Labeling-detection

Thioflavin T UltraPure Grade - 1 g

  • Cat.Number : AS-88306
  • Availability :
    In production

Quantity

The benzothiazole dye thioflavin T (ThT) is a classic amyloid stain for senile plaques containing βA4 peptide in Alzheimer's disease brain. ThT also binds rapidly and specifically to the anti-parallel β-sheet fibrils formed from synthetic β-amyloid (1-42), but does not bind to monomer or oligomeric intermediates. The fibrillar β-sheet-bound dye species 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 is a useful probe for the aggregated fibrillar state of β-amyloid (1-42) fibrils as the amyloid-specific fluorescence reports only fibrillar species. The binding of ThT does not interfere with the aggregation of this peptide into amyloid fibrils. The putative conformational changes detected by the ThT fluorescence suggest that small pharmacologic ligands can perturb and possibly dissociate Aβ amyloid fibrils.

Specifications

Chemistry
CAS registry number
  • 2390-54-7
Molecular Formula
  • C17H19ClN2S
Molecular Mass/ Weight
  • 318.9
Properties
Absorbance (nm)
  • 450
Emission (nm)
  • 482
Color
Quantity & Purity
Purity
  • Peak Area by HPLC ≥95%
Storage & stability
Form
  • Lyophilized
Resuspension condition
  • DMSO
Storage Conditions
  • -20°C Protected from Light
Activity
Application
Biomarker Target
Detection Method
Research Area
Sub-category Research Area
Usage
  • Research use

You may also be interested in the following product(s)

IMG-EN-AS-72216-01.jpg

AggreSure ß-Amyloid (1-42), human - 0.25 mg

Cat.Number : AS-72216
$330.00 Excl. Tax

Citations

Heterogeneous amylin fibril growth mechanisms imaged by total internal reflection fluorescence microscopy.

Biochemistry. . 2011 Mar 21 ; 50(14) 2808 | DOI : 10.1021/bi101908m

  • SM. Patil

Spectral properties and factors determining high quantum yield of thioflavin T incorporated in amyloid fibrils.

Spectroscopy . . 2009 Aug 28 ; 24 4 | DOI : 10.3233/SPE-2010-0418

  • A.I. Sulatskaya

Charge transfer process determines ultrafast excited state deactivation of thioflavin T in low-viscosity solvents.

J Phys Chem . 2010 Aug 19 ; 114(32) 8345 | DOI : 10.1021/jp105186z

  • V. Stsiapura

In vitro formation of amyloid from α-synuclein is dominated by reactions at hydrophobic interfaces.

J Am Chem Soc . 2010 Jul 21 ; 132(28) 9797 | DOI : 10.1021/ja102896h.

  • J. Pronchik

References

Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence

J Biol Chem . 2003 May 09 ; 278(19 16462 | DOI : 10.1074/jbc.C300049200

  • T. Ban
  • et al

IMPY: an improved thioflavin-T derivative for in vivo labeling of beta-amyloid plaques

Brain Res . 2002 Nov 29 ; 956(2) 202 | DOI : https://doi.org/10.1016/S0006-8993(02)03436-4

  • MP. Kung
  • et al

Thioflavin T Is a Fluorescent Probe of the Acetylcholinesterase Peripheral Site That Reveals Conformational Interactions between the Peripheral and Acylation Sites

J Biol Chem . 2001 Jun 29 ; 276(26) 23282 | DOI : https://doi.org/10.1074/jbc.M009596200

  • GV. De Ferrari
  • et al