Radioactive Ligand Detection
Radioactive Ligand Detection - Related Videos
05:13
Biolayer Interferometry Technology to Detect Interactions between Ligand and Analyte
0 Views •
2025
In this video, we demonstrate biolayer interferometry (BLI) technology to detect the intermolecular interactions between ligands and target analytes in real-time. BLI measures changes in the interference pattern of white light reflected off a layer of immobilized ligands on a biosensor surface as they interact with analytes in solution.
10:24
Detection of Ligand-activated G Protein-coupled Receptor Internalization by Confocal Microscopy
0 Views •
Cited by 2 •
2017
This protocol describes confocal microscopy detection of G protein-coupled receptor (GPCR) internalization in mammalian cells. It includes the basic cell culture, transfection, and confocal microscopy procedure and provides an efficient and easily interpretable method to detect the subcellular localization and internalization of fusion-expressed GPCR.
03:18
Radioactivity and Nuclear Equations
0 Views •
2020
Nuclear chemistry is the study of reactions that involve changes in nuclear structure. The nucleus of an atom is composed of protons and, except for hydrogen, neutrons. The number of protons in the nucleus is called the atomic number (Z) of the element, and the sum of the number of protons and the number of neutrons is the mass number (A). Atoms with the same atomic number but different mass numbers are isotopes of the same element. A nuclide of an element has a specific number of protons and...
17:38
Radioactive in situ Hybridization for Detecting Diverse Gene Expression Patterns in Tissue
0 Views •
Cited by 21 •
2012
This protocol is successfully used to quantitatively detect levels and spatial patterns of mRNA expression in multiple tissue types across vertebrate species. The method can detect low abundance transcripts and allows processing of hundreds of slides simultaneously. We present this protocol using expression profiling of avian embryonic brain formation as an example.
02:48
Radioactive Decay and Radiometric Dating
0 Views •
2020
Radioactivity is a spontaneous disintegration of an unstable nuclide and is a random process, as all the nuclei in the sample do not decay simultaneously. The number of disintegrations per unit time is called the activity (A), which is directly proportional to the number of nuclei in the sample. The decay constant (λ) is an average probability of decay per nucleus in unit time. The SI unit for activity is the becquerel, which is one disintegration per second. Another unit of activity is the...
FAQs
Radioactive labeling provides a detectable signal that distinguishes ligand molecules participating in the assay from those that do not. After the ligand interacts with its target, separating bound from unbound material allows the measured radiation to be assigned to the binding fraction. The resulting signal provides a basis for quantifying interactions and comparing binding under controlled conditions.
Competition assays test whether an unlabeled compound can reduce access of a radiolabeled ligand to the same binding site. A change in the measured bound signal indicates that the compounds compete for target access. This approach helps compare ligand specificity and identify compounds that interact with the same receptor, enzyme, transporter, or other target protein.
Time-dependent measurements can follow how rapidly a ligand associates with a target and how rapidly it dissociates. Association describes the development of binding, whereas dissociation describes the loss of bound ligand after conditions change. Tracking these processes adds a dynamic dimension to affinity measurements and helps characterize the behavior of protein-ligand interactions.
Binding results can provide information about both how strongly a ligand interacts with a target and how much target is present. Comparing measurements under controlled conditions helps separate these interpretations: affinity concerns the interaction itself, whereas receptor abundance concerns the quantity of available binding protein. This distinction supports more informative characterization of biochemical samples.
A typical workflow uses a radiolabeled ligand, exposes it to the selected target under controlled conditions, and then separates ligand bound to the target from unbound ligand. The separated material is measured with an appropriate radiation detector. Comparing the detected signal across conditions can reveal binding, competition, affinity, target abundance, or kinetic behavior.
The emitted radiation is measured with either a scintillation counter or a gamma counter, as specified for radioactive ligand detection. The instrument records the signal associated with the separated assay material, allowing samples or experimental conditions to be compared. Selecting the measurement approach is therefore part of converting ligand binding into interpretable biochemical data.
This method is useful when researchers need to characterize protein-ligand interactions, examine cellular signaling, or evaluate candidate compounds in drug screening. It can provide information about receptor abundance, ligand specificity, binding affinity, and association or dissociation kinetics. Competition experiments further support comparisons among unlabeled compounds that may access the same binding site.