Fluorometer Spectrofluorometer

A fluorometer, or spectrofluorometer, is an analytical instrument that measures fluorescence to identify and quantify chemical substances based on their light-emission properties. It illuminates a sample at a selected excitation wavelength, then detects emitted light at longer wavelengths; a spectrofluorometer uses monochromators to scan excitation or emission wavelengths and generate fluorescence spectra. In chemistry, these instruments support concentration measurements, molecular identification, reaction monitoring, and studies of photophysical behavior. Because fluorescence can provide high sensitivity and selectivity, fluorometric analysis is valuable for detecting trace compounds and characterizing interactions in solutions, materials, and biological or environmental samples.

Fluorometer Spectrofluorometer - Related Videos

Research

JoVE Journal - Biology

Measuring Photophysiology of Attached Stage of Colacium sp. by a Cuvette-Type Fast Repetition Rate Fluorometer

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Cited by 1 •

2021

Fast repetition rate fluorometer (FRRf) is a beneficial method for measuring photosystem II photophysiology and primary productivity. Here we describe a protocol to measure PSII photophysiology of epizoic alga, Colacium sp. on substrate zooplankton using cuvette-type FRRf.

G Protein-selective GPCR Conformations Measured Using FRET Sensors in a Live Cell Suspension Fluorometer Assay

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Cited by 4 •

2016

Simple methods to detect the selective activation of G proteins by G protein-coupled receptors remain an outstanding challenge in cell signaling. Here, Fӧrster resonance energy transfer (FRET) biosensors have been developed by pairwise tethering a GPCR to G protein peptides to probe conformational changes at controlled concentrations in live cells.

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features

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Cited by 1 •

2022

The study details the methodology of FRET mapping including the selection of labeling sites, choice of dyes, acquisition, and data analysis. This methodology is effective at determining binding sites, conformational changes, and dynamic motions in protein systems and is most useful if performed in conjunction with existing 3-D structural information.

Quantifying Bacterial Infection-Induced Amyloids Using Thioflavin T Fluorescence

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2025

Source: Balczon, R., et al. Methods for Detecting Cytotoxic Amyloids Following Infection of Pulmonary Endothelial Cells by Pseudomonas aeruginosa. J. Vis. Exp. (2018)This video demonstrates the protocol to quantify amyloids in culture supernatants from pulmonary endothelial cells infected with virulent bacteria, using thioflavin T, a fluorescent dye that binds to amyloid beta-sheet structures. An increase in fluorescence compared to baseline indicates the presence of amyloids in the culture...

Studying the Permeation of FITC and FITC-Ferritin through an In Vitro Blood-Brain Barrier Model

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2025

This video demonstrates a method to study permeation through an in vitro blood-brain barrier (BBB) model using astrocytes and endothelial cells on a membrane insert, with free FITC and FITC-loaded ferritin. FITC-ferritin bound to receptors on endothelial cells and crossed the membrane barrier to the lower chamber while free FITC showed restricted permeation and remained in the upper chamber.

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