Basic Considerations for Bioluminescence Resonance Energy Transfer (BRET) Assays…
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Download nowBasically, any protein that exerts any kind of action, effect or influence on another protein interacts with that protein. However, in the field of life sciences, the term protein-protein interaction (PPI) is used in a more specific way:
Protein-protein interactions can be classified in several ways (according to Acuner-Ozbabacan et al. 2011):
The majority of cellular processes are regulated by transient PPI, and thus a large part of the research on PPI concentrates on this type of interaction.
There are dozens of methods available to investigate PPI, and each has several advantages and disadvantages, e.g.
Due to the large numbers of false positives and negatives that most methods produce, it is usually necessary to confirm each interaction by using 2 or 3 different methods.
Most methods fall into one of 3 groups of methods: in silico, in vitro and in vivo. (Srinivasa Rao et al. 2013):
In silico methods use computer models to predict protein-protein interactions. They include sequence-based approaches, structure-based approaches, chromosome proximity, gene fusion, in silico 2 hybrid, mirror tree, phylogenetic tree, and gene expression-based approaches.
In vitro methods are performed in a controlled environment outside a living organism. In vitro methods used for PPI detection include tandem affinity purification, affinity chromatography, coimmunoprecipitation, protein arrays, protein fragment complementation, phage display, X-ray crystallography, and NMR spectroscopy. In some of them (for example, coimmunoprecipitation) interaction takes place in vivo, but the interaction is fixed and detected after the death of the cell or organism, and are hence sometimes labelled as ex vivo methods.
In vivo methods are performed in living cells or organisms. The great advantage of in vivo methods is that they preserve the native surroundings in which the interaction takes place. In addition, some of them, such as FRET, are reversible and can be used to quantify protein-protein interactions dynamically, which is highly advantageous. Follow the link below for more information about this type of methods.
Many of the in vivo methods mentioned above use either fluorescent or luminescent labels. Thus, instruments able to measure fluorescence and/or luminescence are required to use them. There are many different instruments that can be used to for this kind of measurements, including microplate readers, fluorescence microscopes, in vivo imaging systems, and others. Each instrument is different in terms of performance, flexibility, throughput, sample size and, most importantly, the techniques for protein-protein interaction studies they are able to perform. Follow the link below for more information about instruments for this application.
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Download nowBasic Considerations for Bioluminescence Resonance Energy Transfer (BRET) Assays…
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Download nowBioluminescence Resonance Energy Transfer (BRET)-based studies of receptor…
PDF | 334.9 KB
Download nowA Functional BRET Assay for 7TM Receptors Using the Mithras LB 940 Multimode…
PDF | 312.0 KB
Download nowBioluminescence Resonance Energy Transfer (BRET) as a means of monitoring…
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Download nowComparison of filter sets for BRET1 assays: ß-arrestin2 (ßARR2) recruitment to…
PDF | 187.6 KB
Download nowFRET as a Tool to Study G-protein Coupled Receptor Oligomerization in HEK Cells.
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PDF | 312.6 KB
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Download nowPromega NanoBRET™ protein:protein interaction system with the MITHRAS² Multimode…
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Download nowPromega NanoBRET™ protein:protein interaction system with the TriStar² S…
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