihua
Journal: Analytical chemistry (2014): 1622--1631
Ag nanoclusters as probes for turn-on fluorescence recognition of TpG dinucleotide with a high selectivity
Authors: Peng, Jian and Shao, Yong and Liu, Lingling and Zhang, Lihua and Liu, Hua and Wang, Ying
Journal: Analytica chimica acta (2014): 78--84
Selective recognition of ds-DNA cavities by a molecular rotor: switched fluorescence of thioflavin T
Authors: Liu, Lingling and Shao, Yong and Peng, Jian and Liu, Hua and Zhang, Lihua
Journal: Molecular BioSystems (2013): 2512--2519

References


View all 28 references: Citation Explorer
Methods for enhancing the accuracy and reproducibility of Congo red and thioflavin T assays
Authors: Eisert R, Felau L, Brown LR.
Journal: Anal Biochem (2006): 144
Lipophilic analogs of thioflavin S as novel amyloid-imaging agents
Authors: Wu C, Cai L, Wei J, Pike VW, Wang Y.
Journal: Curr Alzheimer Res (2006): 259
Oligo(ethylene glycol) derivatives of Thioflavin T as inhibitors of protein-amyloid interactions
Authors: Inbar P, Li CQ, Takayama SA, Bautista MR, Yang J.
Journal: Chembiochem (2006): 1563
Mechanism of thioflavin T accumulation inside cells overexpressing P-glycoprotein or multidrug resistance-associated protein: role of lipophilicity and positive charge
Authors: Darghal N, Garnier-Suillerot A, Salerno M.
Journal: Biochem Biophys Res Commun (2006): 623
Characteristics of the binding of thioflavin S to tau paired helical filaments
Authors: Santa-Maria I, Perez M, Hern and ez F, Avila J, Moreno FJ.
Journal: J Alzheimers Dis (2006): 279
Efficient radiosynthesis of carbon-11 labelled uncharged Thioflavin T derivatives using [11C]methyl triflate for beta-amyloid imaging in Alzheimer's Disease with PET
Authors: Solbach C, Uebele M, Reischl G, Machulla HJ.
Journal: Appl Radiat Isot (2005): 591
Chiral bias of amyloid fibrils revealed by the twisted conformation of Thioflavin T: an induced circular dichroism/DFT study
Authors: Dzwolak W, Pecul M.
Journal: FEBS Lett (2005): 6601
Development of novel amyloid imaging agents based upon thioflavin S
Authors: Wei J, Wu C, Lankin D, Gulrati A, Valyi-Nagy T, Cochran E, Pike VW, Kozikowski A, Wang Y.
Journal: Curr Alzheimer Res (2005): 109
The binding of thioflavin-T to amyloid fibrils: localisation and implications
Authors: Krebs MR, Bromley EH, Donald AM.
Journal: J Struct Biol (2005): 30
Mechanism of thioflavin T binding to amyloid fibrils
Authors: Khurana R, Coleman C, Ionescu-Zanetti C, Carter SA, Krishna V, Grover RK, Roy R, Singh S.
Journal: J Struct Biol (2005): 229