Monitoring the prevention of amyloid fibril formation by α-crystallin by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0450-WXH)

Introduction

The molecular chaperone, α-crystallin, has the ability to prevent the fibrillar aggregation of proteins implicated in human diseases, for example, amyloid β peptide and α-synuclein. α-Crystallin is a molecular chaperone of the small heat-shock protein (sHsp) family. It is known to recognize and interact with long-lived partially folded proteins on their off-folding pathway to prevent their aggregation. Two closely related subunits of α-crystallin exist in high concentrations in mammalian lenses, αA- and αB-crystallin; in humans they are present in a ratio of 3 : 1. Whereas αA-crystallin is lens specific, αB-crystallin is also found extralenticularly in retina, heart, skeletal muscle, skin, kidney, brain, spinal cord and lungs, as well as in CNS glial cells and neurons in some pathological conditions, e.g. Alzheimer's disease and dementia with Lewy bodies.

Add to Cart Please Inquire

Principle Applications Procedure Materials Notes Related Products

Principle

Dual polarization interferometry (DPI) is an analytical technique that allows the simultaneous determination of thickness, density, and mass of a biological layer on a sensing waveguide surface in real time. DPI focuses laser light into two waveguides. One of these functions as the "sensing" waveguide having an exposed surface while the second one functions to maintain a reference beam. A two-dimensional interference pattern is formed in the far field by combining the light passing through the two waveguides. The DPI technique rotates the polarization of the laser, to alternately excite two polarization modes of the waveguides. Measurement of the interferogram for both polarizations allows both the refractive index and the thickness of the adsorbed layer to be calculated. These measurements can be used to infer conformational information about the molecular interactions taking place, as the molecule size (from the layer thickness) and the fold density (from the RI) change.

Applications

Study the ability to prevent the fibrillar aggregation of proteins by α-crystallin.
Treatment research.
Drug discovery.

Procedure

1. Setting of dual polarization interferometry
2. Preparing the DPI sensor chip
3. Immobilization of target on DPI biosensor
4. Reagent was injected to react
5. Quantitative analysis

Materials

• DPI biosensor
• DPI sensor chip

Other recommended products

Conformational Detection of Acyl carrier protein (ACP) by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0386-WXH)
Effects of Alpha-tocopherol transfer protein (α-TTP) on membranes by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0422-WXH)
Characterisation of polygalacturonic acid-based layer-by-layer deposited films by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0456-WXH)
Real-Time Analysis of Specific Binding between Apolipoprotein E Isoforms and Amyloid beta-Peptide by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0467-WXH)
Assessment of activity of antigens (allergens) immobilised on sensor chips by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0408-WXH)
Real-time Measurement of protein structure (d-biotin interactions with streptavidin) by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0379-WXH)
Study of immobilization of Enamel Matrix Derivate Protein onto Polypeptide Multilayers by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0457-WXH)
Orientation and characterization of immobilized antibodies for improved immunoassays by Dual polarization interferometry (DPI) (CAT#: STEM-MB-0468-WXH)