Product overview

Name Thioflavin T (ThT)
Biological description

Cell-permeable fluorescent amyloid stain for in vitro amyloid beta staining in brain tissues. Used to detect amyloid fibrils and to study amyloid fibril structure and the mechanism by which they form. Stains insoluble senile Aβ plaques, confirms formation of β-sheet structure from mutant huntingtin exon-1 aggregates in vitro and may also be used to monitor polyglutamine amyloid formation of tNhtt-42Q aggregates in Huntington's diseases models in vitro.

Alternative names Thioflavin T
Purity >95%
Description

Cell-permeable fluorescent amyloid stain

Write Your Own Review
You're reviewing:Thioflavin T (ThT)
Rate this item:

Optical Data

Max excitation wavelength Switches from 385nm to 450nm when bound to amyloid beta fibrils
Max emission wavelength Switches from 445nm to 485nm when bound to amyloid beta fibrils

Solubility & Handling

Storage instructions -20°C
Solubility overview

Soluble in water (10 mM), and in DMSO (5 mM)

Important This product is for RESEARCH USE ONLY and is not intended for therapeutic or diagnostic use. Not for human or veterinary use

Calculators

Molarity

=
x
x
More Info

Dilution

x
=
x
More Info

Chemical Data

Purity >95%
Chemical name 2-[4-(Dimethylamino)phenyl]-3,6-dimethylbenzothiazolium chloride
Molecular Weight 318.9
Chemical structure  Chemical Structure
Molecular Formula C17H19ClN2S
CAS Number 2390-54-7
PubChem identifier 16853
SMILES CC1=CC2=C(C=C1)[N+](=C(S2)C3=CC=C(C=C3)N(C)C)C.[Cl-]
InChiKey JADVWWSKYZXRGX-UHFFFAOYSA-M
Appearance Yellow solid

References for Thioflavin T (ThT)

References are publications that support the biological activity of the product
  • Thioflavin T fluoresces as excimer in highly concentrated aqueous solutions and as monomer being incorporated in amyloid fibrils.

    Sulatskaya AI et al (2017) Scientific reports 7 : 2146
  • Mechanism of thioflavin T binding to amyloid fibrils.

    Khurana R et al (2005) Journal of structural biology 151 : 229-38
  • The binding of thioflavin-T to amyloid fibrils: localisation and implications.

    Krebs MR et al (2005) Journal of structural biology 149 : 30-7

3 Item(s)