Assay-kits

SensoLyte® Thioflavin T ß-Amyloid (1-42) Aggregation Kit - 1 kit

485.00
Check your price
  • Cat.Number : AS-72214
  • Availability :
    In stock
  • Shipping conditions : Ice delivery fees must be applied

Alternative choices

Quantity

The SensoLyte® ThT β-Amyloid (1-42) Aggregation kit provides a convenient and standard method to measure Aβ42 aggregation using Thioflavin T dye. Aβ42 peptide is pretreated to ensure it is in a monomeric state. An optimized fibrillation buffer is included with the kit, and two known inhibitors are supplied as controls. The assay is based on the property of ThT dye in which fluorescence (Ex/Em=440/484 nm) is increased when bound to aggregated Aβ peptides. Alzheimer's disease (AD), the most common cause of dementia, is characterized by the presence of senile plaques and neurofibrillary tangles, surrounded by damaged neurons. Beta-Amyloid (Aβ) peptides, Aβ40 (1-40) and Aβ42 (1-42), were found to be a major component of the above plaques. Many studies suggest that these peptides can form toxic oligomers and fibrils under physiological conditions and rapidly aggregate. Since Aβ aggregation is evidently an essential event in the pathogenesis of AD, a reliable assay is important to study Aβ fibrillation kinetics and screen for Aβ aggregation inhibitors.

Specifications

Packaging
Kits components
  • Component A: Assay Buffer: 25 ml Component B: Beta-Amyloid (1-42) (Aß42), human: 0.5 mg (2 x 0.25 mg, net peptide) Component C: Thioflavin T (ThT): 20 mM, 100 µl Component D: Morin: 20 mM, 25 µl Component E: Phenol Red: 20 mM, 25 µl
Chemistry
UniProt number
  • P05067
Properties
Absorbance (nm)
  • 440
Emission (nm)
  • 484
Storage & stability
Storage Conditions
  • Store kit components at 4°C. Components B,D and E should be stored at -20°C if not used within one week.
Activity
Application
Biomarker Target
Detection Method
Research Area
Sub-category Research Area
Usage
  • Research use
Codes
Code Nacres
  • NA.32

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

Tube of AggreSure Beta-Amyloid (1-42), human - 0.25 mg

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

Cat.Number : AS-72216
250.00 Excl. Tax
Tube of Beta-Amyloid (1-42) peptide

Beta-Amyloid (1-42)

Cat.Number : AS-20276
271.00 Excl. Tax
Image of a kit SensoLyte 520 Neprilysin Activity Assay Kit Fluorimetric

SensoLyte® 520 Neprilysin Activity Assay Kit Fluorimetric - 1 kit

Cat.Number : AS-72223
485.00 Excl. Tax

Citations

The Monofunctional Glycosyltransferase of Escherichia coli Localizes to the Cell Division Site and Interacts with Penicillin-Binding Protein 3, FtsW, and FtsN

J Bacteriol . 2018 Dec 31 ; 190(5) 1831-4 | DOI : PMC225871

  • Adeline Derouaux

Supratherapeutic concentrations of cilostazol inhibits β-amyloid oligomerization in vitro

Neurosci lett . 2018 Apr 21 ; 677 19-25 | DOI : 10.1016/j.neulet.2018.04.032

  • H. Shozawa
  • et al

Do amyloid structures formed by Staphylococcus aureus phenol-soluble modulins have a biological function?

Int J Med Microbiol . 2017 Sep 01 ; 308(6) 675-682 | DOI : 10.1016/j.ijmm.2017.08.010

  • Y. Zheng
  • et al

Neuroprotective Effect of Corydalis ternata Extract and Its Phytochemical Quantitative Analysis

Chem Pharm Bull . 2017 Jan 01 ; 65(9) 826-832 | DOI : 10.1248/cpb.c17-00300

  • Y.J. Kim
  • et al

Novel Curcumin loaded nanoparticles engineered for Blood-Brain Barrier crossing and able to disrupt Abeta aggregates

Int J Pharm . 2017 May 08 ; 526(1-2) 413-424 | DOI : 10.1016/j.ijpharm.2017.05.015

  • R. Barbara
  • et al

Microtubule modification influences cellular response to amyloid-β exposure

AIMS Biophysics . 2016 Jan 01 ; 3(2) 261-285 | DOI :  https://doi.org/10.3934/biophy.2016.2.261

  • N. Shamitko-Klingensmith
  • et al

γ-Lactam alkaloids from the flower buds of daylily

J Natur med . 2016 Feb 05 ; 70(3) 376-383 | DOI : 10.1007/s11418-015-0963-z

  • T. Matsumoto
  • et al

References

Chemical structures of constituents from the whole plant of Bacopa monniera

J Natur med . 2016 Mar 24 ; 70(3) 404-411 | DOI : 10.1007/s11418-016-0986-0

  • T. Ohta
  • et al